CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_AP019735	Alistipes communis strain 5CBH24	17 crisprs	PD-DExK,WYL,RT,cas3,DEDDh	4	2	3	2

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_AP019735_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_1

31791-31909

Orphan

Consensus_repeat	Method
CCGCTTAGACAGGCGGCGCCTCGGCAAAATCGCAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_1

>merge|NZ_AP019735|1|31791-31909|CRISPRCasFinder
CCGCTTAGACAGGCGGCGCCTCGGCAAAATCGCAAGCTTCGCTTGCTTTTGCGCTCGGCTTGCACAACTTTGCGGGATTGCATCCCGCTTAGACAGGCGGCGCCTCGGCAAAATGCAAA

>NZ_AP019735|1|1|31791-31909|CRISPRCasFinder
CCGCTTAGACAGGCGGCGCCTCGGCAAAATCGCAA	GCTTCGCTTGCTTTTGCGCTCGGCTTGCACAACTTTGCGGGATTGCATC
CCGCTTAGACAGGCGGCGCCTCGGCAAAATGCAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141413514.1\|26147_26708_-\|DUF4251-domain-containing-protein	unknown	unknown	gnl\|CDD\|372897
NZ_AP019735.1\|WP_026074670.1\|35060_35693_+\|outer-membrane-beta-barrel-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_026074672.1\|30386_30740_-\|aspartate-1-decarboxylase	unknown	unknown	gnl\|CDD\|376751
NZ_AP019735.1\|WP_019129238.1\|29821_30334_-\|DUF456-domain-containing-protein	unknown	unknown	gnl\|CDD\|377293
NZ_AP019735.1\|WP_019129230.1\|35763_36804_-\|glycerophosphodiester-phosphodiesterase-family-protein	unknown	unknown	gnl\|CDD\|176509
NZ_AP019735.1\|WP_141413515.1\|31997_33995_+\|dihydrofolate-reductase	unknown	unknown	gnl\|CDD\|367566
NZ_AP019735.1\|WP_019129226.1\|40601_40862_-\|HPr-family-phosphocarrier-protein	unknown	unknown	gnl\|CDD\|224836
NZ_AP019735.1\|WP_141411780.1\|30753_31590_-\|pantoate--beta-alanine-ligase	unknown	unknown	gnl\|CDD\|376824
NZ_AP019735.1\|WP_141413517.1\|38906_40568_-\|phosphoenolpyruvate--protein-phosphotransferase	unknown	unknown	gnl\|CDD\|224006
NZ_AP019735.1\|WP_034779249.1\|34391_35048_+\|DUF4136-domain-containing-protein	unknown	unknown	gnl\|CDD\|379281
NZ_AP019735.1\|WP_019129241.1\|25847_26015_+\|4Fe-4S-binding-protein	unknown	unknown	gnl\|CDD\|274983
NZ_AP019735.1\|WP_141411778.1\|22193_23834_-\|fimbrillin-family-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141411777.1\|21942_22140_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141411779.1\|26896_29800_-\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_AP019735.1\|WP_019129242.1\|24532_25804_+\|serine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235461
NZ_AP019735.1\|WP_162852307.1\|38014_38863_-\|prolyl-oligopeptidase-family-serine-peptidase	unknown	unknown	gnl\|CDD\|223730
NZ_AP019735.1\|WP_141411781.1\|36819_37977_-\|mannitol-1-phosphate-5-dehydrogenase	unknown	unknown	gnl\|CDD\|235031
NZ_AP019735.1\|WP_141411782.1\|40865_42713_-\|PTS-mannitol-transporter-subunit-IICBA	unknown	unknown	gnl\|CDD\|237905
NZ_AP019735.1\|WP_141411783.1\|43309_44533_+\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|271185
NZ_AP019735.1\|WP_019129243.1\|23884_24025_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141413514.1\|26147_26708_-\|DUF4251-domain-containing-protein	gnl\|CDD\|372897	pfam14059, DUF4251, Domain of unknown function (DUF4251). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 164 and 196 amino acids in length.	5.16211e-34
NZ_AP019735.1\|WP_026074672.1\|30386_30740_-\|aspartate-1-decarboxylase	gnl\|CDD\|376751	pfam02261, Asp_decarbox, Aspartate decarboxylase. Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalyzed by the enzyme aspartate decarboxylase EC:4.1.1.11 which requires a pyruvoyl group for its activity. It is synthesized initially as a proenzyme which is then proteolytically cleaved to an alpha (C-terminal) and beta (N-terminal) subunit and a pyruvoyl group. This family contains both chains of aspartate decarboxylase.	2.70849e-74
NZ_AP019735.1\|WP_019129238.1\|29821_30334_-\|DUF456-domain-containing-protein	gnl\|CDD\|377293	pfam04306, DUF456, Protein of unknown function (DUF456). This family is a putative membrane protein that contains glycine zipper motifs.	5.48336e-21
NZ_AP019735.1\|WP_141413515.1\|31997_33995_+\|dihydrofolate-reductase	gnl\|CDD\|367566	pfam03571, Peptidase_M49, Peptidase family M49.	8.41199e-37
NZ_AP019735.1\|WP_019129226.1\|40601_40862_-\|HPr-family-phosphocarrier-protein	gnl\|CDD\|224836	COG1925, FruB, Phosphotransferase system, HPr-related proteins [Carbohydrate transport and metabolism].	1.89266e-21
NZ_AP019735.1\|WP_141411780.1\|30753_31590_-\|pantoate--beta-alanine-ligase	gnl\|CDD\|376824	pfam02569, Pantoate_ligase, Pantoate-beta-alanine ligase. Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.	4.23974e-133
NZ_AP019735.1\|WP_141413517.1\|38906_40568_-\|phosphoenolpyruvate--protein-phosphotransferase	gnl\|CDD\|224006	COG1080, PtsA, Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism].	0
NZ_AP019735.1\|WP_034779249.1\|34391_35048_+\|DUF4136-domain-containing-protein	gnl\|CDD\|379281	pfam13590, DUF4136, Domain of unknown function (DUF4136). This domain is found in bacterial lipoproteins. The function is not known.	2.10217e-27
NZ_AP019735.1\|WP_019129241.1\|25847_26015_+\|4Fe-4S-binding-protein	gnl\|CDD\|274983	TIGR04105, hypothetical_protein, [FeFe] hydrogenase, group B1/B3. See for descriptions of different groups.	5.7891e-09
NZ_AP019735.1\|WP_141411779.1\|26896_29800_-\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	7.67119e-51
NZ_AP019735.1\|WP_019129242.1\|24532_25804_+\|serine--tRNA-ligase	gnl\|CDD\|235461	PRK05431, PRK05431, seryl-tRNA synthetase; Provisional.	0
NZ_AP019735.1\|WP_162852307.1\|38014_38863_-\|prolyl-oligopeptidase-family-serine-peptidase	gnl\|CDD\|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	3.08595e-25
NZ_AP019735.1\|WP_141411781.1\|36819_37977_-\|mannitol-1-phosphate-5-dehydrogenase	gnl\|CDD\|235031	PRK02318, PRK02318, mannitol-1-phosphate 5-dehydrogenase; Provisional.	0
NZ_AP019735.1\|WP_141411782.1\|40865_42713_-\|PTS-mannitol-transporter-subunit-IICBA	gnl\|CDD\|237905	PRK15083, PRK15083, PTS system mannitol-specific transporter subunit IICBA; Provisional.	0
NZ_AP019735.1\|WP_141411783.1\|43309_44533_+\|tyrosine-type-recombinase/integrase	gnl\|CDD\|271185	cd01185, INTN1_C_like, Integrase IntN1 of Bacteroides mobilizable transposon NBU1 and similar proteins, C-terminal catalytic domain. IntN1 is a tyrosine recombinase for the integration and excision of Bacteroides mobilizable transposon NBU1 from the host chromosome. IntN1 does not require strict homology between the recombining sites seen with other tyrosine recombinases. This family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	2.71644e-58
NZ_AP019735.1\|WP_019129230.1\|35763_36804_-\|glycerophosphodiester-phosphodiesterase-family-protein	gnl\|CDD\|176509	cd08566, GDPD_AtGDE_like, Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (AtGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homolgoues. Members in this family shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. AtGDE exists as a hexamer that is a trimer of dimers, which is unique among current known GDPD family members. However, it remains unclear if the hexamer plays a physiological role in AtGDE enzymatic function.	1.56567e-48

>NZ_AP019735.1|WP_141411780.1|30753_31590_-|pantoate--beta-alanine-ligase
MKTVTSVKALREVLSAVDSTGIGLVPTMGALHAGHRSLVERARRENATVVVSVFVNPTQFNDKNDLRNYPRTPEADCALLEAAGADVVFMPSVEEMYPVPDLRQYDFGRIDKVMEGATRPGHFNGVAQVVSKLFAMVQPARAYFGEKDFQQIAVVKSMVAQSGFPLEIVECGIVRGDDGLALSSRNALLDAAHRAAAPDICRALRLGAERAAGMTPAELADFVTRETERSGLLEVIYFQSVDALTMQQVAAWDESERIQGCIAVQAGAVRLIDNIRIK
>NZ_AP019735.1|WP_026074672.1|30386_30740_-|aspartate-1-decarboxylase
MQIEVLKSKIHRVTITEANLNYVGSITIDEELMEAANLIEGERVQIWNVTNGERLDTYVIRGRRGSGAICLNGAAARKAQVGDVLIIASYARMEFEEAKTFRPWVVFPDTATNRLVE
>NZ_AP019735.1|WP_019129238.1|29821_30334_-|DUF456-domain-containing-protein
MDVFLSITAFLCCLVGIVGCIVPVLPGPVLSYAGLFCAYACSYSTLTPAEMWLWAGLTAAVTAADYFLPGYMAKLFGGTRAGMVGATVGMIAGLFVGGLIGIVVGPFVGAVAGELLNDRERIGQALVVGVGSFLSFLVGTGIKLVAAVGMLTFVVADTWPALRAWFATVF
>NZ_AP019735.1|WP_141411779.1|26896_29800_-|insulinase-family-protein
MKRVFLLVAAAVLSLVVTSCSKYRYEEVADDPLHSRIYTLDNGLKVYMTVNGEAPRIQTYIAVRVGSKNDPLETTGLAHYFEHLMFKGTKSFGTQDYEAERPMLDEIERLFEVYRTTTDADERRAIYARIDSVSQEASKLAIPNEYDKLMSAIGAAGTNAFTSYDMTVYTEEIPSNQIDNWAKIQSDRFANAVIRGFHTELETVYEEYNMSLTSDSRKMLDSLMVALYPHHPYGMHTVLGTQEDLKNPSITNIKNYYKTYYVPNNMAICLSGDFDPDRMIATIDKYFGGLKPNPELPEWSFTPEPAMTAPVEKTVLGQEAEMIYLGWRTGGASSEDADMIQLVSSLLSNGKCGLLDVDIQQQQKMLGVGAEGLQLADYGMMVAIGYPKPGQTLEEARDMLLDEIGKLRAGDFDEELLASTIANYKRGEMQALEENGNRAMAYVDAFINGVDWKRSVEELDRLSKVTKADVVAWANEKLDPEVYAAVYKRQGVDPNIHKIDKPQITPIATNRDKSSEFLAAIQAAEVEAVQPVFVDYASDLSVGKMKQDIEVLYKQNTTNGLFSLYYVYDFGTTTDPAFGIASDYFDLLGTDTQSLQEIQREFYDLACSFGIHAGGERIYVTISGLAENMDKAVKLAEEYMQNVEGDDAVLAQLKANAMKARNDAKLNQNANFRALQQYTFYGPEAIRARTLTDEQLMALTSDELLARIRSLSDYEHYVMYYGPETEAKLIAALDAIHRTSQELKPVRKVRFPLLTVDKSEVNVAQYDAKQIYYLQYSNRGEKFSTDNDPGETLFNSYFGGGMNAVVFQEMREARSLAYTAFATFTEMRDKDDPYIFYAFIATQNDKMRQAVEAFDEIIENMPESEKAFELAKQGILANLSTQRTVRDNVLWSFVSAREMGVGVDRNKAVYDAVQGMTLADVKAFHDKWVKGRKYTYSILGDRNDIDMDYLRTLGPVHEVSQRELFGY
>NZ_AP019735.1|WP_141413514.1|26147_26708_-|DUF4251-domain-containing-protein
MTLCLLAGVVNPARPQARRTRTQTEQTRSADRERAKREQAVADSLAHLKALRSLDRLDFALEADRLTLRRGRVVFVSSDTNFVTLSGDMATVQVAPFMGGGPNGIGGITLEGHASNIRVRTDKRGNTTFSMNVFGRGISATLSIRLPAGSNRASVSIDPNFSSDRIQLTGVLVPLDESRVFKGSAL
>NZ_AP019735.1|WP_019129241.1|25847_26015_+|4Fe-4S-binding-protein
MAYKITDACVACGTCIGECPVEAISAGDIYVIDADKCIDCGTCAGVCPSEAIIPE
>NZ_AP019735.1|WP_019129242.1|24532_25804_+|serine--tRNA-ligase
MLTLKQLRDDKEAAVRRLAKKGVDARPVIDRIEQLDDRRKAIQQELDNCLSQQNQAAKMIGALMGQGKRDEAEAKKAEVAALKEKSVKLSAEMKQTADALQAEIVLLPNFPAEIVPEGTSAEDNLVVKLVENYTPLPAEALPHWELAKKYDIIDFDLGVKLTGAGFPVYKGKGARLQRALINYFLDYNTRAGYQEVEPPVMVNEASGFGTGQLPDKEGQMYHATVDNFYLVPTAEVPVTNIFRDVILDEKDFPVKMTAYTPCFRREAGSYGKDVRGLNRLHQFDKVEIVRLSLPDDSYEALDDMVAHVEGLVKSLGLPYRILRLCGGDMSFTSALTYDFEVYSEAQKRWLEVSSVSNFESFQANRLKLRYRDANKKIHLAHTLNGSSLALPRIVAALLENNQTPEGIRIPEVLIPYTGFDIIK
>NZ_AP019735.1|WP_019129243.1|23884_24025_-|hypothetical-protein
MNYYQSEKEAYVVPRAIVFDVKVEEGFASSGEGEITPGEEDSEWGN
>NZ_AP019735.1|WP_141411778.1|22193_23834_-|fimbrillin-family-protein
MKRSFFALLAAAVSGLASCQQDGTQDDAALPMNVYSFDATTEGTRVSLDHTALTYTWDGSEQVMVWYAPATSAPDYDYTLIGNPFVAESAGAKTAFSLRTEYDLSEMGYDDQNYVLMYPWPYAGTSGVSGDEVTYTIGTREGDGYVQKDVFEGIYNLMRAETTGSSLLVGRPPVTFEHLLTSLRFYVKESAEPAFDDIRITDMEILFPENVIGETKVNFREGYVASASSRKVIVDLDAPLTPQKSYKDESGEANDDQYALVVVKPFTLKANTDGNANDRILVTLRGTGTDIHTGEAERITQTLVLTSDSDMEFEAGHFRAVSLQLENDWTPVDVQLTEAFAPAGDYAHGAGIMFDKRGECFGFHASIKDAADKERMIVLDNTSNRWSLGTSWLYAQSAFYMPSSTVLKGYTQGDIAVTFDAHVVFSGKDKNPCPIIIGFNHCSTRTNGDTGDGGFVALASVDAEPALMTAKEAKENGGYPEDAAYWRSYEVVIPAETIAGIDQFMEPNKDGSAAHMGFKLDGQVGASSSKGRMVYIKNICFSYENK
>NZ_AP019735.1|WP_141411777.1|21942_22140_-|hypothetical-protein
MMKPILNDGCDSLPCRPLDCYVPPCLTNLAVAAERGFAASYFDDEDEFVSDGFDDGGAPDLSDWD
>NZ_AP019735.1|WP_141413515.1|31997_33995_+|dihydrofolate-reductase
MTTSVACLGSCTNPAASDAQQPWIVDRFDDIKVIRYEVPGFERLPLEQKELIYYLAEAAKCGRDILFDQNCAANLPIRRTLETLYLNYKGDRTSDEWKALEKYLKKVWFANGIHHHYSNDKFRPEFSESFFREAAASVGMDRFPADFDFLCKVIFDPAIYPTRLNQAAGADMLWTSASNYYSNVRQHEAEQFYAAMAAADAGDPCPVSYGLNSQLVKEEKTGRLYERMWKVGGMYSPAIERIVYWLEKARDVAAEPQKQTLAALIDYYRTGDLKQFDRYNILWLQDTVSNVDFVNGFIETYGDPLGYKASWEANVNFVDSAACRRTRIISENAQWFEDHSPVDPAYKKKVVKGVSAKVITVAMLGGDCYPATPIGINLPNADWIRKEHGSKSVTIDNITYAYDRAAHGNGFEEEFMLRPEDRERIDKYGKIGDDLHTDLHECLGHGSGQLAPGVKGDELKSYGSTLEETRADLFGLYYLGDPKLVELGLVPSFDVAKAQYASYILNGMMTQLARIEPGKNVEESHMRNRKLIAEWCYEQGKADNVIEWRTEQGKTYVVVNDFEKLRELFGQMLREIQRIKSEGDYEAGKALVEQYAVKVDPKLHREVLDRYEALHIEPYGGFVNPEYELVERDGRIVDVKIAYPANYVEQMLGYSRDYSFLPDRN
>NZ_AP019735.1|WP_034779249.1|34391_35048_+|DUF4136-domain-containing-protein
MTTKNLLTSLLVLLAVAVVSCQKEPSTSGLHEDYLVYTDYDQQADFSDVETFYLPDSILVIGNADKTEYWKDADAQEIIGTVADLMESRNFVRTDDKETAQTGLQISYVERVTYFVGYDYPYWWWYYPYYWAPGYWGDWLGWHYPYQVYYGYTAGSMLIEMVDLTADRQSNRKLPVIWDSFIGGLLTSSHKVNMQRTLDAVNQAFMQSPYLETNSVNR
>NZ_AP019735.1|WP_026074670.1|35060_35693_+|outer-membrane-beta-barrel-protein
MKTLSIFSRKALLLAVAAVTFALPGRAQLIQNTYLNVDWQVTVPLGSAFADKASGWGMNFEGGYFVTPEITVGAFISYQTNIESIGRQTLQLGSGAAMTTAQKHTLFELPFGVVGRYNFLKGSVFQPYAGLRIGADYAEMSSYYYTIQQYQDTWGVYLSPEIGVSIFPSPAQRFGFHVALFYSYASNNDDLLIYTMNNINRFGVRVGISF
>NZ_AP019735.1|WP_019129230.1|35763_36804_-|glycerophosphodiester-phosphodiesterase-family-protein
MKRPFIAVTALTLATAISFTSVAEERPASEKRLHTVQINSLEDLKAYFRYDPERDIIVSGHRGGMMPGYPENCIESCEKTLSMMPTFFEIDFSFTKDSVMVLMHDLTIDRTTNGKGRVADYTYEELQGFRLVDRDGKLTPYRIPRLKDMLEWGKDKVVFNFDNKYINTKGVSDEVRKASLDYYIRQLRPGGDWSMYHNIMLSVRSLDEAMYYWNAGIRNVMFCCEISSREMFDAYDACPIPWDYIMAYIRLSVDPRLQEVYDLLHERGVSTMTSITGSSDKVKNPRDRRVCYLRDLVSEPDLIETDYPSEFVDLPRSRAEIHALQDRAIEGNRSVKADKAKKNRRK
>NZ_AP019735.1|WP_141411781.1|36819_37977_-|mannitol-1-phosphate-5-dehydrogenase
MKRAIQFGAGNIGRGFIGAVLSEAGYHVVFADVNMEVIDRINKDGAYTVHIMDVESRDVRISNISGVDSGGGEIVDEIVRAEIITTAVGLRILPFIAPAIAKGIAARRAAGVGEPLNVIACENGIRATSQLREEVYKHLSTEEAAWCDAHVGFADCSVDRIVPPVRSENPIDVVVENFYEWNVEEKSFVGGAPHIEGMNLADNLLAYIERKLFTLNTGHAITAYLGRMKGLATIDESIADPAIFAIVKEAMQQSGQALVEKFGFDRDAHFKYIDKIIGRFKNPYLKDDVTRVGREPLRKLSSTDRLVKPMMTAREYGLPCDKLLLGIGAALHYNNPEDPQSVKMQELIAAKGLRQAVSEITSIPATDPVIEEIAAATAEVEKRIR
>NZ_AP019735.1|WP_162852307.1|38014_38863_-|prolyl-oligopeptidase-family-serine-peptidase
MKKLFLTCFCCASAVLGARAQDEHIVIWDNASAPTSSGLFGPTVIEKEVFVANNNVAELFVYKAEEPSGRAVVVCPGGGYHNLAIGYEGHDMARWLADHGTTAAVLKYRMPNGHCEVPRNDAEQALRIMREHAAEWGYDASRVGIVGSSAGGHLAASTGTISDEKPAFMILFYPVITAEEGKLHKNSFKYLLGKDYSSEEARNYSLEKRVSALTPPTLLLLSDDDRIVPPVNSLLFYEALKRNGVKASIHVFPTGDHGWGIKPEFKYIEQWQRYALDWLEQF
>NZ_AP019735.1|WP_141413517.1|38906_40568_-|phosphoenolpyruvate--protein-phosphotransferase
MADAVAIGRVWRYRAGAYAPSGRVVPSGERPAEQSRFDAAVAAAEGELEKLAAANEIFAAHLELAADPMLMENVAEKIAEGMTAADAVHAASGELAALFAQIDDEYLRARADDVRDVCRRILRQLVPSETDPFAAIPDGSILAADELAPSDTARIDFSRVRGVVTRRGSATSHLAILARNRNLPAVVGLGDDFDRLDDGTIVVLDGLAGELLIAPDEHTAAEYRRRMEEAEARSAAADAYASQPVTTRDGRALAVLANAGSVDEVERAIRSGADGIGLFRSEFLYMQRQDGFPDEQVQTAAYARAAELCGGRPLVIRTLDIGGDKSLPYYRFPEEENPFLGWRAIRVSLELRDMFRTQLRAILRASARGGVRVMFPMIVSLAELRDALALLEECKEELRRQEVPFDDRIPVGVMIETPAAVFMADELAAEVDFFSIGTNDLTQYVLAVDRGNRRIAAMYDTLHPAVVRAMRLTVDAAHRHGCEVGICGEFAGCAAHAELLVGLGFDELSVAPPSVPAVKERIRGLETPQAELTARRAVEAATASEVHELIGVG
>NZ_AP019735.1|WP_019129226.1|40601_40862_-|HPr-family-phosphocarrier-protein
MVSKTVTIEAPNGMHARPVSALVALVKASGQQVTLRTPAKSVSGASMIGILSLGLKKGSEVEVAVEGDNEQAVLDEVVAAIEAITD
>NZ_AP019735.1|WP_141411782.1|40865_42713_-|PTS-mannitol-transporter-subunit-IICBA
MKERIQRFGKSLSSMVMPNIGAFIAWGFITALFIPTGWWPNASLGQFVEPMLRYLLPLLIAMTAGRHVAGDRGGVIAAVAVMGVILGSDIPMFIGAMAIGPFAGWVIRSFDRWAEGRIPAGFEMLVNNFSVGILGIVCALIGFYAVGPVVSALTVFLSAGVSLMIEHGLLPLVAVFIEPAKVLFLNNAINHGIFSPIGIEQARQTGQSIMFLLETNPGPGLGVLLAYWAFARGAARSSAPGAIVIQFFGGIHEIYFPYVLMRPAIIVAPIVGSAAAILFYSLTGTGLTAVASPGSIIAVAAMAPKGETLLVLAGVVVAAAVSFFVAAPIVKRAHLEEVKPVQKPNGTVIGGTSRAPRALEGPIRTVVFACDAGMGSSAMGATRFRKRIEPLGSGVRVTNSSVDTIPEGTDVVVCQSQLSQRAGKAAPASEVIVIGNFLSDPALDGLYGRIEGQTRASEAPQSEEVPAAATPAAPASEMLTLQGIRTGLAPVGKEEAIRAAGALLAACGYVDGKYAEAMVARERVATTYLGMGIAIPHGTAEAKSRIRRSGIVVMQYPEGVDFGEERAQLVIGIAGAGDEHIEILARVTSALEDEEVLRRLKTTDDPRYILEKLAI
>NZ_AP019735.1|WP_141411783.1|43309_44533_+|tyrosine-type-recombinase/integrase
MKQMDVRVAFYLKKSETNANGCCPVMARLTVGNHSEAAFSAKMSVPVSSWVSGRATGKSTATREINRQLDELRASALAIYKEQSAIREEVTAEEVRDLLLGKASGQTTLLSYFQTFIEHFEKRVGVNREKGTLRSYRYARNCVSAFLQTQYKLSDIPFTALDRSFIDRYDLYLRTERRIAPGTVVLLTTRLNTIVGEAVAEGIITADPFAGYEPKRPERAQKYLTADELHRLMTTPLHHPTLYQTRDLFLFSCYTGIPYGDMCRLSEDDLEIAEDGEVWIKTTRKKTKIDYELPLLDIPLHILDKYRGIAPEGKLLPMYGNTTLNRALKRIASICGIEKRLVFHCGRHTYATEITLSQGVPLETVSKMLGHTRIDTTQIYAKVTDDKIGADTQNLDKKLAERFSIAL

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Crispr_ID: NZ_AP019735_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_2

351154-351247

Orphan

Consensus_repeat	Method
GCAAATAAATTTGCATGGCGCCCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_2

>merge|NZ_AP019735|2|351154-351247|CRISPRCasFinder
GCAAATAAATTTGCATGGCGCCCGTTTATTCGTATCTTTGACTTCGTCTTAGATACTTCGCCTCGGCCATGCAAATAAATTTGCATGGCGCACG

>NZ_AP019735|2|2|351154-351247|CRISPRCasFinder
GCAAATAAATTTGCATGGCGCCCG	TTTATTCGTATCTTTGACTTCGTCTTAGATACTTCGCCTCGGCCAT
GCAAATAAATTTGCATGGCGCACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141411966.1\|346416_348015_+\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|379837
NZ_AP019735.1\|WP_026075036.1\|352254_352719_-\|porin-family-protein	unknown	unknown	gnl\|CDD\|379226
NZ_AP019735.1\|WP_141413530.1\|341119_344353_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_AP019735.1\|WP_141411964.1\|338614_341062_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019131154.1\|352861_355591_-\|pyruvate,-phosphate-dikinase	unknown	unknown	gnl\|CDD\|236446
NZ_AP019735.1\|WP_141411968.1\|348979_349630_+\|LUD-domain-containing-protein	unknown	unknown	gnl\|CDD\|376839
NZ_AP019735.1\|WP_019131161.1\|361029_361302_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226580
NZ_AP019735.1\|WP_141411971.1\|360475_360949_-\|nucleoside-deaminase	unknown	unknown	gnl\|CDD\|238612
NZ_AP019735.1\|WP_141411962.1\|335888_336452_+\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|239516
NZ_AP019735.1\|WP_019131156.1\|356925_357699_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379312
NZ_AP019735.1\|WP_141411967.1\|348244_348955_+\|pirin-family-protein	unknown	unknown	gnl\|CDD\|380375
NZ_AP019735.1\|WP_026075038.1\|359650_360199_-\|30S-ribosomal-protein-S16	unknown	unknown	gnl\|CDD\|237744
NZ_AP019735.1\|WP_019131157.1\|357763_358942_-\|tRNA-2-thiouridine(34)-synthase-MnmA	unknown	unknown	gnl\|CDD\|234664
NZ_AP019735.1\|WP_019131155.1\|355699_356500_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141411965.1\|344378_346358_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_AP019735.1\|WP_141411970.1\|358961_359477_-\|16S-rRNA-processing-protein-RimM	unknown	unknown	gnl\|CDD\|234650
NZ_AP019735.1\|WP_019131144.1\|336984_338259_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141411963.1\|336570_337008_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413531.1\|349626_350991_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|129794
NZ_AP019735.1\|WP_141411969.1\|351519_352179_+\|nitroreductase-family-protein	unknown	unknown	gnl\|CDD\|380318

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141411966.1\|346416_348015_+\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	gnl\|CDD\|379837	pfam16370, MetallophosC, C terminal of Calcineurin-like phosphoesterase. This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.	5.52888e-33
NZ_AP019735.1\|WP_026075036.1\|352254_352719_-\|porin-family-protein	gnl\|CDD\|379226	pfam13505, OMP_b-brl, Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.	3.83416e-11
NZ_AP019735.1\|WP_141411969.1\|351519_352179_+\|nitroreductase-family-protein	gnl\|CDD\|380318	cd02142, McbC_SagB-like_oxidoreductase, oxidase similar to the microcin B17 processing protein McbC. This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.	4.23528e-17
NZ_AP019735.1\|WP_141413530.1\|341119_344353_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_AP019735.1\|WP_019131154.1\|352861_355591_-\|pyruvate,-phosphate-dikinase	gnl\|CDD\|236446	PRK09279, PRK09279, pyruvate phosphate dikinase; Provisional.	0
NZ_AP019735.1\|WP_141411968.1\|348979_349630_+\|LUD-domain-containing-protein	gnl\|CDD\|376839	pfam02589, LUD_dom, LUD domain. This entry represents a domain found in lactate utilization proteins B (LutB) and C (LutC), as well as several uncharacterized proteins. LutB and LutC are encoded by th conserved LutABC operon in bacteria. They are involved in lactate utilization and is implicated in the oxidative conversion of L-lactate into pyruvate.	6.14339e-35
NZ_AP019735.1\|WP_019131161.1\|361029_361302_+\|hypothetical-protein	gnl\|CDD\|226580	COG4095, COG4095, Uncharacterized conserved protein [Function unknown].	1.76704e-11
NZ_AP019735.1\|WP_141411971.1\|360475_360949_-\|nucleoside-deaminase	gnl\|CDD\|238612	cd01285, nucleoside_deaminase, Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.	7.17711e-47
NZ_AP019735.1\|WP_141411962.1\|335888_336452_+\|NUDIX-domain-containing-protein	gnl\|CDD\|239516	cd03424, ADPRase_NUDT5, ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. Like other members of the Nudix hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue Nudix motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the Nudix motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer.	2.76195e-41
NZ_AP019735.1\|WP_141411967.1\|348244_348955_+\|pirin-family-protein	gnl\|CDD\|380375	cd02910, cupin_Yhhw_N, Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, N-terminal cupin domain. This family includes the N-terminal cupin domains of YhhW and YhaK, Escherichia coli pirin-like proteins with unknown function. YhhW is structurally similar not only to human pirin but also to quercitin 2,3-dioxygenase (quercitinase). Although the function of YhhW is not completely understood, YhhW and its human ortholog have quercitinase activity and are likely to play an important role in transcription and apoptosis. This N-terminal cupin domain of YhhW has a metal coordination site and is thought to have catalytic activity while the C-terminal cupin-like domain has diverged considerably and has closer alignment with C-terminal pirin. YhaK is found in low abundance in the cytosol of E. coli and is strongly up-regulated by nitroso-glutathione (GSNO). There are major structural differences at the N-terminus of YhaK compared with YhhW; YhaK lacks the canonical cupin metal-binding residues of pirins and may be involved in chloride binding and/or sensing of oxidative stress in enterobacteria. YhaK showed no quercetinase and peroxidase activity; however, reduced YhaK was very sensitive to reactive oxygen species (ROS). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.	3.55049e-72
NZ_AP019735.1\|WP_026075038.1\|359650_360199_-\|30S-ribosomal-protein-S16	gnl\|CDD\|237744	PRK14521, rpsP, 30S ribosomal protein S16; Provisional.	9.11512e-64
NZ_AP019735.1\|WP_019131157.1\|357763_358942_-\|tRNA-2-thiouridine(34)-synthase-MnmA	gnl\|CDD\|234664	PRK00143, mnmA, tRNA-specific 2-thiouridylase MnmA; Reviewed.	0
NZ_AP019735.1\|WP_141411965.1\|344378_346358_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	1.63907e-34
NZ_AP019735.1\|WP_141411970.1\|358961_359477_-\|16S-rRNA-processing-protein-RimM	gnl\|CDD\|234650	PRK00122, rimM, 16S rRNA-processing protein RimM; Provisional.	1.0905e-20
NZ_AP019735.1\|WP_141413531.1\|349626_350991_-\|MFS-transporter	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	2.46557e-57
NZ_AP019735.1\|WP_019131156.1\|356925_357699_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	1.88066e-19

>NZ_AP019735.1|WP_141413531.1|349626_350991_-|MFS-transporter
MPRRLWAILAVTFGVALSVLDGTIANVALPTIAHELGVSSADSIWVVNAYQLAIVVSLLSFSTLGDVVGYRRIYIGGLVFFTLSSVGCAFAGSLEMLIAMRVIQGFGGAAVVSINTSIIRIIYPRDQLGRGMGINATVVAIASVAGPTLAAAILSMASWHWLFAINIPIGIAAVWLSMRFLPYNPVRLSDRRFDWRDGVMNALTFGLLIASVEGFSHGLDPRIVACGASAFCVVGYLFVRSQLRKPYPLLPFDLLRIPIFSLSVFTSICSFVAQMLALVALPFFLQKELGYSDVQTGLLLTAWPAVIVVVAPVAGLLVERVHAGVLGGVGLTVMAAGLLLLALLPDHPTDGAIIWRLVVCGAGFGLFQSPNNSILIASAPAYRSGSASGMLATARLIGQTTGAALMALFFHLFPSNSTHLALYVSAALALAGALASSTRISLALPESLRRAKEA
>NZ_AP019735.1|WP_141411968.1|348979_349630_+|LUD-domain-containing-protein
MQNETPDFPTRLAACARQLRRHGFEAVCVADLAEAGRRLRDEIARCAPRSISYGDSMTLRATGIVEELRNGSRYEFIDGFDPALPRPEQLEVRRKGLLADFFMTGVNAVTLGGSLYWVDMVGNRTAPVIFGPRRVVLLAGRNKIVDTQADAERRVQQIAGPKNVARHTGFRTPCAVTGLCADCNSPQRICNSRVWLERCYPAGRILVLLIDEEAGL
>NZ_AP019735.1|WP_141411967.1|348244_348955_+|pirin-family-protein
MEKVIHRAATRGYFDHGWLQTFHTFSFADYYNPQRIHFGALRVLNDDTVAGGEGFGSHPHDNMEIISIPLSGELRHEDSMGHGEVLRPGEIQVMSAGTGIVHSEFNNLPDREVKFLQIWIFPDRDDLTPRYEQIRLAKAEPDRLRPIVAPKGEGGEHVGWIHQKAWLSTLDLTSGAETDYELHGANHGVYLFVLEGVVEAAGETLRTRDGMGIRRTERVALRGIENSHLLLIEVPM
>NZ_AP019735.1|WP_141411966.1|346416_348015_+|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein
MKMNPIFNLLRRTMFAALAATTIACGGDDPVVPQLPGGGNNGQDGTEEEKPEIKPDEGITLYGLVSDSEGNPLEGIVVSDGYSVVATDAKGVYQIVRSANAKYVFISAPSGYEIPTQANYGSYQGTYQAANSLTGSSTKPYRADFTLTKLSQSDTRFLLFGLGDPQPDNDEHIKRFRTETVPDVKKIKADYTIPTVGIALGDILGKGDAQTFTSMKRALGETGVPFFTTIGNHDKSSVDYTGDTYRDVLGPRWYSFNRGEVHFVAMDNCLFSGQDYTGGFTDEQVAWLEKDLSFVPTSKMIVLYYHIPLRDTNYRNRQKVLDLISKYQNPTLMCAHTHYFQPYHMRSHNLFERIHGGTCGYFWRSNCGGDGTPNGFMVYEIDGTKIVDTYFKASQRPDDHQIRLYHGDAVFAGPYATYKYDLGADVVVANVFAAGMDGTTWKVELSEDGGKTWSDMSPIEQNYGDRWIRGYHIGVEHHPTESGTSPCYHQYQYKLKDAAATAIEVRATDSFGHVYTQDTFTADNDFTEAEKY
>NZ_AP019735.1|WP_141411965.1|344378_346358_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKNILKYLLLCCSALSLFGCEDYLDKTPQGDKTEEDVFTRFNETEQLINRLYFYVRAADQPLVHIRYFSDSALADECEGSSAENGWSNKFNEGDWEPGAELYSKCNATTDAGACHTFWPALYQDIRCANVILEGIEKYNTPDSQVHPGTLSQRIGEVYFLRAYLHYCVLKSYGECPYVDYTVDPNNLPKFERENVHSIVEKICNDCDNAFSRVPERYLAEQFGRVEKGTCLALKAMARWIAATPLYNGSTLKGDNRNYASEYQRYDPARWDAAAAAAKAVIDFTTNTGEKRYSLYQGADKSNTTNFGNVDESNGKVYTRLWELFSGTARSLDAKKCEWIWFFLQAKTVGYHNDMYPPSSQGQAREVPVQEHVDEYEVIGPDGYGYPIYALKENHKALYGGLISEEDMAKAYDDANPYENRDPRFYRDITYHGAMFKGKWINTATGSDEINAANSTTTGYFTHKFFDGYYTKGMSGDWNMDAPLIRLATIYLVYAEAVTRSKGATDEVYNMMNDLRARSFMAPIPPAAKTNKELLLDYILRERRVELYHEKSRFFSTRFYLEPTSPTELAKESQWNALPGSNDEKAQQYFAKYGAYPKTQHRICGMRPVEDPDGKISVGGKKYRMERFWKEDRVFLEKHYLFPIPTEELQRANIQQNPNW
>NZ_AP019735.1|WP_141413530.1|341119_344353_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MCLFCLGEAAVASPGKADAEPAAQAQSSKLTVKGFVKDDKGDPMIGVTLIVKGTNFGTVSNADGSYSIDVPYGGATLMVSYIGYAPQEINVNNRTKIDITLLEDSKALEEVVVVGYNVQKKETITGSIATITTKDLKQSPTANINNALAGRMPGLLVNQFSGGEPGNDAAQLNIRGISTYGQSGVIMIVDGIERDMSYLAPDEIETFTILKDASATAPYGIRGANGVIVVTTKRGRKGEKPTVDFKASVGISEPIRYPDYLGSADYATLYNEAMLNDNPSLAADSPSLFTQTAIDNYRRAKGDNSDGLGYNWDYFDYAFQPSVLQDYSLSVRGGTDRARYFILGSYYKQGGNYKHSNSDNANNFLRYNFRANVDVDATKRLKISVDLGARVTEYTYPGATAANIISLANTQPPYLPIVLPNNGNEVNQGDFEENGGYLLYADNDYRYNMLGQLSRSGFSKRTRRYLQGSFKLSHDLDFITEGLSIAAQFSYDTFNQHTINNSVPTHSTGNLTYPGYSTWMLPEEYSIDEWKNNSAYWIQNGSYVTANQRTTDDAQGNSLSHANPEGTSRFQARLDYARKFGDHNVTAMVLYYMQNKIVGKEVPYRYMGFSGRATYDYKNKYLFEFNIGYNGSENFARGHRFGVFPAGSIGWVVSQEEFMKNVRWIDHLKLRASYGLVGNDQMGSTRFAYLQYYTSGSNMNIYFGEDKKAFGTTLIEGIFANPSLTWEKARKFNFGIDAEFFHQRLTLSVDVFKEHRYDILTSLNTDDKLGFPYIVGQTAPIVNSGIVDNRGIEFQLGWDGRIGQHFRYWIRPNFTFARNKVKFCNEISYIDNNGRDCPWRYQTGRRVGENFCYIFDHFVADRDEADRLNAMNGGSGFAIWGPVQPGDVVYKDMNGDGVVNNYDRAAVGNPRTPEIQYGIPVGLSYKGFDFSMLWQGSALCSVQLSGPAVWDFPLYDQSRTGKVRKMHLNRWTPETAATATYPALHYGIHNNNKQQYSSLFLYDASYIRLKNVEIGYTLPKAWTSKAGIQSVRIYAQGQNLLTFDRLGDVDMDPEIKNGDGSWFPVQRVVNLGINMTF
>NZ_AP019735.1|WP_141411964.1|338614_341062_+|hypothetical-protein
MRKSLLFLLNTLLAAATLCVVSCGIDDVDAEDGAIQFELYDTEGTLIEGLQSMKFGATTAYTLKSAFVTYTEVTAPAGWKCSVIPSSRSCTVTAPVASDLEAEAGGDITIAITSQAGRTMSYTLSVAALEESISLTFDGDATTKNHIFSYGKSLVFPFSCENTSSLEVEAPEGWTTETDLENSQLTVTAPMPDSQNPTLTGAVKVTPLSVRGTAGESSSISVELSTKMPVIQFAEPIDRFVFGEQRNIPCTMQYVDKCDITAPEGWTVELDIAASMLKVTAPAEGVGIPAGTVTLDAVSAEELTESFETQLSLKGIATGDDFVAFGKAVTEAAPLDEFMQEGTVILLQDVDLSAFSQTCFVGQAENPFTGTFDGKGHTLTVSLNDGDAKELGLFHTLDATAAVKNLTLAGSMTISKIDPVTAGTLAVFNNGAALTGVTNTAAITFSGLKTSSTMGNLGGLVGQDKAGSIYTDCHNTGNFEFLQSVRSVAIGGLVGSAADDTVGSFVDCSNKGKINMNLADSGQDSGRIGGIIGMTEAAEWSYTNCVNEGAMTMDFNGTNKQFHSLGGILGYGYGSFEKCYNRGQIVMNNAKSANRRIGGIAGCIGSDKGKDKLSLKMVDCHNEADIAVTTNYTGGLVGIAEKMKSGLIENCTNTGNLSNPKTDETAAGSVPSQIGGIIGSAYGNLQIKGCINRGSITGVFRYRAAGILSAARNAGNSIESCENYGNITVTTIEPATTAFPLVAGLVVIENSNTVVTISTSKNVGTLTATVKSAEHVNPVYIYQKVFEKDEADVTICDQATKDASAGTVMNITIKE
>NZ_AP019735.1|WP_019131144.1|336984_338259_+|hypothetical-protein
MYKAAADQLEAIPAHGPEFDSVDYYNCYLKLYHTMAQTAMAGPLQREYRRLKGLYRDSVLLVVDRNRLTCTLMRHDKRYEEGGDPQESIRELNAFFSRNDNSTPNKAVIANSLADAYGRLGDDEQRLRYLTLTAIYDLEVPSLAYSALPRLADLLFRRGDLVRANRYITRSLDDAIDCNSVNRILIASRTMTEINQSFMQEIARHQHRLYLLLAVVTGTILLLTGILVFTLRQKRTIKQLQTQHANDNERLRELNERLSVINRQQETINDELSKANTVKDKYIRHYMQLSTLYINKLERFRVQLFKTFNTHGLDRLLRELRSPSSTEREYKAFFNEFDTVFLSIYPDFIEQVNALLHETERLKSTKLNTEFRLLAVIRLGITDNAQIAQFLHISINTVYTYRNRLRNAATIPPQEFEKRILEIR
>NZ_AP019735.1|WP_141411963.1|336570_337008_-|hypothetical-protein
MVGCGLVHSQEDEILAADEPCGVDPLRIAQLAGVRFEPVAVTERRVELELLEFVVEMEGGGIPVARGAAFMQIVAVGVDPVEFEPDRLFAFGYERIEPSEKFVLGEGQQRVEIPPPSAFREWRSLFVAARQMFHPMNSPPMIERA
>NZ_AP019735.1|WP_141411962.1|335888_336452_+|NUDIX-domain-containing-protein
MKQPDHRPWKVLNSEYLAHEPWFTVRREAVELPGGARIPSYYVLEYPDWVNVIARTDDGRFLLIDQYRHGLGRTSYEIVAGVRDPQDATPLDAARRELYEETGYGGGEWKEYMVLSANPATHTNLTYTFLATGVQPLSTQHLEASEDIRIHLFTFEEVRRLLEENCIPQALMAAPLWRYVAEHSERR
>NZ_AP019735.1|WP_141411969.1|351519_352179_+|nitroreductase-family-protein
MKNLLFVAAALLGACATQPPKPAATPVEMTECIALAAPAAKAGATINEALAARRSWREFGPEKLSLEELSGVLWAAAGENRTDGKLTAPSALALYPITVYAVFEEGIYRYDGREQTLTRVAEGDHRAAAGRQPFVATAPLNLVYIADLQTYEGKGIPEENVLMLCAMDAAGYAENVNLYTAGHALRSITRGSAAADELLSLLRLDPARYRFILAQSVGK
>NZ_AP019735.1|WP_026075036.1|352254_352719_-|porin-family-protein
MKKLLLLLAAVVCISTTASAQDKGDWAIMPRINIYTAWDADTVFGIGAAARYNVLDQLRLEPALTLLCHDGCSIDLNCDVHYLFPVADRWNLYPLAGISVNDFGDWSAGINLGAGFDYAVADRWDITAGLKYMIETHKNWSNPLIISVGASYRF
>NZ_AP019735.1|WP_019131154.1|352861_355591_-|pyruvate,-phosphate-dikinase
MADVKRVYTFGNKAAEGNGKMRELLGGKGANLAEMNLIGIPVPPGFTITTEVCTEYYAHGKDKVIELLRPEVERAVKHIEQLTNMRFGDKTMPLLVSVRSGARASMPGMMDTILNLGMNDVAVEAVAKRTGNPRFAWDSYRRFVQMYGDVVLGMKPQTKEDHDPFEVLIEEQKAKRGVKQDTELTTDDLKELVAAFKAAVKKQTGEDFPADPWDQLWGAVCAVFGSWMNERAILYRKLNNIPAEWGTAVSVQAMVFGNMGENSATGVAFSRDAATGENIFNGEYLINAQGEDVVAGIRTPQQITVEGSKRWAKAQNISEEERRAKYPSLEEVMPAVYKELDEIQHHLEKYFTDMQDIEFTIQDGKLWMLQCRNGKRTGAAMVKIAMDMLREGLIDEKTAVLRCEPAKLDELLHPVFDKTAIKHAEVIVKGLPASPGAATGPVVFFADDAEKVLAKTGQKAVLVRIETSPEDLKGMLDAAGILTARGGMTSHAAVVARGMGKCCVSGAGELKIDYKARTIEVNGYTIKEGDWISLNGSTGEVYLGQVATRDADLSGDFGKLMELAGKYSVLKVRANADSPKDAEQAFAFGAEGIGLCRTEHMFFEGDRIKAVREMILADDEAGRRVALAKLLPIQRGDFEGLFKVMKGYPVTVRLLDPPLHEFVPHFEKEQRELAKEMGVPFEKIAAKVEELSEVNPMLGHRGCRLGNTYPEITEMQTRAIIEAAMNVRAAGIPVHVEIMVPLVGNHKELRYQKNIIDRTADEVFAERNDKIDYMVGTMIEVPRAAVTANQIAEVAEFFSFGTNDLTQMTLGFSRDDIAKFLPVYLEKGILKNDPFQILDRNGVGQLVREAVLKGRSTRLQLKCGICGEHGGEPSSVEFCHYAGLNYVSCSPFRVPIARLAAAHAALTGK
>NZ_AP019735.1|WP_019131155.1|355699_356500_-|hypothetical-protein
MAGFCLLAAGLRVRAQPPHGVAFYDADCLYDTVPSPFGNDTRYLPQGEMRWTGERYRRKVMQTAAVIDSLGLPLVGLYGVENESVVRDVAAACKGDYAYLFRTTDSYNGLDFALFYFGDRFFPDRVEAGHFWMTAAGELRGAGRVCLLMSASDRYIGYKIEEHRRQHPDERLLVAGRTAGAEPQRCGLSEPLAAARRAGRGTRRAGNRWEMRSNVLIDTAFRVVRGDVYARRWLFDPSGEAPWATYTRRRYEGGPGANLPVFCYFR
>NZ_AP019735.1|WP_019131156.1|356925_357699_+|class-I-SAM-dependent-methyltransferase
MSKEYNLISDFDYRIIAAFFAGLDRQGPGDDAQTRRALSFIDGLPPRPRIADIGCGTGRQTAVLASALDGPVTAVDLLPEMIEGLHRRMETEGRTEQVTGIVASMLSLPFAEASFDLLWAEGSIYNIGFEKGLTQWRRFLKPDGFIAVTECSWLSSARPDEMEFFRDNFPEIDDISGKIRCMERAGYRPVAHFILPDSCWTENYYAPAAARAREFLATYDDAPLARHFVERLEEEIEQYRRYGRRYGYVFYIGQRTE
>NZ_AP019735.1|WP_019131157.1|357763_358942_-|tRNA-2-thiouridine(34)-synthase-MnmA
MQRVVIGLSGGVDSSVAAYLLKEQGYEVVGLFMINWHDTTGTLEGDCPWHDDRVFAELVARRLDIPFHVVDLSEEYRRRVVDYMFAEYERGRTPNPDVLCNREIKFDVFLKEALRLGADFVATGHYCRRECVAAADGTEHYRLLAGVDGNKDQSYFLCQLSQEQLSRALFPVGGLTKPEVRRIAEEQHLATARRKDSQGICFVGKVDLPVFLQQKLAAKRGNVHEIRADWPKYARTAAPDDLPALAEPWRYTVRDGKKIGEHNGAHFYTIGQRKGLGIGGRRESLFVLATDVGQNVIYVGEGDAHPGLYRKALFMKAGDLHWIDPAERMRAGQRRRFRVRIRYRQPLQGAELVVCDEGGYLLFDEPQRGVTPGQFAVWYDGETLVGSGVIDR
>NZ_AP019735.1|WP_141411970.1|358961_359477_-|16S-rRNA-processing-protein-RimM
MVMLLPVAKVTKLFGAERGGGVVVALYAEFPEDFAPESEPLFVRIDSLDVPLWCERFERRGAAGALAEFADWDTARRASELVGLELFVEADEERSDDEFYMEDLIGFAADVDGRQGEVTDYYDSEANPLLGVTIDGREYLVPAVGEFIAEIDFEGRRLRMTLPEGLLSLND
>NZ_AP019735.1|WP_026075038.1|359650_360199_-|30S-ribosomal-protein-S16
MAVKIRLARHGKKAAPFYHIVAADSRAPRDGKFIEKLGTYNPITNPATIELNFERALDWLMKGAQPTDTCRAILSYKGVLYKKHLLGGVAKGAFSESDAEAKFNKWMEEKLGKIASKESKLATDAKAAEKARLAAEAKVKEERAKAIAEKKAAEAAAAAEAEGAAAEGEAAEAPAEGEAAAE
>NZ_AP019735.1|WP_141411971.1|360475_360949_-|nucleoside-deaminase
MNGSKNKFMELAIALSEKSVAEGGGPFGAVVVRRGEVVATGTNSVTLLNDPTAHAEVSAIRAACAAVKDFKLEECEIYSSCEPCPMCLSAIYWAGIRKIYFANTREDAKRIGFDDSFIYDQIPLAPSRRTVPSEEMMRAEALQAFRLWERKEDKVEY
>NZ_AP019735.1|WP_019131161.1|361029_361302_+|hypothetical-protein
MHPSDIIGSIAAIAMVFGYLPQTVRTVRTRSTDDIATGTFLMMGFGSACFAVQGILTGNIPLFVTNLLTTIMSSIVFGIKIYNDYFKKRR

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Crispr_ID: NZ_AP019735_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_3

706304-706401

Orphan

Consensus_repeat	Method
TTGCCCTCGGCTTATTCGTACTTTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_3

>merge|NZ_AP019735|3|706304-706401|CRISPRCasFinder
TTGCCCTCGGCTTATTCGTACTTTGATTGTGCCGAAGATACTCCCGCCCGGCAATGCTCAAATAAATTTGACATTGCCCTCGGCTTATTCGTACTTTG

>NZ_AP019735|3|3|706304-706401|CRISPRCasFinder
TTGCCCTCGGCTTATTCGTACTTTG	ATTGTGCCGAAGATACTCCCGCCCGGCAATGCTCAAATAAATTTGACA
TTGCCCTCGGCTTATTCGTACTTTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141412158.1\|698468_699857_-\|asparagine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235176
NZ_AP019735.1\|WP_141412163.1\|705453_705897_+\|lipoprotein	unknown	unknown	gnl\|CDD\|369706
NZ_AP019735.1\|WP_141412168.1\|713496_714450_+\|calcium/sodium-antiporter	unknown	unknown	gnl\|CDD\|223604
NZ_AP019735.1\|WP_141412161.1\|702320_702992_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197715
NZ_AP019735.1\|WP_141412159.1\|700530_701847_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225789
NZ_AP019735.1\|WP_141412160.1\|701843_702317_+\|23S-rRNA-(pseudouridine(1915)-N(3))-methyltransferase-RlmH	unknown	unknown	gnl\|CDD\|376840
NZ_AP019735.1\|WP_141412166.1\|709375_710746_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|227203
NZ_AP019735.1\|WP_141413550.1\|711255_712599_-\|sodium:proton-antiporter-NhaD	unknown	unknown	gnl\|CDD\|215071
NZ_AP019735.1\|WP_141412165.1\|707430_709371_+\|sulfatase-like-hydrolase/transferase	unknown	unknown	gnl\|CDD\|293739
NZ_AP019735.1\|WP_141412169.1\|714458_716279_+\|excinuclease-ABC-subunit-C	unknown	unknown	gnl\|CDD\|234792
NZ_AP019735.1\|WP_141413549.1\|696285_696843_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019131377.1\|693196_695353_+\|putative-porin	unknown	unknown	gnl\|CDD\|379481
NZ_AP019735.1\|WP_141412162.1\|703183_705457_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_AP019735.1\|WP_141412167.1\|710740_711172_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_AP019735.1\|WP_141412171.1\|719005_721513_-\|Hsp70-family-protein	unknown	unknown	gnl\|CDD\|212667
NZ_AP019735.1\|WP_026075092.1\|696950_698369_-\|RNA-polymerase-factor-sigma-54	unknown	unknown	gnl\|CDD\|235648
NZ_AP019735.1\|WP_141412170.1\|717234_719004_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|223540
NZ_AP019735.1\|WP_019131393.1\|712849_713215_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_026075090.1\|695405_696089_+\|transglycosylase-SLT-domain-containing-protein	unknown	unknown	gnl\|CDD\|381606
NZ_AP019735.1\|WP_141412164.1\|706503_707358_+\|carboxylating-nicotinate-nucleotide-diphosphorylase	unknown	unknown	gnl\|CDD\|238806

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141412158.1\|698468_699857_-\|asparagine--tRNA-ligase	gnl\|CDD\|235176	PRK03932, asnC, asparaginyl-tRNA synthetase; Validated.	0
NZ_AP019735.1\|WP_141412163.1\|705453_705897_+\|lipoprotein	gnl\|CDD\|369706	pfam08139, LPAM_1, Prokaryotic membrane lipoprotein lipid attachment site. In prokaryotes, membrane lipoproteins are synthesized with a precursor signal peptide, which is cleaved by a specific lipoprotein signal peptidase (signal peptidase II). The peptidase recognizes a conserved sequence and cuts upstream of a cysteine residue to which a glyceride-fatty acid lipid is attached.	8.3723e-05
NZ_AP019735.1\|WP_141412169.1\|714458_716279_+\|excinuclease-ABC-subunit-C	gnl\|CDD\|234792	PRK00558, uvrC, excinuclease ABC subunit UvrC.	0
NZ_AP019735.1\|WP_141412161.1\|702320_702992_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|197715	smart00421, HTH_LUXR, helix_turn_helix, Lux Regulon. lux regulon (activates the bioluminescence operon.	1.60662e-17
NZ_AP019735.1\|WP_141412159.1\|700530_701847_+\|hypothetical-protein	gnl\|CDD\|225789	COG3250, LacZ, Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].	1.8087e-22
NZ_AP019735.1\|WP_141412160.1\|701843_702317_+\|23S-rRNA-(pseudouridine(1915)-N(3))-methyltransferase-RlmH	gnl\|CDD\|376840	pfam02590, SPOUT_MTase, Predicted SPOUT methyltransferase. This family of proteins are predicted to be SPOUT methyltransferases.	3.96636e-76
NZ_AP019735.1\|WP_141412166.1\|709375_710746_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|227203	COG4866, COG4866, Uncharacterized conserved protein [Function unknown].	8.16294e-57
NZ_AP019735.1\|WP_141413550.1\|711255_712599_-\|sodium:proton-antiporter-NhaD	gnl\|CDD\|215071	PLN00137, PLN00137, NHAD transporter family protein; Provisional.	1.35194e-137
NZ_AP019735.1\|WP_141412165.1\|707430_709371_+\|sulfatase-like-hydrolase/transferase	gnl\|CDD\|293739	cd16015, LTA_synthase, Lipoteichoic acid synthase like. Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.	5.40835e-66
NZ_AP019735.1\|WP_141412168.1\|713496_714450_+\|calcium/sodium-antiporter	gnl\|CDD\|223604	COG0530, ECM27, Ca2+/Na+ antiporter [Inorganic ion transport and metabolism].	5.93033e-66
NZ_AP019735.1\|WP_019131377.1\|693196_695353_+\|putative-porin	gnl\|CDD\|379481	pfam14121, Porin_10, Putative porin. This family of membrane bet-barrel proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 655 and 722 amino acids in length. SRI_1264 is identified by Gene3D as a membrane bound beta-barrel. These sequences are putative porins.	1.50347e-168
NZ_AP019735.1\|WP_141412162.1\|703183_705457_+\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	4.22281e-47
NZ_AP019735.1\|WP_141412167.1\|710740_711172_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	4.39309e-17
NZ_AP019735.1\|WP_141412171.1\|719005_721513_-\|Hsp70-family-protein	gnl\|CDD\|212667	cd10170, HSP70_NBD, Nucleotide-binding domain of the HSP70 family. HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs.	1.35681e-87
NZ_AP019735.1\|WP_026075092.1\|696950_698369_-\|RNA-polymerase-factor-sigma-54	gnl\|CDD\|235648	PRK05932, PRK05932, RNA polymerase factor sigma-54; Reviewed.	1.48914e-145
NZ_AP019735.1\|WP_141412170.1\|717234_719004_-\|AAA-family-ATPase	gnl\|CDD\|223540	COG0464, SpoVK, ATPases of the AAA+ class [Posttranslational modification, protein turnover, chaperones].	3.20455e-61
NZ_AP019735.1\|WP_026075090.1\|695405_696089_+\|transglycosylase-SLT-domain-containing-protein	gnl\|CDD\|381606	cd13403, MLTF-like, membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins. This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.	1.72453e-64
NZ_AP019735.1\|WP_141412164.1\|706503_707358_+\|carboxylating-nicotinate-nucleotide-diphosphorylase	gnl\|CDD\|238806	cd01572, QPRTase, Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.	1.71843e-138

>NZ_AP019735.1|WP_141412163.1|705453_705897_+|lipoprotein
MKKFLLLALAAFALAACNDDDTPDEFVQGDNTIAVFENDRLVFYDYDVFWEYSEPYTDPYGVTCIDLYMNKTRFVQNMPALDMEVPGIPIHPTPAGFEFDLRQAVPYYRGEPMPRYTLYDLEGELNGTLLEVEFSCIGYDVEYLGRF
>NZ_AP019735.1|WP_141412162.1|703183_705457_+|TonB-dependent-receptor
MKFNAMIPTPFRRRFCVCLLLCVAALCAHAEPRRTVRTHDEAPEAIDTAVVMDNVQVTAIKQGLTLRNRPVAASVVGRETIERRGVTAIKELSQLVPNFHIPDYGSRMTSSVYVRGLGARIDQPVMGLNVDNVPYLSKDDYDFDLADIERIEVLRGPQSTLYGRNTMGGVMNIYTLSPLAYEGTRLGAEYASGNTLRLRASTYHRPSPRTGISLAARFMHGDGFFTNEYTGRTCDWERSGGARMRLQFRPDERWSIDNTLAFGMLRQGGYPYASAATGRIAYNDPCGYRRTTLNDGLTIRYAADGWEIASITSYQYSDDRMTLDQDFLPDSYFTLTQAKQDHGLTEDIVVRSRGEGRYGWLVGAFGFYRHRSMQAPVLFKEDGLERLIADKAEQYTGLRPHFASDRMALDSDFRNPAWGAALYHESQLRLGRFDLSAGLRIDYERTRLCYLSSTDIDCTFGDGRITPFTERDTLHKSFVQLLPKAAAVYRINDGNSLYASVAKGYKAGGFNTQMFSEVLQNSVMERMGVYWDRHYDIDRVVAYKPEKSWNFEVGSHFAFADGRIRGEATLFYILCRDQQLTVFPEGQTTGRMMTNAGRTRSRGGELSVQALVARRLDLRLSYGFTHATFAEFRSGNADYAGKRIPYAPRHTAAAVAEYTVSVGRSWLDGIVLSVDGRGVGPIEWNEANSLRQKFYALAGCAIRFEQRHGSLSLWCRNLTQTRYDVFYFESIGNAFLQRGRPREWGVTLTINLQHNER
>NZ_AP019735.1|WP_141412161.1|702320_702992_+|helix-turn-helix-transcriptional-regulator
MQPHRPAIAVVTPSILTGLGLESILRRIIPMAEVEVYDRFERFAADRPDRFFHYFVASQTFVEHNAFFLERRHKSILLTDGAPQSTLRELHCLDIAQSEEGLVRDILRLHQHAHREGYPDGTAAAYPATHPTHPSARPACDPHGRMTDETVQPSLTQREIDVLRLVVAGLLNKQIAQRLDVALTTVISHRRNLVRKLGIRSVAGLTIYAVTKGYVDAEQLGEQ
>NZ_AP019735.1|WP_141412160.1|701843_702317_+|23S-rRNA-(pseudouridine(1915)-N(3))-methyltransferase-RlmH
MNIELLVVGKTDSKEVEALVELYVRRVNRYCRFAVTALPDVRNTRSLTQNQQRTAEGEAILRQLAAGDHVVLLDERGDEMRSVEFAYWLQKRMLGGVRRLVLVIGGPYGFSDAVYARADGRLSLSRMTFSHQIVRAIFAEQIYRAFAILNHEPYHHE
>NZ_AP019735.1|WP_141412159.1|700530_701847_+|hypothetical-protein
MKRFITLWTALFALAGAGAQTAEVFRSEFVPFDTRDDAALLRRGNIAHYETFSPQIVVQQADTTTVGQVVEVPLLLTDRDIYLHLENVGSAYTLLVNDARVADVEDDRTPREFLISPYIRPGRNAVMLDLRPSKTPQLQADAPAPRLAYANSYLVFQHRLHIDDYSVALVPDSTRKYGVLKLDIVVENSYNGEEPITAGYDIYDPKGKLLDYGSREIMVEGRSRDTVHIERLIYHAYANQWDDKRQPLYKVTLYTKRNSMLWEYIPLYVGFGESEYRDGRFYRFDKELSLRPQRYNAAADEKTTAAEMKALKARGINTLLPDYPQPYWFYTLADRTGFYVVDCAAIYAPDARDDRSVGGTPSNDPRLTDEYLGRVKAMYHRSRNHTSIIGFALGRDSGNGYNMYKAYQWLKSVEPSKPVFYVGADGEWNSDAIPFRMQ
>NZ_AP019735.1|WP_141412158.1|698468_699857_-|asparagine--tRNA-ligase
MKTLRIVELIKSDAVDCDVTVKGWVRTKRGNKNVAFIALNDGSCVASIQVVVELAKFDDETMRQIATGACIRVDGRLVKSPGEGQGVEVQASSIEIYGTADPATYPLQKKGHSLEFLRDIAYLRPRTNTFGAVLRIRHAMAFAIHKFFNDRGFYYWNSPLITASDCEGAGAMFQVTTLDLNNPPRTEDGRIDYSQDFFGKPCNLTVSGQLEGELGALSLGRIYTFGPTFRAENSNTPRHLSEFWMIEPEMAFYELEDNMELAEEFLKYLIGYALENCREDLEFMCKMWDKELIERLEFVLHNDFKRLDYTEGIEILKVSGRKFEFPCDWGCDLQSEHERYLVEEHFKRPVILVNYPKEIKAFYMKQNDDGRTVRAMDVLFPKIGEIIGGSEREADYGKLCARIKELNMNERELWWYLDTRRWGSAPHSGFGLGFERLLLFVTGMGNIRDVIPFPRTPQHAEF
>NZ_AP019735.1|WP_026075092.1|696950_698369_-|RNA-polymerase-factor-sigma-54
MAIHQKQVMTLQQKLSPQQIQMIKLLELPTVQLEQRIKQEIEENIVLEEAEQQNEEEEPQQISVDEYLREDDTPAYKMRANNYSKDDKPRQIPLSGGRSLQEYLIEQLGYRNLSEEEMRLAVYLVGSIDEDGYLRRDLESVADDIAFTLGEEVSPERLEAILKVIHDLEPAGIGARNLRECLLLQLSQLPMTTRSRRLARKILTSYFDEFAKKHYEKLISRLQVTEDEFRDAIAEIRHLSPKPANGYSDGGSDAAPYVVPDFILDYHDGRFELSLNSYNVPDVRINRRYVEMMRDMVSSDGRVQEKNREAVQFVKNKIDSAKWFISAIKQRRDTLMRTMQEILDFQQEYFKTGDQSKLRPMILKDIADRTGLDVSTISRVVNSKYVQTQFGIILLKSLFSEAMQTASGGEVSSYEIKNILRSCIDDEDKRRPLTDETLMDILNDKGYCIARRTVAKYREMLGIPVARLRKQI
>NZ_AP019735.1|WP_141413549.1|696285_696843_-|hypothetical-protein
MPLYVILLLVAGPTQLSYFPASVKFYLLWVTVLYTAVIPLLSVGLLRSVGRISSLAIDDRRERILPLAIGIVCYLLCAATVARIPSAMIVRKFMLAGACCELFCLAVTFYWKISLHLAAQGAAAALLVLLTFGNAGNLTGALAVAVLAAGALASARLWLGCHTIRQVAAGYAGGFIVATLAVLLL
>NZ_AP019735.1|WP_026075090.1|695405_696089_+|transglycosylase-SLT-domain-containing-protein
MLKKTFLTFVFLTLLTTFYGLNANFGPYGNRTAGSFIGSAERTEIAHTISVYDELIRSVSEEEGYDWRLMSAIAYHESRFSPDIVSKRGAAGLMQIMPAVARQFNVTGDRLLDPETNVRLAAQVLSKIDAGLRFAPGTPDDDRMSIILAAYNGGIGHVNDARRLARSHGENPDSWETVARYLALKALPEYYEQQEVRCGRFTGGSQTRAYVRDVLKRYDRYCRIAAR
>NZ_AP019735.1|WP_019131377.1|693196_695353_+|putative-porin
MSKRLGTYLLPAVLLLAALLPGRVCAQLDARSLMRAQQRGENTNLYGVPNPAPEDEEGQAQQPVDSTKEKRIKKPLESYFFSDSIRALPNFKWNVSQDYNRVRIEPLDTTLTAWRIDYPFYRNGVGDAPIGALGQGSVPLNYFERPQWQDFSFASPFHSYIYDMRNAPFYNGKRPFLQMTYIESGQKRYRETNFEIRHAQNISPSTSFSIDYKSRGTRGLYEWSRTKNQNIAVTVAHTGKRYSVHAGYVNNHIETQENGGVVGEWAIRDTVFEMPSGVPMRLTNAKAENIYRNHAFFLTQSYAIPLQRVTENDFSLADLSAVFIGHSIEYDIWSKTYTDIFGTYTDERGSKDENGNFVATEGHEYYDNWFIHPDASRDTLCERRLSNRLFVQAQPWDRNGVIGTIDGGVGFDIHTYSQFALGDYITGKYRRTRKTSYFAYGSIAGKIKKYVDWDANMKVYPSGYRGGDMSLGAHLALKGYLRGHALILEGRFSNEKRSPGYWQENLFSNHYVWSNSLAKENETRIEASFRVPDYALELAAWQGVVKNKIYYGPVGPGDSNVGVLQHDGNVSLTSLYARKDFRIGGLHLDNRVLLQWSTNQEVIPVPLVSAFLSYYYEFWVVRDVLRLQIGLDGRYNTKYYAPGYNPALSAFYNQRETEVGNYPYTDVFVMGKWKRMRIFLKYQHVNRGLFGNGDYFSVARYPLNPGMFKMGISWGFYD
>NZ_AP019735.1|WP_141412164.1|706503_707358_+|carboxylating-nicotinate-nucleotide-diphosphorylase
MKTEYKPYVDALIELAIREDIGDGDHTSLCCIPADERGRMRLLCKQEGIIAGIEIARLVLERLDPTVEFDQRIADGTRVRPGDVAFYVSGALRSLLQAERILLNIMQRMSGVATQTAVYVARLEGLHTKVLDTRKTTPGMRVLDKMAVKLGGGENHRMGLFDMILLKDNHIDFAGGIVPAIRGAKQYLRERDKNIPIECEVRTLEDIDLVFEAGGVDRIMFDNFSPEMTRKAVEKVAGRCETESSGGITLDTLRTYAETGVDFISVGALTHQIRSLDMSLKACE
>NZ_AP019735.1|WP_141412165.1|707430_709371_+|sulfatase-like-hydrolase/transferase
MKRLLKSHIALLAWRLALLYAVLAICRAIFWRYNYAGISPLADAELPALARGALLFDTVSVLYANALLIVLSLIPLHLRERRWWQRMLYFYYVVVNALLVVAVNLGDAVYFRYTQKRFTAEEIFFADNDNSLQLVGKFMAENIPLLLAGIGLIALLALAGGRKARPEPLCRRPLCYYGGGTVLLVVAALLSVAGMRGGVTRMTRPVTLSNATLYASDNARANLILSNPFCILRTVGSGGKINYERYFAPEELDGIYTPVHCPDSVGTAPLEGRNVVVFVMESMSAEHSAHLHPELYADRQVKGYTPFLDSLMQAGYCFERMYANGTRSIQALPAVLGSIPSFKTPFVLMPQALAPTRQLPRILRDKGYATAFFCGSAAGSMGFGAYARSAGIERLYSREDYEARHGRDDFDGYWGIWDEPFLQYAGEEMSALPEPFFAALFTLSSHHPFVVPDAYRDLLPEGLTRNHKCVAYTDNAFRRFFARYAGEEWFRRTVFVFVADHVSSEKFADATRVFPGDHHIIGLLYTPDGALRGRCDEAVSQIDLMPTLLGLMGNREPYFAFGRDLFGEQTPEGGFALAYDSGFEAVGGDRLLFFDERRTTGSYRTDDLRREHDLGNDPEAAALERRVKAFVQQYYRHLEQKDFTVE
>NZ_AP019735.1|WP_141412166.1|709375_710746_+|GNAT-family-N-acetyltransferase
MEFRPVRLEDKAAIERFTRPSGICNCDLAFANMYCWEGTYRSAWCVEEGFLLIRFYIDGSHHIGYMQPLGEGDFTHLIPRLEADARAAGQPLRISGLTPEGAAAVRRAHPEFGIWRNRDYEDYVYRADDLRNLTGRRYQPKRNHINRFEAAYDYRYEELTPALAPECMRLEREWRAGHDSHAAELTAEQRAMQRAFDHFGELELRGGALFVGEKLVAFTIGSAINDEAFCIHVEKADTRYDGAFTMINRLFAQHLPPHYTLIDREEDLGLEGLRQSKLSYHPLFLQPKLTAQRLTEEQLQLRALWLACFPEDTQDDVEQFLLSRYDERRCLVARRDGRIAAMLHIVPFRDTAYIYAVATAPDCRQQGLAGGLLREALDRCRAEGFRYAALIPGSEELQRWYAGFGFAGDYPARFRTHDDFDFGTGDPAHDRAMVLPLTGEPFAGETLDLSDLPQES
>NZ_AP019735.1|WP_141412167.1|710740_711172_-|GNAT-family-N-acetyltransferase
MIRIYEATEPSDLLAEAFARLLPQLSERMTAPDREAVARIVASPATRQLVAAAEDGRIVGLLSVALYDVPSGRKAWIEDVVVDAATRGRGIGEALVREALALARREGVARVMLTSNATRRASHRLYERMGFVRYETDCFRLDL
>NZ_AP019735.1|WP_141413550.1|711255_712599_-|sodium:proton-antiporter-NhaD
MLILFVVGYAFIAFEHKTGINKSAIALLMCGILWSIFSLEYPSALPGLTQTTVSDEILRHLGSTCEILVFLIGAMTIVDLIDFHGGFEFITRRITTRRKVRLLWLVALLTFFMSALLDNMTTTIIMVMLLRKIVPTTKERMLFASVIVIAANSGGACSPIGDVTTIMLWMKGNVSSAKLIESLLLPCLVSLVIPLVIASRWLKGSLPETDPADAGSSQPDYISDGESRAILFLGCALLVAVPVFKSVTHLPPYMGMVTALGIMWVFTELMYRRKRNIEESIKCRVAKVLKHIDMSTILFFLGILMAVAALESAGILSGFATGLNEHLHNVYAINTLIGILSSVVDNVPLVAASMGMYPIPDAAAVAASADPTYAAMFVQDGVFWHLLAYCAGVGGSLLIIGSAAGVVAMGLENINFVWYFKKISLMAFVGYLAGIGVYMLEVFLFGI
>NZ_AP019735.1|WP_019131393.1|712849_713215_-|hypothetical-protein
MKLRTIFGCVLAGVLWVLLAADARCVASDGETPLPAPSELTRQVPVRVADAYGLRALLVRLSLEAGDTSAFDRMQDLGRDFPSRDGASGGWGQDASYVLSAVERRVPGDADLILLLRKIRI
>NZ_AP019735.1|WP_141412168.1|713496_714450_+|calcium/sodium-antiporter
MEYLYLLAGLVLILAGANYLTDGSVALAERFRVPGFLIGLTIVAVGTSTPELVVSFLSALEGQGDMAVGNVVGSNLFNVFIILGVCALIRPLPLTRQNIRRDLPVGVAASLVLCAVLADEVLDPTHPARIGRIEGLAMLLLYVLSVWTAARAARREQPAEETPAARPIAGWLMALMIVGGLAALVFGGEIFLHNAVAIARKLGVSESVIAITLVAGGTSLPELASSVVSVVKGRPDIALGNVVGSNIANILLILGLCSTVVPLTPGGIDAVTLGAVVLSSLLLFAAAFTFRRRALDRWEGVLFLAIYGAYLWWLLAK
>NZ_AP019735.1|WP_141412169.1|714458_716279_+|excinuclease-ABC-subunit-C
MTPSDRNPLKEQVALLPLEPGVYQFLDRTGTVIYVGKAKSLRKRVSSYFMQNKEHPPKVRVLVRQIAEIRHIVVDSETDALLLENSLIKELQPRYNILLKDDKTYPWIVVRRENFPRIQSTRQLQRDGSQYFGPYSSVTMQHSILEFIREVIPLRTCSLNLAPEAIARGRYTVCLQYHLGNCKGPCIGAQSAEEYRQLLDMAVSVLKGDLRPVRAYLEGEMRRAAEALQFETAQRYKSRLAALENYSARSVIVSARIVDVDVFSLVEDDDAAYCNFLRIRNGSITAVSTVRLTPGVDTDRAQMLTLAIQHVVEQIAGGELAREVIVPFLPSATMLFDGVTFTVPRRGEKLDLLAFSERSARIYRAEQLKNMEIKNPERHTERLMNAMQRELRLPRQPRHIECFDNSNLQGTNPVASCVVFRDGRPSRKEYRHFNIKTVVGADDFASMREIVFRRYTRLMAEGQELPDLVIVDGGKGQLSNAYAVLCELGLEKQVPIVGLAKRLEEIYYPGDPMPYYLSRTGEPLKVVCHIRDEAHRFGITFHRQKRSNDFLRSELKGIAGIGPRTVETLLGHFRTVARIRNASDEELIELIGAARTQRLRKHFASS
>NZ_AP019735.1|WP_141412170.1|717234_719004_-|AAA-family-ATPase
MPTFSKKQRIGNYIVTFHVKDSKYAETYRVKDETGKNFFLKLFDYSKLHRTQFDEGGEILELSIVKNVHHPNILTLHDDGELICNGCKKAYAVYDYIVGETLAEKVNRERQCSLYDARQITLGILEGVRYLHTKPQPIMHNELTIQNIMLDLSKSIPTPKIIDFGYARYLQQSQRDFLTEGLNPFYMAPETFNGVFTAQSDLYSVGVLLYHILFGLPPHFIDLSPFQQDRNNLIDAILNERRKPLKVPEFSDTNLWSPIVEVINKALAENIDDRFKNAEEFIKALTGEIKICRNSSHSSPTQSRQLSKSSTRSGNGFADVAGMEMLKEQLRSDVIDLLKNPEQAKELGLALPNGLLFYGPPGCGKTYFAEKFAEEVGCNYMYIRCSDIASPYIHGGQDKIAAVFAEARKNAPTILFFDEIDAMLQSRSKQDNASMSGEVNEFLSQLNNCGIDGVIVIGATNKPNEIDDAALRAGRLEFKYYIPLPDFETRKALFRIHLKRRKVDLGIDYDKLAKLTDNYISADIKLIVDTAARFVFRNKLNRISLEVLENAIKITKPSVSLETIKSYEAIKAKFEPSNSEPTARRKIGF
>NZ_AP019735.1|WP_141412171.1|719005_721513_-|Hsp70-family-protein
MVQVKMRYGIDLGTTNSAICKIENGEPVIRKTDTLKDTLPSCVSYTKKRIIRVGDSAYNDLRQDKSKATKKWSRGEENVYIEFKRTMGSSTQYMSSYMGRGFSSEELSAEVLKTLRSFITEESITSAVITIPAKFKTDQIAATKRAATLAGITHCELLQEPIAASMAYGLSTTKKDGYWMVFDFGGGTFDAALLKVEEGIMQVVDTEGDNYLGGKNLDYAIVDGIIIPYLKEHFSIDCILADDSKREILRDAMKFYAEQAKNQLSFKPKCDITSQLDEFGDDDEGNELELDMIITEEQLKPVVAPIFQKAIDICKQLISRNNLAGKLDTLILVGGPTYSPVLRQMLREQITPNVDTSIDPMTAVARGAALYASGIDCEATTESKSGFIALEVQYESNTVETLEFVTVKASSKDSSMPLPSQLYIELIRGDKAWSSGKVEINEIGDVIECQLIEGKANTFAIVAYDNSGNIIPCFPNEITIVQGTKIGNAVLPYNIGIEVHDEIIDKDVFMPLTGLEKNQQIPAVGVKNGLKTPKQIRPGMAADRLIIPIYLGEFNAEGTSAIHNDHVCNVEINGDDVPALIPMNSDIDIIIKVDRSQMMRLEATFPVIGETIEKEIEIGQRDGVHIQELTQRLNEAMAQLNRFKEQSGISDAEINDADAIITDVYKRFDNEKNSEDGKMHLLADLRRAFIALERVEKNHEWDTLETEIREEFDRLEKANNDLGNKHDEAIESLRKQADEAITRKDVQYGRIVLKQIHEQFFAVTYIYQIIGFIHHHSQSFGTLKWKDPMQARSLLNIGLQIIQNNPTAEELLPIVRAVIDLLDIPENEKPTIGSL

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Crispr_ID: NZ_AP019735_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_4

868802-868911

Orphan

Consensus_repeat	Method
CCGCAAACTCCGTTTGCTTTTGCCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_4

>merge|NZ_AP019735|4|868802-868911|CRISPRCasFinder
CCGCAAACTCCGTTTGCTTTTGCCCGCGGCTTGTGCACTTTGCGGAAGACGAGCTTCCGCTTAGATAGGCGGCGCCTCGGCAAAGCCGCAAACTTCGTTTGCTTTTGCCC

>NZ_AP019735|4|4|868802-868911|CRISPRCasFinder
CCGCAAACTCCGTTTGCTTTTGCCC	GCGGCTTGTGCACTTTGCGGAAGACGAGCTTCCGCTTAGATAGGCGGCGCCTCGGCAAAG
CCGCAAACTTCGTTTGCTTTTGCCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141412241.1\|879300_880509_+\|L-serine-ammonia-lyase	unknown	unknown	gnl\|CDD\|273233
NZ_AP019735.1\|WP_019131488.1\|864948_865389_-\|50S-ribosomal-protein-L11	unknown	unknown	gnl\|CDD\|234661
NZ_AP019735.1\|WP_141412235.1\|869527_870046_+\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|240049
NZ_AP019735.1\|WP_026075119.1\|865405_865966_-\|transcription-termination/antitermination-factor-NusG	unknown	unknown	gnl\|CDD\|180161
NZ_AP019735.1\|WP_019131491.1\|866324_867512_-\|elongation-factor-Tu	unknown	unknown	gnl\|CDD\|183708
NZ_AP019735.1\|WP_141412239.1\|875145_876399_-\|L-rhamnose-isomerase	unknown	unknown	gnl\|CDD\|179217
NZ_AP019735.1\|WP_141412232.1\|859182_863043_-\|DNA-directed-RNA-polymerase-subunit-beta	unknown	unknown	gnl\|CDD\|234749
NZ_AP019735.1\|WP_141412237.1\|872150_872948_-\|rhamnulose-1-phosphate-aldolase	unknown	unknown	gnl\|CDD\|179615
NZ_AP019735.1\|WP_019131485.1\|863287_863665_-\|50S-ribosomal-protein-L7/L12	unknown	unknown	gnl\|CDD\|234671
NZ_AP019735.1\|WP_141412238.1\|873986_875141_-\|lactaldehyde-reductase	unknown	unknown	gnl\|CDD\|182595
NZ_AP019735.1\|WP_141412236.1\|870022_871906_-\|PQQ-binding-like-beta-propeller-repeat-protein	unknown	unknown	gnl\|CDD\|274511
NZ_AP019735.1\|WP_019131496.1\|872956_873985_-\|L-rhamnose/proton-symporter-RhaT	unknown	unknown	gnl\|CDD\|237401
NZ_AP019735.1\|WP_141412234.1\|868935_869487_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|182270
NZ_AP019735.1\|WP_019131490.1\|865988_866186_-\|preprotein-translocase-subunit-SecE	unknown	unknown	gnl\|CDD\|376355
NZ_AP019735.1\|WP_019131486.1\|863703_864225_-\|50S-ribosomal-protein-L10	unknown	unknown	gnl\|CDD\|234632
NZ_AP019735.1\|WP_019131500.1\|877960_878851_+\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_AP019735.1\|WP_141412240.1\|876425_877850_-\|rhamnulokinase	unknown	unknown	gnl\|CDD\|198349
NZ_AP019735.1\|WP_019131483.1\|854884_859147_-\|DNA-directed-RNA-polymerase-subunit-beta'	unknown	unknown	gnl\|CDD\|234794
NZ_AP019735.1\|WP_026075117.1\|853545_854547_+\|GGGtGRT-protein	unknown	unknown	gnl\|CDD\|316570
NZ_AP019735.1\|WP_019131487.1\|864243_864942_-\|50S-ribosomal-protein-L1	unknown	unknown	gnl\|CDD\|180071

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141412241.1\|879300_880509_+\|L-serine-ammonia-lyase	gnl\|CDD\|273233	TIGR00720, hypothetical_protein_NEICINOT_00681, L-serine dehydratase, iron-sulfur-dependent, single chain form. This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis].	5.59442e-143
NZ_AP019735.1\|WP_019131488.1\|864948_865389_-\|50S-ribosomal-protein-L11	gnl\|CDD\|234661	PRK00140, rplK, 50S ribosomal protein L11; Validated.	2.55538e-89
NZ_AP019735.1\|WP_141412235.1\|869527_870046_+\|NUDIX-domain-containing-protein	gnl\|CDD\|240049	cd04693, Nudix_Hydrolase_34, Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of nudix hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.	3.35594e-40
NZ_AP019735.1\|WP_026075119.1\|865405_865966_-\|transcription-termination/antitermination-factor-NusG	gnl\|CDD\|180161	PRK05609, nusG, transcription antitermination protein NusG; Validated.	2.72207e-58
NZ_AP019735.1\|WP_019131491.1\|866324_867512_-\|elongation-factor-Tu	gnl\|CDD\|183708	PRK12735, PRK12735, elongation factor Tu; Reviewed.	0
NZ_AP019735.1\|WP_141412239.1\|875145_876399_-\|L-rhamnose-isomerase	gnl\|CDD\|179217	PRK01076, PRK01076, L-rhamnose isomerase; Provisional.	0
NZ_AP019735.1\|WP_141412232.1\|859182_863043_-\|DNA-directed-RNA-polymerase-subunit-beta	gnl\|CDD\|234749	PRK00405, rpoB, DNA-directed RNA polymerase subunit beta; Reviewed.	0
NZ_AP019735.1\|WP_141412237.1\|872150_872948_-\|rhamnulose-1-phosphate-aldolase	gnl\|CDD\|179615	PRK03634, PRK03634, rhamnulose-1-phosphate aldolase; Provisional.	4.1337e-111
NZ_AP019735.1\|WP_019131485.1\|863287_863665_-\|50S-ribosomal-protein-L7/L12	gnl\|CDD\|234671	PRK00157, rplL, 50S ribosomal protein L7/L12; Reviewed.	2.50727e-36
NZ_AP019735.1\|WP_141412238.1\|873986_875141_-\|lactaldehyde-reductase	gnl\|CDD\|182595	PRK10624, PRK10624, L-1,2-propanediol oxidoreductase; Provisional.	0
NZ_AP019735.1\|WP_141412236.1\|870022_871906_-\|PQQ-binding-like-beta-propeller-repeat-protein	gnl\|CDD\|274511	TIGR03300, assembly_YfgL, outer membrane assembly lipoprotein YfgL. Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking].	7.75821e-30
NZ_AP019735.1\|WP_019131496.1\|872956_873985_-\|L-rhamnose/proton-symporter-RhaT	gnl\|CDD\|237401	PRK13499, PRK13499, L-rhamnose/proton symporter RhaT.	1.73411e-123
NZ_AP019735.1\|WP_141412234.1\|868935_869487_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|182270	PRK10151, PRK10151, 50S ribosomal protein L7/L12-serine acetyltransferase.	9.28219e-26
NZ_AP019735.1\|WP_019131490.1\|865988_866186_-\|preprotein-translocase-subunit-SecE	gnl\|CDD\|376355	pfam00584, SecE, SecE/Sec61-gamma subunits of protein translocation complex. SecE is part of the SecYEG complex in bacteria which translocates proteins from the cytoplasm. In eukaryotes the complex, made from Sec61-gamma and Sec61-alpha translocates protein from the cytoplasm to the ER. Archaea have a similar complex.	3.19451e-10
NZ_AP019735.1\|WP_019131486.1\|863703_864225_-\|50S-ribosomal-protein-L10	gnl\|CDD\|234632	PRK00099, rplJ, 50S ribosomal protein L10; Reviewed.	4.14102e-41
NZ_AP019735.1\|WP_019131500.1\|877960_878851_+\|AraC-family-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	2.27365e-23
NZ_AP019735.1\|WP_141412240.1\|876425_877850_-\|rhamnulokinase	gnl\|CDD\|198349	cd07771, FGGY_RhuK, L-rhamnulose kinases; a subfamily of the FGGY family of carbohydrate kinases. This subfamily is predominantly composed of bacterial L-rhamnulose kinases (RhuK, also known as rhamnulokinase; EC 2.7.1.5), which are encoded by the rhaB gene and catalyze the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Some uncharacterized homologous sequences are also included in this subfamily. The prototypical member of this subfamily is Escherichia coli RhuK, which exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. Although an intramolecular disulfide bridge is present in Rhuk, disulfide formation is not important to the regulation of RhuK enzymatic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases.	0
NZ_AP019735.1\|WP_019131483.1\|854884_859147_-\|DNA-directed-RNA-polymerase-subunit-beta'	gnl\|CDD\|234794	PRK00566, PRK00566, DNA-directed RNA polymerase subunit beta'; Provisional.	0
NZ_AP019735.1\|WP_026075117.1\|853545_854547_+\|GGGtGRT-protein	gnl\|CDD\|316570	pfam14057, GGGtGRT, GGGtGRT protein. This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are approximately 330 amino acids in length and contain many highly conserved residues including a GGGtGRT motif.	0
NZ_AP019735.1\|WP_019131487.1\|864243_864942_-\|50S-ribosomal-protein-L1	gnl\|CDD\|180071	PRK05424, rplA, 50S ribosomal protein L1; Validated.	1.04238e-142

>NZ_AP019735.1|WP_019131491.1|866324_867512_-|elongation-factor-Tu
MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITTVLAKAGLSELRSFDSIDNAPEEKERGITINTSHVEYQTANRHYAHVDCPGHADYVKNMVTGAAQMDGAILVVAATDGPMPQTNEHVLLARQVNVPKIVVFLNKCDMVDDPEMLDLVEMEVRDLLNKYEYDGDNAPIIRGSALGALNGEPKWEEKVMELMNAVDEYIPLPLRENEKPFLMPVEDVFSITGRGTVVTGRIETGVIKVGDPVEIIGLEEKVLTSTCTGVEMFRKLLDEGEAGDNVGLLMRGIDKKEVKRGMVVAKPGSITPHTKFEAEVYILKKEEGGRHTPFHNKYRPQFYLRTMDVTGEIALPEGVDMVMPGDHVTITVTLIYPVALNEGLRFAIREGGRTVGAGQIIKILE
>NZ_AP019735.1|WP_019131490.1|865988_866186_-|preprotein-translocase-subunit-SecE
MLNYIKESYKELVEKVSWPTFAQLQSSTIVVMVASLIFALVVLVMDISFENLMKGIYSFLGNIGH
>NZ_AP019735.1|WP_026075119.1|865405_865966_-|transcription-termination/antitermination-factor-NusG
MSEIKKQWYVIRAVGGKENKVKEYIESEIRHNHLEDYISQILIPTEKVYTIRNGKKISKEKVSYPGYVLIEAAFVGQIPIIIRNTPNVLGFLGDTKEESRKMIATPLRPQEVSRILGRVDELSEMEEENEVPFFVGETVKVTDGPFSSFQGTIEAVDNERKKLTVSVKIFGRKTPMELSFTQVEKE
>NZ_AP019735.1|WP_019131488.1|864948_865389_-|50S-ribosomal-protein-L11
MAKEVAAFIKLQIKGGAANPSPPVGPALGSKGVNIMDFCKQFNARTQDKAGKVLPVIITVYSDKSFDFVVKQPPVAIQLKEAAKVKSGSAQPNRDKVGEVTWEQIEAIARDKMPDLNCFTVEAAMRMVAGTARSMGINVKGEFPKK
>NZ_AP019735.1|WP_019131487.1|864243_864942_-|50S-ribosomal-protein-L1
MSKLTKNQKNAYAKVEPNKAYKLAEAAALLKEITFTKFDASVDIDVRLGVDPRKANQMVRGVVTLPHGTGKTVRVLVLCTPEKEEEAKAAGADYVGLDEYVEKIKGGWTDVDVIITTPNVMGKVGALGRILGPRGLMPNPKTGTVTMDVAKAVSEVKAGKIDFKVDKFGIVHTSIGKVSFSPEQIVDNANEFLSMIMKLKPSAAKGSYVKSIYLSSTMSPGLQIDAKSVETK
>NZ_AP019735.1|WP_019131486.1|863703_864225_-|50S-ribosomal-protein-L10
MTKEEKAVVINNLAEQLNEYPHFYLTDIETLNAEQTAQLRRKCFENEIKLVVVKNTLFGKALEKAEKADADLMKVLEGSTSVMFATTAKAPAVVIKEFRKKSEKPVLKAAFVEECVYVGDNQLDALCNIKSKEELIGEIVSLLQSPAKNVISALQANAGQKIAGLVKTLEERN
>NZ_AP019735.1|WP_019131485.1|863287_863665_-|50S-ribosomal-protein-L7/L12
MADVKKLAEELVNLTVKEVNELATVLKEEYGIEPAAAAVAVAAPAAGAGEAAAAEKTSFDVILKNAGQSKLQVIKVVKEIAGLSLGDAKALVDGAPKAVKEGVSKEEAESIKGQLEEAGAEVEVK
>NZ_AP019735.1|WP_141412232.1|859182_863043_-|DNA-directed-RNA-polymerase-subunit-beta
MSTNTTQQRISFSTVKNRVPYPDLLEVQLKSFRDFFQMDTTAENRKNEGLYKVFQENFPITDTRNNFVLEFIDYYVDPPRYSIEECLERGLTYSVPLKAKLKLYCTDTEHEDFGVVVQDVYFGTIPYMTERGTFVINGAERVIVSQLHRSPGVFFGQSMHTNGTKLYSARIIPFKGSWIEFATDINNVMYAYIDRKKKLPVTTLLRAIGFEADQQILEIFDLADEVKVTKANLKKAVGRMLAARVLSTWVEDFVDEDTGEVVSIERNNVIVDRETVLQEEHIEQIIESGAKTILLHKENPSGIDFSIIYNTLQKDPCNSEKEAVVYIYRQLRASEPPDEATARDVIEKLFFSDKRYDLGDVGRFRINKKLGLEIDPEIRTLTREDIIAIIKYLIQLINSRAEVDDIDHLSNRRVRTVGEQLSNQFSVGFVRMARTIRERMNVRDNEVFTPVDLINAKTLSSVINSFFGTSQLSQFMDQINPLAEITHKRRLSALGPGGLSRDRAGFEVRDVHYTHYGRLCPIESPEGPNIGLISSLCVYAKISDMGFIETPYRSVNDGVIDLDNSHIRYYSAEEEEGKVVAQSNVPIDDEGHFLQPNRIKARKGADFPVVTDKEVDLMDVAPNQIASIAASLIPFLEHDDANRALMGSNMMRQAVPLVTCEAPIVGTGIEKDMISDSRIQIVAEGDGEVVFADATQIRIKYERTPDEVVCSFAPEVTTYELPRYRRTNQNTSITLKPVVLTGDRVTKGQILTEGYSTQGGELALGRNLKVAYMPWKGYNFEDAIVISERIQREDIFTSVHVDEYIMEVRDTKRGVEELTSDIPNVSEDATKDLDANGIIRIGANVHPGDILIGKITPKGESDPSPEEKLLRAIFGDKAGDVKDASLKAQPSLHGVVIDTKLYSRAGKEAKKSKAAEKAMLEKLDEKFAAEIADLTKLLVQKLWSLVQGKTTTGVTDYFGAELYAAGTKFTQKMLEELSRQTTDERTGVPTGFLNLGSCGWTSDEHVNALIEATINNYTIEWKKADAAIKREKYNLTNGDELPQTGVIQMAKVYIAKKRKLKVGDKMAGRHGNKGIVARIVRDEDMPFLEDGTIVDICLNPLGVPSRMNLGQIYEAVLGWAGRELGVKFATPIFDGASLDQINEYTAEAGIPRSGRTYLYNGETGERFDQPATVGVTYMLKLGHMIDDKMHARSIGPYSLITQQPLGGKAQFGGQRFGEMEVWALEGFGAANILQEILTIKSDDVTGRAKAYEAIVKGDNLPKPGIPEAMNVLLHELRGLALSVKLE
>NZ_AP019735.1|WP_019131483.1|854884_859147_-|DNA-directed-RNA-polymerase-subunit-beta'
MPFNKDNKPAGGYNRISIGLASPEEILAQSSGEVLKPETINYRTYKPERDGLFCERIFGPVKDYECHCGKYKRIRYKGIVCDRCGVEVTEKKVRRERMGHISLVVPVVHIWYFRSLPSKIGYLLGIPSKKLEAIIYYERYVVINPGAAAEQGIERLQTLAEKEYLDVLAALPKGNQSLDDSDPNKFVAQMGAEAIYTLLQQVDLDSMSYALRHKASTETSQQRKSEALKCLNVIESFRASNGLNKPEWMVLKVIPVIPPELRPLVPLDGGRFATSDLNDLYRRVIIRNNRLKRLIEIKAPEVILRNEKRMLQEAVDSLFDNSRKSNAVKNESNRPLKSLSDSLKGKQGRFRQNLLGKRVDYSARSVIVVGPELKMHEMGIPKDMAAELYKPFIIRKLIERGIVKTVKSAKKIIDRKDPVIWGILENVIKGHPVLMNRAPTLHRLGIQAFQPKLIEGKAMQLHPLACTAFNADFDGDQMAVHLPLGNAAILEAQLLMLGSHNVLNPANGAPITVPSQDMVLGLYYITKPRKGVKGEGLVFYGPEEAIIAYNEKRADLHAEVKCMVNDIDENGQRVSVLKDTTIGRILFNQVVPEEVGYINTVLTKKSLRDIIAVVMKKAGADKVAAFLDDIKNMGYRMAFQGGLSFNLDAVIIPEEKEKLVQEGYDRSDAIMEDYNMGLITNNERYNQIIDVWTNINTKLTKVVIDTLVKDQDGFNPVYMMLDSGARGSKEQIRQLSGMRGLMAKPQKSGVEGGQQVIENPILSNFKEGLSVLEYFVSTHGARKGLADTALKTADAGYLTRRLVDVAQDVIINEEDCGTLRGLTATAIKRNDDVVQTLYDRILGRTALNDVIHPLTGEVICKAGQEITEDIAEAIEKSPLESVEIRSVLTCEARHGVCAKCYGRNLATARMVQKGEVVGVIAAQSIGEPGTQLTLRTFHVGGVAGGSVVETNVVSKYEGRLEIEELRTIKGKNAQGEATNVVISRQSEIRIVDPKTEIVLYTHPLPYGATLFMTDGAEVKKGDLICEWDPYNAVIISEFEGKASYENVIEGVTYREERDEQTGLSEKVVIESKDKTKNPVIKIINREGEEVKSYNLPVSAHVVVKDNAKIHAGDILIKIPRAVGKSGGDITGGLPRVTELFEARNPSNPAIVSEIDGEVSFGKIKRGNREIVITSKQGDVKRYLVPLSRQIIVQENDYVKAGSPLSDGAITPSDILRILGPTKVQEYIVNEVQEVYRMQGVKINDKHFEVIVRQMMSKVQIEDPGDTRFFEDQIVDKWEFMDVNDALYDKVVVTDAGDSTSVQPGQIISLRKLRDENSSLKRKDMRQVQVRDIVPATSNQVLQGITRAALQTSSFISAASFQETTKVLNEAAIQGKVDPLENLKENVICGHLIPGGTGLREYDDLLVGLKSDVENLTAAAQ
>NZ_AP019735.1|WP_026075117.1|853545_854547_+|GGGtGRT-protein
MASLFESYERRIDKINAVLAQYGINGVEDAKAICAEKGLDPYKTCEETQPICFENAKWAYVVGAAIAIKKGCKNAADAAEAIGEGLQAFCIPGSVADDRKVGIGHGNLAARLLREETQCFAFLAGHESFAAAEGAIKIAEMANKVRKNPLRVILNGLGKDAAQIISRINGFTYVQTKFDYYTGELAIVKETPYSTGLRGKVRCYGADDVREGVAVMWKEDVDVSITGNSTNPTRFQHPVAGTYKKERVLAGKKYFSVASGGGTGRTLHPDNMAAGPASYGMTDTMGRMHSDAQFAGSSSVPAHVEMMGFLGMGNNPMVGATVAVAVAVEQAMK
>NZ_AP019735.1|WP_141412234.1|868935_869487_+|GNAT-family-N-acetyltransferase
MKTIPILPGIALHELRTADAADIFAAIDGERAYLGRWLPFVQFTRNEEDSLRFVRSVLEASYRETVFTIRDGERFIGLIGFKSTDPLARTTEIGYWLREAWQGRGIVTTAVRALCRMAREELAMRCVAIKCATGNGPSNRIPQRLGFTLDHVEHRAELLEDGRYTDANVYLLNLADRNTSVRP
>NZ_AP019735.1|WP_141412235.1|869527_870046_+|NUDIX-domain-containing-protein
MNRDNSSELFPVVDETGRVVGCATRGECHDGRRLLHPVVHLHLFNSRGELYLQKRPLWKDIQPGRWDTAVGGHVDYGETPDEALRREVREELGVTEFTPERLTQYIFDSVRERELVYVNRTVYDGPVTPSDETDGGRFWTIGEILRTLGTGLFTPNFESEFRRVFLTDDGIA
>NZ_AP019735.1|WP_141412236.1|870022_871906_-|PQQ-binding-like-beta-propeller-repeat-protein
MKQKIVLLLAAALLLCSGVLARRAPRHVVPRAAELNFAFLTDVHVTPRGESDSLLRAAVAEINASAVDFVLVTGDLCNMGSDAELHCVHGILKRLRKPWFAVPGNHETTWSESACTTFGRLFGNDGRLAFRAGGYLFVGFTAGPYMKMADGSVRREDLQWVEERMRAARPGERIVTFCHYPLTNDVTNRTAVTQLLRRYDVRFDLCGHYHTLRLCNFDSIPGLMGRSLIPKNRRQEPAAGYNLVRVWGDSVALYEKRLGEAPRLSFAIPQGNSAALTALPCDPQPAPITYERTGAALVVEDEASIYTGVAVAGDTIFYGTSLGVLKAYDVKNRREVWRRQFGNAVYSTPLAAGGVVVAGDAAGAVWGLDAATGRRLWRIAAKTPVIGDGLVADGWLYMGLGSGSMAKIELRTGRIAWEFRFGEGQPQGRPAVAGGRVVFGAWDTNLYCLDEATGERLWSWNNGSPQKLYSPGHIVPRIVGGRVFIVAPDRCMTALDLATGREIWRVKRRKVRETTGVSADGSAVYAKTMDGELLAVATDADCYMELWTVDAGWGYDHNPCPVEVREGVAYMANRTGCVASVSGDGRLFWAEKFASSAANDFFVDADNRLWVTFIEGKIFCLGDPVVR
>NZ_AP019735.1|WP_141412237.1|872150_872948_-|rhamnulose-1-phosphate-aldolase
MKLIDNESLDRQIGVVAEVAGYLWERGWAERNGGNISVNVTGLCADAVCELPALDGPYPLPKPVPHIAGGCFLVTGTGRRMRYVASQPLANVALIRVAADGASYEIVADEPVRPTSELPAHLSVHDYLIGAGRPERAVVHTHPIELVAMTHNPEFLGKDVLTRLLWSMIPETRAFCPKGLGIVPYTLPGSQELADRTIALLDDYDVVMWTKHGALAIGTDLIEAFDQIDVLSKSAKIYESARSMGFVPTGMSDAEMQELKEVFGL
>NZ_AP019735.1|WP_019131496.1|872956_873985_-|L-rhamnose/proton-symporter-RhaT
MEILIGLLIIAVGSFGQSSSYVPIRKVRDWSWESFWLVQGIFAWIVFPWLGASLALPEGVTLGALWAAGGAWQSVFYGVLWGVGGLTFGLSMRYLGVALGQSIALGTCAAFGTLFPALLAGQNLFRGEGLALLLGVCITLAGIAVIGYAGSLRSRLLSDEERRAAVKDFALTKGLLVALLAGAMSACFSLGLESGAAIQAAAVAAGVKELFALNPVILLVTLGGFATNAAYCIFCNVKNRTGRDYFSVPAGVWVNNVLFCALAGVLWYSQFFGLGMGKSFFAEAPLMLAFSWSILMSLNVLFSNLWGILLHEWRGVDRRTAAVLVTGLLILIFSTVYPQLVK
>NZ_AP019735.1|WP_141412238.1|873986_875141_-|lactaldehyde-reductase
MYRIVLNETSYYGAGCRSVIAEEVRKRGFRKALLVTDKDLIRFGVAEKIERVLADAGIPYEIYSEIKANPTIRNVQQGVEAFKRSGADFMVALGGGSSIDTAKAVGIIVNNPEFADVRSLEGTAATKHRAVPTFAVPTTAGTAAEVTINYVITDEEAKRKMVCVDPNDIPMCAVIDCELMYSMPKGLTAATGMDALTHAVEGYLTPGAWTMSDMFELKAIELIARHLKNAVDDGSDETARAGMAEAQYIAGMGFSNVGLGIVHSMAHPLGAFYDTPHGVANATLLPYVMEYNAESPSRAKYLDIARAMGVKTDGMSVDEGVRAAVDAVKALSLSIRIPQRLHELGVREEDIPALAVAAFNDVCTGGNPRPTSVEEIERLYHIAY
>NZ_AP019735.1|WP_141412239.1|875145_876399_-|L-rhamnose-isomerase
MKTQLIEEAYRIARERYAAVGVDTDEALEKLQRVSLSLHCWQADDVTGFENRGGELTGGIQATGNYPGKARNVEELRADILKAASYIPGTHRLNLHEIYGEFGGEKVDRNEVEVKHFAGWIEWARAHGMKLDFNSTSFSHPKSGSLSLSNPDPEIREFWIEHTRRCRAIAEAMGEAQGDPCIMNLWVHDGSKDLTVNRMLYRELLRDSLDRIFEQKYDHMKDCIESKVFGIGLESYTVGSNDFYIGYGASRGKIVTLDTGHFHPTELVADKLSSLLLFTPEVMLHVSRPVRWDSDHVTIMNDDTLELCKEIVRCDALDRVHIGLDYFDASINRIGAYVIGSRATQKCMMQALLEPLAKLRAYEADGQGFERLALLEESKSLPWNAVWDMFCLKNDVPVGEEFIADVQRYEAEVTSKR
>NZ_AP019735.1|WP_141412240.1|876425_877850_-|rhamnulokinase
MQKNIIGVDLGATSGRVILARAGGDRLRMEELHRFPNRMREIDGRFYWDIHALYEEILRGLSVAGGRGERIDSIGIDTWGVDFACVDPDGDLLGLPRAYRDPYTDGVPEEFFRTVPRESVYAKTGIQVMNFNSLYQLYALNREHNPALAAAEHVLFMPDALSYLLTGEQVCEYTILSTSQLMNPRTRELDGELLRAAGVDASLFARRVMPGERVGVLRDEVARRTGLGRVEVFAVAGHDTASAIAAVPAADERFAYLSSGTWSLMGIELPAPVITEESCAMNFTNEGGVDGTTRFLKNITGMWLLEECRRIWAKEGRTYTYAEIMAMAAAAEPGRTRIDPDDEAFAHPADMPAAIRDWCRGRGKVPPADDAALVRCIFESLAARYGEVLGNLRGVAPFAIERLHVIGGGAQNDLLNQLTADACGIPVVAGPSEATAIGNVMVQARALGLVGSLARMRDYIRRSVEVREFLPRTK
>NZ_AP019735.1|WP_019131500.1|877960_878851_+|AraC-family-transcriptional-regulator
MGSFPQSIVHYLPVTDHDERWGIVCTTAGYQNVPPGSPYPLTQHPDSYSFTRSRGRVLGEYQLLYIVSGQGEFRSASSPAAPVKAGTVVMLFPDEWHTYAPDPETGWEEWWVGFRGENIDRRVAEGFFSPKTPLLHIGHSAGIVSCYQEIIRSAEEERKGFQQLVTGIVLHLLGSVLFKRDNLQYLDNPIVEKINRAREMMRRHIGDNLPPEEIARRLNIGYTWFRRTFRAYVGIAPAQYQLQLRHNKARELLTTTDRTVSEIAAELGFENVSQFSAFFRQREKITATQYRSKYGF
>NZ_AP019735.1|WP_141412241.1|879300_880509_+|L-serine-ammonia-lyase
MKSIKELYRIGTGPSSSHTMAPRRAAEQFLARHPEAAAFRVTLYGSLAATGRGHMTDRAIIDTLLPTAPVDIVWQAREFLPFHPNGMRFQALDTAGTPTDTWTVYSIGGGELAEEGVPPRQAEEIYEMNTLDEILAWCRRTGRTYWEYVEECESDDIWDYLAEIWQAMRESVERGLDHEGVLPGPLHLTRRAATYHVRASGYKQSLQSRGLVFAYALAVAEENASGGRIVTAPTCGSSGVVPAVLYHLQKSRGFSDARIYRALATAGLFGNVVKHNASISGAEVGCQGEVGVACAMAAAAANQLFGGSPSQIEYAAEMGLEHHLGMTCDPVCGLVQIPCIERNAYAAARALDANLYSAFTDGGHRVSFDRVVEVMKQTGHDLPSIYKETGEGGLAREYDPDK

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Crispr_ID: NZ_AP019735_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_5

900984-901083

Orphan

Consensus_repeat	Method
CTTAACGAAAACGTTGGTTTTCTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_5

>merge|NZ_AP019735|5|900984-901083|CRISPRCasFinder
CTTAACGAAAACGTTGGTTTTCTCTCTTCGTTTTCTCGCCTCGGCATAGCCTGAACAAGTTCGGCTCTGCGCTCGGCTTAACGAAAACGTTGGTTTTTCA

>NZ_AP019735|5|5|900984-901083|CRISPRCasFinder
CTTAACGAAAACGTTGGTTTTCTC	TCTTCGTTTTCTCGCCTCGGCATAGCCTGAACAAGTTCGGCTCTGCGCTCGG
CTTAACGAAAACGTTGGTTTTTCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_019131512.1\|893999_895352_-\|BACON-domain-containing-protein	unknown	unknown	gnl\|CDD\|271342
NZ_AP019735.1\|WP_019131515.1\|901118_902054_-\|FecR-domain-containing-protein	unknown	unknown	gnl\|CDD\|226235
NZ_AP019735.1\|WP_019131508.1\|891033_891957_-\|FecR-domain-containing-protein	unknown	unknown	gnl\|CDD\|226235
NZ_AP019735.1\|WP_141413558.1\|887425_890941_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_AP019735.1\|WP_141412247.1\|903020_904190_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|176524
NZ_AP019735.1\|WP_019131524.1\|915902_916796_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238572
NZ_AP019735.1\|WP_019131511.1\|893052_893934_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|176524
NZ_AP019735.1\|WP_141412250.1\|910846_912670_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413560.1\|907753_910750_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_AP019735.1\|WP_141412248.1\|904307_905849_-\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|379837
NZ_AP019735.1\|WP_141413559.1\|897189_900753_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_AP019735.1\|WP_141412249.1\|905932_907741_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_AP019735.1\|WP_141412244.1\|884254_885583_-\|BACON-domain-containing-protein	unknown	unknown	gnl\|CDD\|271342
NZ_AP019735.1\|WP_141412245.1\|885613_887407_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_AP019735.1\|WP_162502211.1\|892199_892682_-\|RNA-polymerase-sigma-70-factor	unknown	unknown	gnl\|CDD\|274376
NZ_AP019735.1\|WP_019131516.1\|902144_902714_-\|RNA-polymerase-sigma-70-factor	unknown	unknown	gnl\|CDD\|274376
NZ_AP019735.1\|WP_141412252.1\|914559_915891_-\|histidine-type-phosphatase	unknown	unknown	gnl\|CDD\|132717
NZ_AP019735.1\|WP_141412246.1\|895377_897171_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_AP019735.1\|WP_141412251.1\|912895_914563_-\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|379837
NZ_AP019735.1\|WP_141412243.1\|882769_884182_-\|Ig-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|367056

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_019131512.1\|893999_895352_-\|BACON-domain-containing-protein	gnl\|CDD\|271342	cd14948, BACON, Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.	1.02891e-07
NZ_AP019735.1\|WP_019131515.1\|901118_902054_-\|FecR-domain-containing-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	2.51261e-39
NZ_AP019735.1\|WP_019131508.1\|891033_891957_-\|FecR-domain-containing-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	2.9594e-31
NZ_AP019735.1\|WP_141413558.1\|887425_890941_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_AP019735.1\|WP_141412247.1\|903020_904190_+\|hypothetical-protein	gnl\|CDD\|176524	cd08582, GDPD_like_2, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.	2.71344e-25
NZ_AP019735.1\|WP_019131524.1\|915902_916796_-\|hypothetical-protein	gnl\|CDD\|238572	cd01167, bac_FRK, Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.	9.70134e-60
NZ_AP019735.1\|WP_019131511.1\|893052_893934_-\|hypothetical-protein	gnl\|CDD\|176524	cd08582, GDPD_like_2, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.	3.29004e-09
NZ_AP019735.1\|WP_141413560.1\|907753_910750_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_AP019735.1\|WP_141412248.1\|904307_905849_-\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	gnl\|CDD\|379837	pfam16370, MetallophosC, C terminal of Calcineurin-like phosphoesterase. This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.	1.32994e-39
NZ_AP019735.1\|WP_141413559.1\|897189_900753_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_AP019735.1\|WP_141412249.1\|905932_907741_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	1.31099e-50
NZ_AP019735.1\|WP_141412244.1\|884254_885583_-\|BACON-domain-containing-protein	gnl\|CDD\|271342	cd14948, BACON, Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.	1.23007e-08
NZ_AP019735.1\|WP_141412245.1\|885613_887407_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	7.95897e-38
NZ_AP019735.1\|WP_162502211.1\|892199_892682_-\|RNA-polymerase-sigma-70-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	7.75652e-38
NZ_AP019735.1\|WP_019131516.1\|902144_902714_-\|RNA-polymerase-sigma-70-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	7.98864e-52
NZ_AP019735.1\|WP_141412252.1\|914559_915891_-\|histidine-type-phosphatase	gnl\|CDD\|132717	cd07061, HP_HAP_like, Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction. Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.	2.76579e-14
NZ_AP019735.1\|WP_141412246.1\|895377_897171_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	6.09551e-33
NZ_AP019735.1\|WP_141412251.1\|912895_914563_-\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	gnl\|CDD\|379837	pfam16370, MetallophosC, C terminal of Calcineurin-like phosphoesterase. This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.	3.76185e-21
NZ_AP019735.1\|WP_141412243.1\|882769_884182_-\|Ig-like-domain-containing-protein	gnl\|CDD\|367056	pfam02368, Big_2, Bacterial Ig-like domain (group 2). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial and phage surface proteins such as intimins.	2.55904e-08

>NZ_AP019735.1|WP_141413559.1|897189_900753_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKKICGRLTRILCTCAVFVSLTGAAYAQSAPVTLDRKKAPVREILNEIERQTDYLFVYSSEQVDFSVSVTAHDEPVQTVLRRIFEGTPIRFTLEGKHIVLRRQPQTAANAAAASPAKQTVTGTVTDTAGKPVVGATVLVKGGTVGTTTDVDGRFSLTIPAGSPLEVSFLGYARQEIATAGRTSLDIRLEEDAATLDEVVVVGYGTMKRRNLVGAVDQVDSRVIGDRSNGNLARSLQGELPGLNISFSDSKPSRSASFNVRGETSIGAGGNALVLIDGVEGSMDAINPQDVESVSVLKDASSTAVYGARGAFGVVLVTTKSPKRGAPEINYNGSVTFNRRTVIPDVITDGLTWVNWWKDSYNGYYNGSKSLLSHIDSTVPYSEAIYQELIRRQADPSLSRTTTLEGDSMFGWAYMESTDWLDLFYKDWNLSHEHNLSISGGNENADYYVSGRFYDMDGIYRVGDESYKKYDLRAKGSLKIRPWFKVTNNTSLAIIDQHEPKHSRNNFAVQRAINHAAMPLSPVKNPDGSWTTAAAISGYAAFSEGTSYRNNDYVYFRNKLSADIDIVKEVLKVQADYSYNYTTRKRIDVQNPVKYSKKPGVYLLESESAGASLSQVDYDTRYQAANAYLTYTPKLGADHDLTVLAGWNIEDQVYKTLTVSRTGFVTPNKPSFSLMNGVAENPTAGGNAWSYVGAFYRVNYGYKGKYLVEVSGRYDGSSKFPIHSKWGFFPSASVAWRISDEPWMGWSRRALDNAKIRFSAGSMGNGNVSPYSYTSEMTVSTADDIVLGGSYPSYTSVGSTVPVSLTWEKSTTYDVGLDLDFFNNRLSVSGDYYRRYTTDMYTASVALPAVYGTGSPKGNNAEMKTDGWELSLSWRDSFKLGGKPFDYSIKAMVWDSKSVITKYVNDTGSLGTVKGFIENGGSPSSYYVGMTVGEIWGYTVAGLFRDQADIDSSAIHDFVQASDKVTRPGQVKIADLDGNGFIDPGNFAVDDHGDLRIIGNQSPRYRYGVNLSARWNGIGLSVFLQGVGARDWYPGSDAGMFWGKYGRPFFALIPSIHNYTDDMYSAERNNWDTAYWPRMTTYQSNGTKNWTRLLEIPNTRYIQSAAYLRVKNIQLDYSFPKHICSAIRLQGLKIYVNAENLFTFTPLHKYAPNFDPEGLSYDSDFASAADGYTYPILKSVTVGVNITF
>NZ_AP019735.1|WP_141412246.1|895377_897171_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKNHIAILIGALALCSCEDYLTQENPNKIESEYYFTDESSLEIYTNGFIRSFATAIKSFVDGDKNADTHSWDGQAAYFMDNYSADDATNWTTSNWSQLRSINYYLDNMRNAVASDAILDHYEGVGRFFRALFYIDKVQTFGAVPWYDTSIDATDREALFKDRDNREFVASKILEDLDYACTYCLTSDKYRVRASYIHRYVALALKARFCLYEGTMRKYHAVDPSTGRAWTKDESRFYLGECVKACEAIMGDGVYKLTDDPAKRQTQYRDMFTNADACGVYTDEFIWARDYDIDLKVTYAINNYMVNPQHANYAFTRQFIDTYLMTDGTPFTSKYPDYDDLDLVAECTDRDYRLAQTIRTPGFTRDGGTTQWAPDVKFSKTGYQPIKWLTDDSSKDTNVAAIASDVPLIRYAEVLLAYAEAKAELGEMSEEVWDKTIKPLRERAGVKSIYPTAADPYMVEYFQNQVTDPFILEVRRERGIELTMENSRYQDIIRWHQGELFARPWKGVWISAVDTPLDLNADGTPETIVTANPKLQSTLNILMIDGASEAGHKLSRGTSGNILPSTALERKWQDYKYVKPIPTTARQENPNLTQNPKW
>NZ_AP019735.1|WP_019131512.1|893999_895352_-|BACON-domain-containing-protein
MKTIDKLSFVPLLALLLFAGSCEKDGGVFMRENDAIACDCTEQSISQNVLCDGEWVADCGDVGWIAITPERGSGNGKDYGFFTLNIQYNSGAERTATVHLVYDGAAYPITVTQGACEFAYGEPRVEGNLFRNIESTATLRLPYVCASGRESVEISCTITGAAADGLSVTKQVYTGFAKGSGELTIPVEGAATRAGAVAFELFADGVSVGSCRANVISDPDAVPEGLPVGWNFYALGMTGTAPRGSEWDYSWTTDAIHPATDTNPLDAHRLLPTAGNENAYLTASGVVSDNGNYTFNPGIQIKGLMENDYFLFVIPVRNIKAEHKLSVEASMGAAGSGPGYYALEYSADNKTWMLAEGSTLMEVFGTSAQVHYYVPKENTSGDRKTYDKSTDKGYRKYVFPLTGMETIYEGNLYLRLRICMDRRANGSESTNTIASAWADLKGFEVALVEE
>NZ_AP019735.1|WP_019131511.1|893052_893934_-|hypothetical-protein
MRSVKKILWSCAVLAVVCGCTKLETPPNKNQPSGDGTGVYKVVAHRGGYQECARPDCSISSLKYAIMLRCFASECDIVLTGDNDVLVAHPQSGYLVNGLEPFDHTVAEIRAAGTLANGEPVPTLRDFIRVLQDPELNPHGMRLWLDVKRLTKNGEEIDVNHSINACYRACEIIKEMKAQSLCEFLIPTGGSIFDVVRDKVIDEYRINLAWMTCTHPDNYGKAWAQLSYDKIFGDNTAYGPMDYISAGVPLSVYNVDDDETMDAVIPYYPKLKAIFTNYPSKLIQKLRAQGYAD
>NZ_AP019735.1|WP_162502211.1|892199_892682_-|RNA-polymerase-sigma-70-factor
MFTLCYDRYHRGIYLFVLKYVRCEALAEDIVQEVFFRLWCNRRGLREEGNLAALLYAMAKNLTVNAIRKHKIVETGNVRYYDLHEGRQEPAGESDSDETMRRLRLAVGELPARQRTIFNLKIYESRSNQEIADMLNVSVNTVKVHYARTMKHLCQRLKKN
>NZ_AP019735.1|WP_019131508.1|891033_891957_-|FecR-domain-containing-protein
MGRKSFEKAGGLSPERIRQMDADIAQALSSERETGGVDVPSLKLLDAIDAKIRRRNRRSVAGAFAAVCLPLVALCLTAFAELYGWGHEPVMRSVQVPAGEHLRVLLADGSAVTLNACSELRYPERFARRRREVRLVRGEAFFEVAHDASAPFTVETDDVSVEVLGTKFNVNAYDKEVTTVYLKEGKVRLTERVTGRQNRYLMAPDEMLAVDRNARTCRAVRPAGKSAPEAWLHNNYAFTNAPLEDVVEFLERHYAVEIEVADARILQYSYTMEFYNETIDEVLSVMSQITPIRYSRVNDRITVQAAR
>NZ_AP019735.1|WP_141413558.1|887425_890941_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MLTLACLFALSGLSAQNVTLRFERAKLKTVMDEITRQCDLSFAYSREVVDADRIVSIDLKDAPIDAALQSLFPSGNGIDYAIKNRKILLSAGKQSLHVDTVVSGRVADDQNRPLVGATVVVAGTSQGTTTDLDGNFSLRVNAVDPVLKVDYLGYEPQELRVSPSQTTFDIRLALSSKAIDDVVVVGYGTVKRRDLVGAVDQVDRKVIEDRSTGTLARALQGQLPGLNITFTDSKPTRGASVNVRGSGSIGAGGSTLVLIDGVEGSINAINPQDVESVSVLKDASSSAVYGARGAFGVVLITTKSAKKGTPVINYNGSVTINRRTVTPDVVTDGLTWINWWKDCYNGYYNGSKALLNHVDSTIPYTETIYQELIRRSQDPSLARTTALSGHDQFGWAYYDSTDWHSLFYKDYNWSTEHNLSISGGGDQADYYISGRFYDMDGIYKVGNDSYKKYDVRAKGTLKVRPWLRLTNNMSVSVIDAYEPKHQKNNSQIPRLINHTAMPLSPVKNPDGTWTAAAAKSGYAAFSEGTSWRTNDYVYLRNKFDVNIDLVKDVLTASADYSYNYTNRKRMDAQTVIEYSKKPGEILYESEAAGSNLQSVEYQTRYQSANAYLNWSPKLGDDHTFKALAGWNIEKQKYETLTIKREGFVTASKPSFGLMNGTTTDPTVGGYIWSYVGAFFRLNYGYKGKYLAEVSGRYDGSSKFPTNSKWGFFPSASVAWRVSEEPWMKWSEEWLDNFKIRLSAGSMGNGNVDPYSYTSEMTVVTASDIVLGGGLPSYTTVGSTVPVSLTWEKSTTYDLGLDLDFLNNRLSFSGDYYRRYTTDMYTPSISLPSVYGTTSPKGNNAELRTTGWELSFTWRDSFKLGGKPFDYSIKAMVWDNRTVVTKYENATRSLGTLKGYIQNGGSPSDFYEGMELGEMWGYTVAGLFRDQADIDSSATHDFTQASDKVTRPGQVKIADLDHNGNIDPGAFTADDHGDLSIIGNINPHYMFGVNLAANWNGIGLSVFLQGVMKRDWYPSPDSGYFWGKYARPFMWVLGIHNYTDDMYSEEKNNWDTAYWPRMTTYQSNSSYSWTKLLEIPNTRYKQNAAYLRVKNIQVDYTFPKALCQKIRLGGLKIYLSGENLFTFTPLHKYAPNFDPEALGYDTDFSSTAGDGYTYPVLKSVTLGVNITF
>NZ_AP019735.1|WP_141412245.1|885613_887407_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKYIAILFACVLFCACEDFLTQENPNKIESEYYFKDESSLEIYANGLTRSFATGIKNFVNGDKNADTHAWDGAAAYFKDNYSASDASNWGTSNWSQLRSINFYLDNMRKADAPEAVLNHYEGVGRFFRALFYYAKVRTFGAVPWYEKSIEATDQEALFKDRDNREYVCRKILADLDYACTYCSTAASYRNQASYIHRYVALALKARFCLYEGTMRKYHTLDPSTGRPWQSDESAMYLGECVKACEAIIGDGVYHLTDNAADRRTQYRAMFIESNATTAYANEIIWARNYDSELNVTHYMNSYFINQQYANYAFTRQFINTYLMTDGTPFTDKYPDYDSVDFTTECSGRDYRLAQTIRTPGFTRDGGTTQWAPDVTFSKTGYQPIKWLTDDSSKDTNTSKCDNDVPLMRYAEVLLNYAEAKAELNEMSEEVWNKTIKPLRERAGVTSIYPTTADPYMVEYFQNQVTDPFILEVRRERGIELTMENVRYDDIIRWHQGELFARPWKGIWIAASETPIDLNGDGVNDCIVTSDPNNKSPLKILFIDGASEAGHKLSQGTSGNILPATAIERKWHDYKYVKPIPTTALQENPNLTQNPEW
>NZ_AP019735.1|WP_141412244.1|884254_885583_-|BACON-domain-containing-protein
MNLFHKIGLAVAASAAFFAACSSDDDPFFARENDYLTFDCNEQTVEQSLQCDGAWSIDYDGNDDWIAVTPDSGVGNGELDFITVGVAYNRGGERTGTIYIDFAGHAYPIHITQGACDFAYGALSSAGTLVRGVESDFTLILAYANANGDESVALSCRMTGASEGLVAADCTFDKFQKGSGTITMPVTGVPAQTGEVFFELLVDGESKGTVKSTVVADPSSIVGGFPVWWDFSSESKPTLMADPHNYSWGAGSQYPCEDSAPSTDHKYLDWSDRGGYLTVVCSTASGWGYGEGHCYMKGLQKDDYWLMAFPVKNLKEGTRIAFEAAVGCSGSGARYYALEYSADGTNWFLAEGAETVTGVDGSTGPAHYTVMTDQALPNDKTPACGWASYTFPVEGCSVTDGLFYVRLRVSLDIRLNASATTYTISKTGSERLKGIVKVSLPE
>NZ_AP019735.1|WP_141412243.1|882769_884182_-|Ig-like-domain-containing-protein
MKTINRMVLLLATLFAAIGCSDDDKELVMYSLRFEPNSITLGIGKSYRLVPISDPFYDDVQYEWKSVDERVATVDQSGVVTGVSAGSTEVRAFYGDNRLARCLVSVVESTSSLPDPTAALSEGLSQQMIFSSNQLPYKGTIMQCFDFYDENGYIYYTQSVGDTKTGNRWMVALGRQKRNEAPSDDYMKLQWFGHGTLLVAERADDGDYVWVNSNGTLSGTDYTNNLTFSRIRYQKGAVLSHYAGDTFYMSEYVDAAGTTWTVRDVQPSIDFVNRRLLIGCRTTDMRHNVIYDLDAVLALGKETVEITRTWGGETAAEGVTEKKTETTSVEVRNLNRLTPLGSFRLPSYLNTGQTHQVYSYSHQGQAVWGDYVYWYEGQAIQQTGELYDGSVAYVAVFDYTGKLVCPRTRVAACSDFPSLSTLLDAKNCYCEGEGMQLKQGRKLYLGIATHTSAASGNRLASILQYECDVE
>NZ_AP019735.1|WP_019131515.1|901118_902054_-|FecR-domain-containing-protein
MERDLLYRYFDGDTTPDEERRIMEWAEASPENYRLYLEERRLWCALLLHAGRRTARRPALWRRLAAWRVSGAAACILLLVGLAGIFFAGRMVPDGRMQQVVVPAGQRVELRLADGTKVWLNSKSRLEYPSSFGRRSRRVTLCGEGYFEVAHDERKPFVVETGQYDVRVLGTTFNVYAYDNDRAAFETALMEGSVEVSSRSDASQRLVLQPNEAAVMAADGRLVRTRLTDMGRFRWTEGLICLNDVPFGELLERFSDYYDIRILLKNPKLYDVRCTGKFRQSDGIDYSLHVLQRFVNFRYTHDEERHTIEIR
>NZ_AP019735.1|WP_019131516.1|902144_902714_-|RNA-polymerase-sigma-70-factor
MDGSENRDCGLFTVLFEQYREPFTRFANSFVRDRAVSENLFVDALVDYWQRRGSLPEDTNVPAYLLTSVRNKALNHLRHQRIRERSSDELMRRARSELDFRISSLEDFTTQSLFSSEIHEIVRQTLAEMPAQTRRIFEMSRFENRRNAEIAAELNLSIKTVEFHIGKVLKVLRVRLKDYLLFFFVFILR
>NZ_AP019735.1|WP_141412247.1|903020_904190_+|hypothetical-protein
MKNTLLFLFAALAWSATALCQTPADSAARPRKRVFIAHRGVNMRSTVAGENSLEAIRLAKAAGFGAIETDVRLSADGALVVMHDSTLNRTCLHADGTPLSEPVAVAGKTLRELRSDYILKAADPARRTRIPTLEEYLAECARNGLYTFIEPKLYDPTGRHYRDIVAAADAALGRDRYVVTSNNRANDVIRRTGIDDVRLMGILYQTTFERIEALGDVIVAVSATRFDEADYSRQVARAKAAGLMCESHADKFVHFDRINRHDIDFVSTDFLAPDYRGQGRLLAEYARTDGFVLPASAGEGAIRLGEGQSIVPKRQLPAVPFGALYLELEAEGSARIELGGQTFTLDVPDKRTVTHQVLLHDAAPALRITALAGGITLTAIRAKVVAFEQ
>NZ_AP019735.1|WP_141412248.1|904307_905849_-|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein
MYMRTRYFIAGILLLALFAGCSSDSGEGDAPGGGSGDLYGYVRDASGSAIEGVVVSDGYTCTVTGADGRYAMQRHPNAYYVYYSTPADCKVEVDPSTGLPLFYQKIRKSQPQYDFTLTRQAEETKFRMLAIGDPQVTTTAQVYRFETETVADINSYVAAQTDGLPTYAITLGDIVGNKWELYPDMVKAMARSKTSVPVFQTIGNHDHEFPQVTDLSAQRRYEASFGPVNYSFTRGDVHFVSMDDIIHKATGSDAYTSGFLDWQFEWLKQDLSYVPRTCAVVLCVHIPFRGGFNGAGETYFDEVLELLAQFDRAWIFSAHTHNNKTNYTHAVGSKKIREYILGTSCGAWWHGTVCTDGAPNGYGVFEYDGTSLTNMIYKPTRYDETFQIRLYNGEDVFTGGTAKSWKFDLQQPKNRLMANVWNADDTWTIEVYENGVKTGDMAKKSMIDPWSSAYFCGFCGLKESYASKNDHIFYYTVKSPGAALRVVARDGYGNVFEQTEITTPLEADYPDAY
>NZ_AP019735.1|WP_141412249.1|905932_907741_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MLKKIIYLIVSGGLLLSGCSLDYEPLNGPSSGSFPASEEEAMAGLYAAYKGLANMTVKETPFPMRINDCISDIGTYRTGAGNQIKAMSSTLTADNTMCEKVYKTVYKIAGRVHLVLDNLDRLRGVIPEDRFNQIKAELLCIRAYYYDLGCQFYGDIPFIDHQLDLDDYSDYPRIPREQVTARLLQDLDDDLLDYLPVQWNPGTFGTTRIGRVAAYALKARIALNWGLWEEAARCSKIATTLAEGVYDLEPLDCTYYATHADGEPSAANLFGFAGQTSREWLWAIQYNRLINYTSATYYEAPRIHGGCSWLGPSQAMIDTFQCTDGKPITESPLYDWQNPWANRDPRLDLFCLRPDTRLWGVQYDTDVRVEKVKDYNQSTAGKEVLISNADAVGNKSEYAANGSKGPGGYLWRKYSDKGMMGLVNGTKTEDDINAGIIRFAELLLIEAEANIEWDGGDLAIAEANINRVRARVNMPPVTDRSREGLRKALRYERKAELCNEGFRWFDIRRWKIASKAVNGPMYAPGYSTVQNPGNYISNVKPSFDDDWVVTYDLSDTWDGKTGNLRVFQTMVFNPEKDYLWPIPYTELVTNPAIGVENQNPGY
>NZ_AP019735.1|WP_141413560.1|907753_910750_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MYAQKSQLSGTVSDAENIPLVGASIIVEGTHVGTTTDADGAFRLPAAPGQRLTVSYLGYKSKTVTVGSRTSLDIILESDNSLINEVVVVGYDTQKKVNLTGSVASVSAEDLANRPIVSSSTALQGIAPGVTVTTQSGAPGGDGGMIRVRGIGTFGGSSAAPLVLIDGVEGSLDAVDATQIDQISVLKDAASSAIYGSRAANGVILVTTKRGKKGQTSVTYRGYVGWQSPTDTPETVSAEEYMILSRETSFNDGKESIYTDDYIARYRENNRIDPDNYPLTDWQDQILTGSGFTHNHNLSLTASTERVRVMTSFGYLDQKGIIKRTDYQRYNVRNNMNIDFSDKLSMRFDVSFVNGDRRRIPQQNTLFNYMNTRDPLILSRWSTGYWAGLSGGSTNVLPTLEGEGGNVKNNTIRLNGAVTLTFKPVKWLTLEGMVAPRYVTTNNHTFVKKMKFYSDAFGTVSNSSNVAFNYLDESANRSFYGNYQFTAALQHTFAQNHNFKLLLGASRETYDNKTLSAHREDFAYPDYEVIGAGADNETKDNGGGHAQWALQSFFGRLNYNFKERYLFEANVRFDGSSRFAKGNRWGIFPSFSGAWRLTEEPFMQDVRRTLSEFKIRASYGQLGNQNIGSNYPTIQQLDVSSISVNDVITPIVTQTTLANPDITWESTEMYDVGIDATLFDKLSVTADWYYKKTHDILLTLDIPSIIGLGAPYQNAGTVRNVGWEVAVGYHNKWRDFSFGVEANLSDVVNKIIDMKGTTGGSGAIRNQEGSAINSIYGLKCVGMARTQEEADWVNENCPQYGVTTKPGDLIYADMDDSGTIDDKDMTIIGSTVPRYTYGVNLSFGWKGLNLSAFFQGVGKVDGYLSSYYVQPCQQGGTFRKEHLDRWNETNPNGKYPRLTMTDANNWKQSSFWMRSAAYCRLKNIQLSYTLPRTWLKKLRMKSAMVFVNAQNLFTITDFYQGFDPEVAYSGSGDGVELGAVAYNYPQVKVVTMGVELKF
>NZ_AP019735.1|WP_141412250.1|910846_912670_-|hypothetical-protein
MIRNLLPWTAGCLLAAFSVSSCESDDVDYGPISAAIEIGVEEVTPSSAKIRLTTEQENVASYKIVKPTPISEFEYAAHDAIDRLAFIEERGEAAEAPFEQTLAGLMPKVEYSFAVVGLDASGQRITAPTFARFTTAYASSLVEARFETNPDETFTFTGKITPNAYTVSYRYIFDSDHNEATEAELRELLEAGGSGVKTDKGVKELELVKSDKTGVTLAVLSYDDANRPGEFTSTFVSTEDMASVIVDGKETQLARPTEGVDIFEGKVAVPAKSGFTVEINKVAYGFAPYSGNGGVGKVENMMSAAPYYSSSTIADSRGYDCKMAVGRMAATADGGNDFWTNLSEDAQILVRVDLTYADGTPRYWLELVEADDPNLLLEQNFDLFVWGGDYTLASGGKGTAPVADSESAADLDGTEEGTKGGATYTTPKPDIWSTADGAADGDVIAGDLYLKNRNMTGWEVRRIAEHPGTVRLNKSASGSHKYSGYLKTPKLAALTAPTNITLEFDICRFAGDGDIYITVEGAGTYTAAAVNIDGAAAATTVAASGTDFVVTNDLCSKQANTVINKPWSHVELSIAGATAETQIKFDGSRGKDSASDRCLLDNIKITK
>NZ_AP019735.1|WP_141412251.1|912895_914563_-|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein
MKPIRKMRLFAAALAVACLLAATVRTVAAGRGKAVLTGVVYGDGAPLAGVCVSDGVQFATTDAAGRYRIESDKSAGFVFAVTPSNWVAAEADGVQPLFWAALDEADARDEQHDFHFASVDQSRYTVMFFTDLHLTNSSEKRDLDHYRSIALASISDEAAQASARGPVYSLNLGDLSHDLYWYQYDFDVSSAKRFLEQNGFPTLLYSIPGNHDNDGATPAGAGVDRRAEHLYRRTFGPTYYAMNIGDVHWIMMDNIIYKNTPGKGKKNVGVVGARDYDKGFTPEQLAWLRRDLATVDASKTVCLCTHCPVFFDRDRRTLLTDRSQVDSLDALFSRFERVHIFSGHAHRTLYTQDADYPRFDQYVLPATSGDMWVANNDFQALCPDGSDAGFVVASVDGGKLRCDYRTHLYDRKVLRAYDMNAVGEYYRNDSLVRVQRRLYPDRADYGREEYANCVYVNYWGYLPGHRVELFEEGRSLEVVQVEDEDPLYNISHYLPELARKPVFKKGDARVVSHHMFAARARTATAPVEIRITDADGVLLHRETLERPKKFDKEAR
>NZ_AP019735.1|WP_141412252.1|914559_915891_-|histidine-type-phosphatase
MNFISIFRRLFLPLVVLLLAATADAQSAYDEIKADIDKAGGVYFMYPFDTPSATPAPKGYEPFYISHYGRHGARYILSNDQYDNVAEVLRRARADGKLTARGIDACDRFLAIYPHLKGRAGDLTPKGQMQHRRLAGRMYAAYPEIFRRHPRIEAYSTVVPRCIMSMAAFCEGLKEADPSLEIFTETSSVNMYYLNPHSTGNPAGTAEDFRYKSADAPWRPEWRRFCEERIDVETILARLFTDTAYARSICDPLKFEQDLFSVAAHMQCTDLDESFYDLFTFDELCRFWECDNYTYYVEKGPDPRNRGRGTALAETLLDDIVSRAGEDMAAGEPSVRLRFGHDGCIMALLTLMRIDGWTTPVTDPAKIKDVWQVHRIPMASNMQFVFYRNKKNPDDVLVRVLLNEKELRLPLPGDRAPYYRWEDFRDFYAGIVREARLKLEATK
>NZ_AP019735.1|WP_019131524.1|915902_916796_-|hypothetical-protein
MGKPKIVGIGELLWDVLPAGRRLGGAPVNFAFYAQEQGAEACIVSAVGQDASGDELLGGIAALGLGVRAVQRNAHPTSTVEVTLDAAGVPAYRIREQVAWDYIERTAEADAAVAGAAVVCWGSLAQRNAVSRRTILALVDAAPVGCLRLFDINLRLNYYDERIVRDSLERADILKLNEDELPVVARFFGLEGAAERVVAQLVERFSLRYVVFTEGGRGSRVTAADGRTSYLATPRVEVADTVGAGDAFTATFAASLMQGLPMEECHRRAVAVAAFVCTRHGAIAPLSEFMKTEITNR

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Crispr_ID: NZ_AP019735_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_6

1081922-1082059

Orphan

Consensus_repeat	Method
GCGGAAAGTGGTGCAAAGGTAAAACCTTTTTTCGAATCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_6

>merge|NZ_AP019735|6|1081922-1082059|CRISPRCasFinder
GCGGAAAGTGGTGCAAAGGTAAAACCTTTTTTCGAATCCGCCAAATTTTTGAAGAACTTTTTTCGAAGCTTTTTCAAAACCTCTCCGCCTGTTTTCGGGGCGGAAAGTGGCGCAAAGGTAAAACCTTTTTTCGAATCC

>NZ_AP019735|6|6|1081922-1082059|CRISPRCasFinder
GCGGAAAGTGGTGCAAAGGTAAAACCTTTTTTCGAATCC	GCCAAATTTTTGAAGAACTTTTTTCGAAGCTTTTTCAAAACCTCTCCGCCTGTTTTCGGG
GCGGAAAGTGGCGCAAAGGTAAAACCTTTTTTCGAATCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_019130949.1\|1085496_1086882_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019131622.1\|1071808_1074184_+\|BamA/TamA-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|227116
NZ_AP019735.1\|WP_141412331.1\|1091264_1092296_+\|FecR-domain-containing-protein	unknown	unknown	gnl\|CDD\|226235
NZ_AP019735.1\|WP_141412320.1\|1067556_1068060_+\|OmpH-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|377167
NZ_AP019735.1\|WP_141412330.1\|1089075_1089954_+\|DUF4249-family-protein	unknown	unknown	gnl\|CDD\|379442
NZ_AP019735.1\|WP_141412322.1\|1070040_1071063_+\|diaminopimelate-epimerase	unknown	unknown	gnl\|CDD\|234768
NZ_AP019735.1\|WP_141412328.1\|1084788_1085394_+\|signal-peptidase-II	unknown	unknown	gnl\|CDD\|237816
NZ_AP019735.1\|WP_019131619.1\|1069685_1069895_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019131617.1\|1068089_1068653_+\|OmpH-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|377167
NZ_AP019735.1\|WP_019130946.1\|1090595_1091195_+\|RNA-polymerase-sigma-70-factor	unknown	unknown	gnl\|CDD\|274376
NZ_AP019735.1\|WP_141412334.1\|1097812_1099126_+\|BACON-domain-containing-protein	unknown	unknown	gnl\|CDD\|271342
NZ_AP019735.1\|WP_141412323.1\|1071055_1071802_+\|nitroreductase-family-protein	unknown	unknown	gnl\|CDD\|380322
NZ_AP019735.1\|WP_162502269.1\|1082327_1084364_-\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173811
NZ_AP019735.1\|WP_141412319.1\|1064902_1067488_+\|outer-membrane-protein-assembly-factor-BamA	unknown	unknown	gnl\|CDD\|274514
NZ_AP019735.1\|WP_162502270.1\|1086947_1089068_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|366183
NZ_AP019735.1\|WP_141412324.1\|1074610_1075156_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412325.1\|1075233_1076454_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340895
NZ_AP019735.1\|WP_141412321.1\|1068739_1069600_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_AP019735.1\|WP_141412332.1\|1092410_1095977_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_AP019735.1\|WP_141412333.1\|1095996_1097784_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_019131622.1\|1071808_1074184_+\|BamA/TamA-family-outer-membrane-protein	gnl\|CDD\|227116	COG4775, COG4775, Outer membrane protein/protective antigen OMA87 [Cell envelope biogenesis, outer membrane].	6.531e-30
NZ_AP019735.1\|WP_141412331.1\|1091264_1092296_+\|FecR-domain-containing-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	4.88926e-27
NZ_AP019735.1\|WP_141412320.1\|1067556_1068060_+\|OmpH-family-outer-membrane-protein	gnl\|CDD\|377167	pfam03938, OmpH, Outer membrane protein (OmpH-like). This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.	2.6266e-24
NZ_AP019735.1\|WP_141412330.1\|1089075_1089954_+\|DUF4249-family-protein	gnl\|CDD\|379442	pfam14054, DUF4249, Domain of unknown function (DUF4249). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 279 and 365 amino acids in length. There are two completely conserved residues (C and G) that may be functionally important.	3.08156e-22
NZ_AP019735.1\|WP_141412322.1\|1070040_1071063_+\|diaminopimelate-epimerase	gnl\|CDD\|234768	PRK00450, dapF, diaminopimelate epimerase; Provisional.	3.18009e-47
NZ_AP019735.1\|WP_141412328.1\|1084788_1085394_+\|signal-peptidase-II	gnl\|CDD\|237816	PRK14788, PRK14788, lipoprotein signal peptidase; Provisional.	2.74833e-59
NZ_AP019735.1\|WP_019131617.1\|1068089_1068653_+\|OmpH-family-outer-membrane-protein	gnl\|CDD\|377167	pfam03938, OmpH, Outer membrane protein (OmpH-like). This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.	3.28524e-22
NZ_AP019735.1\|WP_019130946.1\|1090595_1091195_+\|RNA-polymerase-sigma-70-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	1.97754e-44
NZ_AP019735.1\|WP_141412334.1\|1097812_1099126_+\|BACON-domain-containing-protein	gnl\|CDD\|271342	cd14948, BACON, Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.	1.99915e-10
NZ_AP019735.1\|WP_141412323.1\|1071055_1071802_+\|nitroreductase-family-protein	gnl\|CDD\|380322	cd02146, NfsA-like, nitroreductase similar to Escherichia coli NfsA. This family contains NADPH-dependent flavin reductase and oxygen-insensitive nitroreductase. These enzymes are homodimeric flavoproteins that contain one FMN per monomer as a cofactor. Flavin reductase catalyzes the reduction of flavin by using NADPH as an electron donor. Oxygen-insensitive nitroreductase, such as NfsA protein in Escherichia coli, catalyzes reduction of nitrocompounds using NADPH as electron donor.	1.28724e-67
NZ_AP019735.1\|WP_162502269.1\|1082327_1084364_-\|S8-family-serine-peptidase	gnl\|CDD\|173811	cd07485, Peptidases_S8_Fervidolysin_like, Peptidase S8 family domain in Fervidolysin. Fervidolysin found in Fervidobacterium pennivorans is an extracellular subtilisin-like keratinase. It is contains a signal peptide, a propeptide, and a catalytic region. The tertiary structure of fervidolysin is similar to that of subtilisin. It contains a Asp/His/Ser catalytic triad and is a member of the peptidase S8 (subtilisin and kexin) family. The catalytic triad is similar to that found in trypsin-like proteases, but it does not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.	2.71294e-70
NZ_AP019735.1\|WP_141412319.1\|1064902_1067488_+\|outer-membrane-protein-assembly-factor-BamA	gnl\|CDD\|274514	TIGR03303, OM_YaeT, outer membrane protein assembly complex, YaeT protein. Members of this protein family are the YaeT protein of the YaeT/YfiO complex for assembling proteins into the outer membrane of Gram-negative bacteria. This protein is similar in sequence and function to a non-essential paralog, YtfM, that is also in the Omp85 family. Members of this family typically have five tandem copies of the surface antigen variable number repeat (pfam07244), followed by an outer membrane beta-barrel domain (pfam01103), while the YtfM family typically has a single pfam07244 repeat. [Protein fate, Protein and peptide secretion and trafficking].	6.40576e-95
NZ_AP019735.1\|WP_162502270.1\|1086947_1089068_+\|TonB-dependent-receptor	gnl\|CDD\|366183	pfam00593, TonB_dep_Rec, TonB dependent receptor. This model now only covers the conserved part of the barrel structure.	1.20186e-15
NZ_AP019735.1\|WP_141412325.1\|1075233_1076454_-\|MFS-transporter	gnl\|CDD\|340895	cd17337, MFS_CsbX, CsbX family of the Major Facilitator Superfamily of transporters. The CsbX family is composed of Bacillus subtilis CsbX protein (also named alpha-ketoglutarate permease), Klebsiella pneumoniae D-arabinitol transporter (DalT), and similar proteins. The csbX gene is a sigmaB-controlled gene that is expressed during the stationary phase of cell growth. DalT is a pentose-specific ion symporter for D-arabinitol uptake. Most members of this family remain uncharacterized. The CsbX family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	6.89031e-173
NZ_AP019735.1\|WP_141412321.1\|1068739_1069600_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	8.97676e-32
NZ_AP019735.1\|WP_141412332.1\|1092410_1095977_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_AP019735.1\|WP_141412333.1\|1095996_1097784_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	7.78693e-42

>NZ_AP019735.1|WP_141412325.1|1075233_1076454_-|MFS-transporter
MTTFYDKTGLPKSLAWGFIGVLIFMMGDGIEQTWLSRYIASQGLDHEVLFTVYGISVALSAWFSGVIAETIGVRRTMLLGYLVYLVGMAGFAGIGMMGLNYPVLLVTYAIKGLGYPLFAYTFIVWIAYRVDKSRLSSAQGWFWFVFTGGLNVLGAYYGAYAMERIGVVPTLWSSLVFASVGAVLALWVNKCDDRNLFVGAERPSSGTSKFRELLSGLAIMKREPKVLVGGIVRVINTTSQFAFVVFMPLYLKDYGIGDTQWASIWGSIFLFNILFNLIFGIVGDHIGWGRTIVWFGGVGCAVSVLLFFYAPVICNNFWFILACGALWCIMLAGYVPLSALVPSLVDKDKGAAVSVLNLGAGLAAFVGPLIVALFRNAIGYVGIVWFMAGLYILSAVMTYCIAPRNR
>NZ_AP019735.1|WP_141412324.1|1074610_1075156_+|hypothetical-protein
MKLFHYLPVGAYAAAAALLLASCGVSKRSLKQSNRALTAALQASAQKEQAEALKLYSDTSIPQGEARKSVSRDNPGQTALEQTIIRWAIDSDPQGARVFYRVLSSIPAVVKNTNETYLMTTPYEETRAFNILGLTYENSRDVQIEIKVVKTGYEAQVKRFNVRQAIDQQEISSFFMLVPKE
>NZ_AP019735.1|WP_019131622.1|1071808_1074184_+|BamA/TamA-family-outer-membrane-protein
MRRLYPIAVAALCILCTACSVVRKLPEGSYLVQKVTIEDDRNVPKKERITASELDRYVWQSPNKRFLGTNFYVWVYNQSNPDKDNWWNRFKRKIGEKPVVYDPALTLKSAENLKAYMESHGFFSSRVRYHVDTTSRRKRAIITYRTEQGPPSRYGKINYEFNDKFIEKIILQDTASTLIRPGGIFNSATLDAERERITRYLRDRGYYNFSVNNISYRYPYDTVGSRVGDLTMVVKQYLTGYNDRGEPVMENNKVYRISEINMLPGYDPTVSFTDREVRYDTVAYRGLNVVYDGKHNVRPRVLRQAIPLYPNYLYNAEQINRTYNNIMSLGYFKSTRITFDELPAPDSTNLVSYIGNADDSLATQYTQEGYLRCNILGTPQLKQSYKIDLEGTTTSSFYGLKASVGYQNRNLFRGMESFDIAFSIGHEFMKSRDSGKRNAKEFGVTAGLAFPRFLLPFFSSRYRPSLVTPRTRLELSFNYQDRPYYRRTLTSMTWTYSWSNEKYSSFAVRPVDLNLVDMSYINQDFFEKLQNLYLRNSYTSQLVAGISGSYTYNNQLKNPGRNATLVRFNWETAGNLIGGLEHLFSSPAKGKDYYEIFGIQYSQYFRVDLSASRKIMLGEKAAIAGRLYAGCGLAYGNSTSIPFDRLFYCGGSNGMRGWIPRMLGPGSVPVDPDKVTYPVQLGDMKLEANLEFRFPIWGIFHGATFFDVGNIWFMGNSAEEYPPEAVFHIRDFYKQLGFNTGLGIRLDIKFAVLRLDWGIQLHNPNNPAGKRWIHDFKWSNTALNFGVGYPF
>NZ_AP019735.1|WP_141412323.1|1071055_1071802_+|nitroreductase-family-protein
MIKEIANHRSIRKYKSSPIDEEVLSDILHSAARASTCGNMQLYSLVVTLDARVRAELAPCHFNQAMVTEAPCVVTVCADVHRFSKWCEQRDAEPAYDNFEWFLNAATDALLAAENLALAAEAHGLGVCFLGTTLYTARDICRILHLPKGVIPLTTVVIGHPAEQPPLTDRLPLDAVVHYDRYKDYTDAEIDELWAEKEASPETSALLAENGLPNLAQIFTRNRYRREDNIAISRAYFELLREQGFFNQ
>NZ_AP019735.1|WP_141412322.1|1070040_1071063_+|diaminopimelate-epimerase
MKIYDYILCSGSGNRFLLFDTLRSDLSGLNIAAFAAEELHRFGVDGLLLLTRDGRGRFGMRMFNTDGSEAEMCGNGIRCVARLARERYPEATGERFAVTSGGREYRITCEEPIFGALPTFGAEIPLSLHGDDFPPSLPAEGFVGQPVPELDEGLAFTFLQPGNPHIVALVAPDSAWLFGSDGRLDTRRLAELGERANRMRGVFPRGINVSLFCRLDEGRIFAATYERGVGITSSCGTAMTSCATAAALLGLAGFDTTVEVWNRGGRVRCLPRRTQQGIVTRLTGDASFETAGRLRLDGKECIATGDASPLDPPCDRLRLTEETLRELHEKYGLTIADDHD
>NZ_AP019735.1|WP_019131619.1|1069685_1069895_-|hypothetical-protein
MKADRNFRRNGSADAEEVFKRATKLAPNRKSGKERHSLYTQFDEEEEDAAFGYKAKQESVLDYYDDGEE
>NZ_AP019735.1|WP_141412321.1|1068739_1069600_-|alpha/beta-fold-hydrolase
MIEKFIMAGRTALHVCDSQQGERCVVLLHGYLESMFVWDDFVPLLYKRVRVVTLDLPGHGISEVRGECHSMEYLADVVRDALQALGIARCTLVGHSMGGYVALAFCERHPEMLDGLVLFSSTPNADTEEKRENRRREIALVRAGKKEQLARVAPGAGFAADNRQRMADAIADLTEQVYLTEDDGIVALLNGMIARPDRNEMLRRSPVRQLFVFGRKDEYIPAAVAEQLAAAHPQAQVVWLADSGHMGFLEEPEAAAEALLRFVGAEPDGQTAASVAGASEMPAAEA
>NZ_AP019735.1|WP_019131617.1|1068089_1068653_+|OmpH-family-outer-membrane-protein
MKKILKIVLTVAFVAGSTSVFAQKLGRINMQELVFAMPETAEMQKNLEAYQKELQDQLETIGVEFNNKLNEYTKQVSDKNSTMSDSVRQLKEKELNDLKTRYDEFVQVSQQDMQKKQGELLEPIIVKAQDAVKEVSKAGGYTVVYDTSVNAVAYFDEAVVTDILPAVKTKLGIKDTPAAAPAAPAAK
>NZ_AP019735.1|WP_141412320.1|1067556_1068060_+|OmpH-family-outer-membrane-protein
MKRLFLTVVLAAAGWCAYAQNYMIVDSEKIFKSIDAYNTAIKDLDKMAEDYQKQVDDKFAEIETLYNNYQQQKASLSATTRQVLEDTILSKEKDATALQESLFGKDGTLMKKRLELIQPIQKKVFDAINAYAQSHGYDLVLDSASNPTLLYNAPKLDQTEGVIKSLK
>NZ_AP019735.1|WP_141412319.1|1064902_1067488_+|outer-membrane-protein-assembly-factor-BamA
MNRLRKICLAIAAPLFCVSGIFAQEKNPADTTAVTTPAAPQDAASDDTEETLPPFDEKAPIMKGKPKRYFIRKINLRGIEYLNKTVVQASTGLVPGDSIYLPSENIADVIAKLWNQRLFADVKVGATIDGDSVDMEISVRERPRVYRWLFEGEGVGKGRQKDIIEKLQLKTGGELSDYVIDKNTKLIKKYFAEKAFRNAEVSVRIENDPVIQNAVNVTFVIDRKRKVKIGKINFHGNEQFKDKRLRRTFKKTHQKSINFFKSSKLKEDDYETDKENLIDFYNSKGYRNFTILSDSIYPINDRRLGIDLSVSEGNKYYIRNITWVGNSVYPTSDLQRMFGVKSGDTYDKKTINKRLGYGKEDNPEDMSIKSLYQNNGYLMSQIEPAEIIIGADSIDMEMKIFEGKQFSINNVGISGNMRVNDEVIRRELYTLPGELYNRALLMQTIRQLAGMGHFDQEKIMPDIKPVSNELVDINWPLEEQASDQFNIAGGWGSGTFVGSVGITLNNLSVRNFFKKGAWRPYPMGQNQKFSISAQTNGTYYKALAMSFTDPWLGGRKPNSFTLSVHLSEQNNAYYFWQTSTQHFRTTGVAAGLGKRLRWPDPNFSFYAEASYERYALKNWDYFVMKNGAANTLALKFVLSRSTVSQPIYPRSGSEFTVSVQLTPPYSLWDGKDYADANLPDEERYHWIEYHKWQLKSKWFFPLTNNQNLVLMAAAEMGYLGHYNKNKVSPFERFEVGGDGMSGYNMYGIDIIAVRGYEEGALDPSNNYSVAYNKYTMELRYPVILKPSSQIYVLGFLEGANAFDSWKQFSPFKIKRAAGFGVRLYLPVVGMLGIDWGYGFDAPANQTGKSGSQIHFMMGQQF
>NZ_AP019735.1|WP_162502269.1|1082327_1084364_-|S8-family-serine-peptidase
MMKKILLLAGIVSLAACTNDPEETFSQGGGSSAGVKVIYDAEGAVEGQLIVKFRPSAADSLAAALASASATRAGFATADELLAAVGVDGIRPLFGSDPRFEERHRAFGLHQWYVVTFDESLPLREMVGELSHDGRIEVLEYARCPRLKNRFPARPLRSAAAAATRASMPMNDPLLPAQWHYDNTGYQVLVTQAGADVNLFDAWKKNQGSSDIVVAVIDQAVQYTHPDLQANIWVNPNPEDDDLHGYNFVNNTAELDWSYADREEYQGQIYYSNADHGTHVAGTIAAVNDNDRGVCGIAGGRNGAGGVKIMSCQIFGDPDKRSYPTEDAFRYAADNGALICQCSYGYSYSTGSRDEMEAMRQWFMNSSEKAAIDYFIANAGKNDPDSPIEGGVVIFAAGNDGDLFGDVSEYPASYEAVVSVAAMGSDFLPAYYTCYNDEVDITAPGGDLYNSSLGTDNGGVLSTILSDPSVTYYDDERRQGLTDSNVYGYMQGTSMACPHVSGVAALGLSYLSQLGYRMTADAYKKLLLESVHPIDPYLTGTKRYDGPTLLLDEYKGKMGAGYLDANLLLENIKVAFGEKTPPRVTARIANRLLKTDTPTSSVALADYFTDDAVSQYDAVANDESVVRVNVSDGVLRMLPKKVGQARVTVSARGFEGTVVSQSFYVTVRSQSNSADGWL
>NZ_AP019735.1|WP_141412328.1|1084788_1085394_+|signal-peptidase-II
MNFKKITILLLVLLVADQALKIWIKTHMTLDEAIMVVPTWFQLRFIENNGAAFGMRLATGGAFDWGKLALSLFRLAMIGLLGYYLRYLGKRKTPAGVLVGLTLILAGAIGNMIDSAFYGLIFSASTPTEVAHFGGSYAPLMMGRVVDMFYFPLFQWNGVPGWLSFLVDSRNYFFGAIFNLADAYISVAVVYLLIFQYKFFK
>NZ_AP019735.1|WP_019130949.1|1085496_1086882_+|hypothetical-protein
MKKILLCLALFCLATGPISCGDSNTDDGTEQGGGGNGGDGGGTGPEPEPGNPEITPEQHKAKLETIGKEVAAQFNPEDSKAAIESLTALEELLAFDDEDVAPSPAPKTYAVATAKSLAAVAAGPDVHALTSLIVRATTTEKYTLDEWAGDYVIEDGEPVKKGELANQYRLTWADAAGTQSEALFTYSAGGVEYTRVDGYAIVIPQDWNLSLKVAGHEELSVVGKSNVSADGLTLAPEVTVTLNGGYVAAAKVNADPKQVTANASFTKNGTQIVDAYAKMVCDGLTDPDNWIVEEEYDWNGDGVIDDTDTYIDPEDHIVDHVKTGEGYVTVMGLKLTLSGDIAKIIQQVNAIADTSTATGSQQEADAYNTNAKAKLAYTADNSTMADVKMQSYSYKDYIYVWNPDTQTGDNQVVTRYDIEPVLEFADGSKIAIEEYVETGFDSLTKTFEDLADAYMDLIDGK
>NZ_AP019735.1|WP_162502270.1|1086947_1089068_+|TonB-dependent-receptor
MTNTLTRLLLTAALCGLFLLSEAQERNAVSAPDPAAPRMPADSISRDYRLDGVVIGTQRPPSPLGSIAEGRFRLLMRNSSALPRFAGSIDPMRILQLMPGVQTAAEGNSGLYVRGNDAGQNLILLNQAPLYAHAHLLGFFSVFNPGQVASFELSKTGGGRIETAMQPATVVVQSREETGVRWGVEGDLGIIASQATVTAPLTDRAALFLSGRRSYTGWLIGALSPKGEDDLNYRLQDYDATLAWQIDDHNKLIVNSHYGDDRTHITYNEGLLGGRLQWYASVSSATLRSELSPTTHMENALYYSRLDTRLTASTTGISAQAPSSIGDLGYKHSTRWHIGRLQLAAGLQYAYRRIRPQHIASDYGGIADAGRGPRYDTHELAPFLAATIPLTHSLTCDAALRYGFYLLQGDGRIASYRHASPQPSLSLDWQVARGSRLRASYNYITQYIHKVPSSNISFSTDFWMAPTRRTPPQHTHHAALGYFAEAAGGRLNFSAEAYYQRMYRVLEYNAPLTGMVNNRYELEQYLHSGDGEAYGMEFMVSYAGRKFNGWISYTLGKSVRQFAALNNGLPFPASLDRRHDLSLAASYMPGERWELSTVFVYASGGAYTPTRDLYIAGGSFVRGHGSYNGARLPDYHRLDLSVTYWLRRKPWRSGINLSLFNLYAHRNPLYISWPVLVDEEKHEYQIHPRRHYLYTVIPSVSWIFKF
>NZ_AP019735.1|WP_141412330.1|1089075_1089954_+|DUF4249-family-protein
MKRSVILLFTLLGSCLGKVSTDTEYHRQLVVEGRIEAGGPAEVMLSENLPFLDVITEQTLEAAVVRYAKVTVTSDDGQSEILTGYYDRNYPTRFVYRSARLHGRTGGTYTLTVDYRGRTCTAVTTVPEPIPLRELRAEPVCDSLFTLQALFDDPPAKNAYFAECRTTDPGAYSPALMGVVDDSVLDNGGSVTLTVNRPLQYLKIKDYKQYFRPGETVDVRFSHISSPTFNFWSRLENEMLNAMNPVFPAYENLPSNIKGDARGIWSGYGSSYYRITMPQKNDCKETTVFPPA
>NZ_AP019735.1|WP_019130946.1|1090595_1091195_+|RNA-polymerase-sigma-70-factor
MKAEESILIERLKKGERTAFNELYGIFWAPLVNYAELIVGDENADDVVQEVFVRIWVGRDKLRNDGSLRGYLLRAVYRTALNVLRSKNYASSYRSQTKLQIEQQLCTYYDPDENEIIRNLYARQIADELDAVVETLSPKCREVFRMSHFEGLSNREISERLNISVSTVENHINNALRQLRGKLGHLKMFLLLTIYILGQ
>NZ_AP019735.1|WP_141412331.1|1091264_1092296_+|FecR-domain-containing-protein
MKNEDSQHPFDERIIWKYFDGTATSEEEQELSQWLATSEKHRCEVAELRAVRQRFAKWRSTLYGPARFIRSLNRLNSRIDALENAPCTAQRPHRLSNLFGHIRIHSLLRTAAVVAVVALTGMFAWRTALMPAPITYFNADTTIMHVAMPDGSDIWLTPGSTLCYDETFPTDERRVHLDGEAYFDVEHDAKHPFDVVTPNLRVRVLGTVFSVRSLRGDHMAETTLAEGAVSLQRADGSNLIRLHPGQRAIYDTQDEQLEIKEVPVGDHLALSYGIITLDGVPLRQIADRIEELYGVKLRLVDDDAPDANYNFSFQKDTPIEDVIELLQFISGTRFEILRYPDSD
>NZ_AP019735.1|WP_141412332.1|1092410_1095977_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKKIGLSLTGWCRMLLCVGLAALPSASLGARGELLADQRLNLNLSFSSASLREVVSAFTEQTGVVFSYETSLGKRTLSDVHVVIQDASLEEMLNTLFYDTGISWKIKDHVVALTAIPSSKKNTSTGPAPSPSANRKPVVTGRVVNEEGEPLVGVNVLVKGTTQGTSTDIDGIYSIAVADDDVLQFTYLGYGSAEWRVGTQTRIDVVLKEDKQMLDEVVVVGYGTVKRRDLVGAVDQVDSKVFSERSNPSISRSLQGAIPNLNISMRDGKPSRAATINIRGTGSIGSGGGALVLIDGVEGDLETVNPQDIASVSVLKDASSAAIYGARGAFGVILVTTKSAEEGETKVTYNGSFSLHARTVKPQLVTDGYEWTTGYINAWNGYYNGQNPLPSYINNIAPYSDSWYKELARRSTDPSLERVRINDKNQYEYFANTDWMDAFYKDFNYSHEHNISVSGGNQNADYYVSGRFYDQDGIYRVGDERYKQYNVRAKGNIRIRPWLRLNNNMDFTVVDYHQPMLYYSLQLPQRMIEHGGQPINPITNPDGTWTYAAVLNGYAGFAEGSSYQQDDKFTMKDKLGIEIDVVKDVLKISGDLSYLFARNKRERVTNMYTGYRGPDTPITVNESQGSTLENLRQDTNYLSSNIYGEYTPKLGDDHTLKLLAGWNLETKKYRGTTIKREGLTVPSKPSFGLMDGLTSDPVVSGYDWSYVGAFFRANYGYQGKYLAEFSCRYDGSSKFPENSKWGFFPSASIGWRLSEEKFMEWSRNWLDNFKIRLSAGSMGNGNIDPYKYIDYMTIKTSTVVIGDALGSYTTAPGAIPLSLTWETATTYDVGFDMDLFRNRLSIGFDWYRRYTTDMYTVGVSLPSVYGTDAPKGNNASLKTNGWELSVGWRDSFELGGKAFSYNVKAMVWDARTWVTEYINPTGALGDYYEGKELGEIWGYRVEGLFRDQEDIDSHAEQSFLQTLDKVTRPGQVKFADLNQDGKIDRGAYTTADPGDLTVIGNETPRYCYGINLGFNWNGIGISTFWQGVGKKDWYPRYDSGFFWGQYNRPFGYMLKQHTGDKVYREELDNWDTAYWPRYTTYQTHQSSVNRPLTINNDRYMQDVSYIRLKNITVDYTFPDRICKKLHIKGLKVWVSGENLWTYSPMFEHCDNYDPEVINAGDSDFRTSEGDGYSYPMLRTVTLGVNLSF
>NZ_AP019735.1|WP_141412333.1|1095996_1097784_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKIFMLLASVALFGSCEDFLSKEDPNKIDAPSYFRNETDLQTYVNGFLQTMSPTAASVATGDARTDCLAWRGEYQFLTDNFDADDQSGWGTSDWEDLRNINYFLDNFRQAAVSETTLAHYEGVARFWRAYFYWNKVKTFGAVPWYDSTIDSNDHEALYKPRDSREYVMRKVLEDIEFASTYCTSSSALEVNSVQITRYVALALKARICLYEGTFRKYHANDPSTGKPWTADEAETYLRAAVSACNELMTSKKYSLVSDPANVSTQYRKLFTSESVFTQEVIWARVYNAELNATHNLNSNFIVQQYGSYSLTKQFINTYLNLDGSRFTDKPGYEKTAFIDEFENRDYRLMQTVRYPGYTRKNNGTDTRYAPDFGYCVTGYQPIKWVIDDTSLDSNTSPCSTSIPIIRYAEILLTYAEAKCELDEFDETVWNETIKPLRERAGVDGTMPATADPYMIEYFLGTVTDNALLEIRRERGCELILENVRWDDDMRWGMGKLAERPWYGVYVGELDKAYDMDGDGKDDVCFVRKEPERPQAGITYRVLGDDFSLTDGDSGYIECYIRMTRKWDDKKYVRPIPTTALNDNPALGQNYGWEK
>NZ_AP019735.1|WP_141412334.1|1097812_1099126_+|BACON-domain-containing-protein
MKRINKWTLLLTASYCVLAVGCKDDEGSYLVRETDVIQFSSNLASSQRITLRCNGAWRSVVPEDAQWLSTTPSEGVGTGEFEWITVSATHNRSAERTATLYLECNGVQYPITVTQANGAIIYGTPTLDGNLIEGEASEASIRFTYSNAYGDETIAVKCTPSGDCDGLSVAGTSFELTNGGATLALDIEGTPTKPGYATFAVSVDDQPIGEVRAKVYSVSEMPVEGLPVQWRFSEIMGGDPEKTDLQKRQPEWTTDKHTLNSDVGSATITVVEAEGKTATALNSWGYNNGHAYIKGLYYNDYWLMTIPVKYVASGTVLNAKGCFGGSGSAAAFFLLEYSADGLTWHQADGAKTETFTIKEKPVEAIYHVQACDVPKFPDDAACSFDCTFPVEVDIPNGNLYIRLRVSANIRITQNNTITTGGGGSNRLAKTWSVSVVE

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Crispr_ID: NZ_AP019735_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_7

1084415-1084511

Orphan

Consensus_repeat	Method
CAAATTTATTTGAACATTGCCGAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_7

>merge|NZ_AP019735|7|1084415-1084511|CRISPRCasFinder
CAAATTTATTTGAACATTGCCGAGCGGGAGTATCTTCGGCACAGCCAAAGATACGATTAAGCCGAGCGCAATGCAAATTTATTCGAACATTGCCGAG

>NZ_AP019735|7|7|1084415-1084511|CRISPRCasFinder
CAAATTTATTTGAACATTGCCGAG	CGGGAGTATCTTCGGCACAGCCAAAGATACGATTAAGCCGAGCGCAATG
CAAATTTATTCGAACATTGCCGAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_019130949.1\|1085496_1086882_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019131622.1\|1071808_1074184_+\|BamA/TamA-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|227116
NZ_AP019735.1\|WP_141412331.1\|1091264_1092296_+\|FecR-domain-containing-protein	unknown	unknown	gnl\|CDD\|226235
NZ_AP019735.1\|WP_019130946.1\|1090595_1091195_+\|RNA-polymerase-sigma-70-factor	unknown	unknown	gnl\|CDD\|274376
NZ_AP019735.1\|WP_141412322.1\|1070040_1071063_+\|diaminopimelate-epimerase	unknown	unknown	gnl\|CDD\|234768
NZ_AP019735.1\|WP_141412328.1\|1084788_1085394_+\|signal-peptidase-II	unknown	unknown	gnl\|CDD\|237816
NZ_AP019735.1\|WP_019131619.1\|1069685_1069895_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019131617.1\|1068089_1068653_+\|OmpH-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|377167
NZ_AP019735.1\|WP_141412326.1\|1081818_1082088_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412334.1\|1097812_1099126_+\|BACON-domain-containing-protein	unknown	unknown	gnl\|CDD\|271342
NZ_AP019735.1\|WP_141412323.1\|1071055_1071802_+\|nitroreductase-family-protein	unknown	unknown	gnl\|CDD\|380322
NZ_AP019735.1\|WP_162502269.1\|1082327_1084364_-\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173811
NZ_AP019735.1\|WP_141412330.1\|1089075_1089954_+\|DUF4249-family-protein	unknown	unknown	gnl\|CDD\|379442
NZ_AP019735.1\|WP_162502270.1\|1086947_1089068_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|366183
NZ_AP019735.1\|WP_019130941.1\|1099145_1100507_+\|Ig-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|367056
NZ_AP019735.1\|WP_141412324.1\|1074610_1075156_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412325.1\|1075233_1076454_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340895
NZ_AP019735.1\|WP_141412321.1\|1068739_1069600_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_AP019735.1\|WP_141412332.1\|1092410_1095977_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_AP019735.1\|WP_141412333.1\|1095996_1097784_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_019131622.1\|1071808_1074184_+\|BamA/TamA-family-outer-membrane-protein	gnl\|CDD\|227116	COG4775, COG4775, Outer membrane protein/protective antigen OMA87 [Cell envelope biogenesis, outer membrane].	6.531e-30
NZ_AP019735.1\|WP_141412331.1\|1091264_1092296_+\|FecR-domain-containing-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	4.88926e-27
NZ_AP019735.1\|WP_019130946.1\|1090595_1091195_+\|RNA-polymerase-sigma-70-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	1.97754e-44
NZ_AP019735.1\|WP_141412322.1\|1070040_1071063_+\|diaminopimelate-epimerase	gnl\|CDD\|234768	PRK00450, dapF, diaminopimelate epimerase; Provisional.	3.18009e-47
NZ_AP019735.1\|WP_141412328.1\|1084788_1085394_+\|signal-peptidase-II	gnl\|CDD\|237816	PRK14788, PRK14788, lipoprotein signal peptidase; Provisional.	2.74833e-59
NZ_AP019735.1\|WP_019131617.1\|1068089_1068653_+\|OmpH-family-outer-membrane-protein	gnl\|CDD\|377167	pfam03938, OmpH, Outer membrane protein (OmpH-like). This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.	3.28524e-22
NZ_AP019735.1\|WP_141412334.1\|1097812_1099126_+\|BACON-domain-containing-protein	gnl\|CDD\|271342	cd14948, BACON, Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.	1.99915e-10
NZ_AP019735.1\|WP_141412323.1\|1071055_1071802_+\|nitroreductase-family-protein	gnl\|CDD\|380322	cd02146, NfsA-like, nitroreductase similar to Escherichia coli NfsA. This family contains NADPH-dependent flavin reductase and oxygen-insensitive nitroreductase. These enzymes are homodimeric flavoproteins that contain one FMN per monomer as a cofactor. Flavin reductase catalyzes the reduction of flavin by using NADPH as an electron donor. Oxygen-insensitive nitroreductase, such as NfsA protein in Escherichia coli, catalyzes reduction of nitrocompounds using NADPH as electron donor.	1.28724e-67
NZ_AP019735.1\|WP_162502269.1\|1082327_1084364_-\|S8-family-serine-peptidase	gnl\|CDD\|173811	cd07485, Peptidases_S8_Fervidolysin_like, Peptidase S8 family domain in Fervidolysin. Fervidolysin found in Fervidobacterium pennivorans is an extracellular subtilisin-like keratinase. It is contains a signal peptide, a propeptide, and a catalytic region. The tertiary structure of fervidolysin is similar to that of subtilisin. It contains a Asp/His/Ser catalytic triad and is a member of the peptidase S8 (subtilisin and kexin) family. The catalytic triad is similar to that found in trypsin-like proteases, but it does not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.	2.71294e-70
NZ_AP019735.1\|WP_141412330.1\|1089075_1089954_+\|DUF4249-family-protein	gnl\|CDD\|379442	pfam14054, DUF4249, Domain of unknown function (DUF4249). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 279 and 365 amino acids in length. There are two completely conserved residues (C and G) that may be functionally important.	3.08156e-22
NZ_AP019735.1\|WP_162502270.1\|1086947_1089068_+\|TonB-dependent-receptor	gnl\|CDD\|366183	pfam00593, TonB_dep_Rec, TonB dependent receptor. This model now only covers the conserved part of the barrel structure.	1.20186e-15
NZ_AP019735.1\|WP_019130941.1\|1099145_1100507_+\|Ig-like-domain-containing-protein	gnl\|CDD\|367056	pfam02368, Big_2, Bacterial Ig-like domain (group 2). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial and phage surface proteins such as intimins.	1.93635e-07
NZ_AP019735.1\|WP_141412325.1\|1075233_1076454_-\|MFS-transporter	gnl\|CDD\|340895	cd17337, MFS_CsbX, CsbX family of the Major Facilitator Superfamily of transporters. The CsbX family is composed of Bacillus subtilis CsbX protein (also named alpha-ketoglutarate permease), Klebsiella pneumoniae D-arabinitol transporter (DalT), and similar proteins. The csbX gene is a sigmaB-controlled gene that is expressed during the stationary phase of cell growth. DalT is a pentose-specific ion symporter for D-arabinitol uptake. Most members of this family remain uncharacterized. The CsbX family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	6.89031e-173
NZ_AP019735.1\|WP_141412321.1\|1068739_1069600_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	8.97676e-32
NZ_AP019735.1\|WP_141412332.1\|1092410_1095977_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_AP019735.1\|WP_141412333.1\|1095996_1097784_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	7.78693e-42

>NZ_AP019735.1|WP_162502269.1|1082327_1084364_-|S8-family-serine-peptidase
MMKKILLLAGIVSLAACTNDPEETFSQGGGSSAGVKVIYDAEGAVEGQLIVKFRPSAADSLAAALASASATRAGFATADELLAAVGVDGIRPLFGSDPRFEERHRAFGLHQWYVVTFDESLPLREMVGELSHDGRIEVLEYARCPRLKNRFPARPLRSAAAAATRASMPMNDPLLPAQWHYDNTGYQVLVTQAGADVNLFDAWKKNQGSSDIVVAVIDQAVQYTHPDLQANIWVNPNPEDDDLHGYNFVNNTAELDWSYADREEYQGQIYYSNADHGTHVAGTIAAVNDNDRGVCGIAGGRNGAGGVKIMSCQIFGDPDKRSYPTEDAFRYAADNGALICQCSYGYSYSTGSRDEMEAMRQWFMNSSEKAAIDYFIANAGKNDPDSPIEGGVVIFAAGNDGDLFGDVSEYPASYEAVVSVAAMGSDFLPAYYTCYNDEVDITAPGGDLYNSSLGTDNGGVLSTILSDPSVTYYDDERRQGLTDSNVYGYMQGTSMACPHVSGVAALGLSYLSQLGYRMTADAYKKLLLESVHPIDPYLTGTKRYDGPTLLLDEYKGKMGAGYLDANLLLENIKVAFGEKTPPRVTARIANRLLKTDTPTSSVALADYFTDDAVSQYDAVANDESVVRVNVSDGVLRMLPKKVGQARVTVSARGFEGTVVSQSFYVTVRSQSNSADGWL
>NZ_AP019735.1|WP_141412326.1|1081818_1082088_-|hypothetical-protein
MQKFLENYLVDSKKGFTFAPLSAPKTGGEVLKKLRKKFFKNLADSKKGFTFAPLSAPKISGKVSEKWFFELLVNLRKSVVFICQFPFRK
>NZ_AP019735.1|WP_141412325.1|1075233_1076454_-|MFS-transporter
MTTFYDKTGLPKSLAWGFIGVLIFMMGDGIEQTWLSRYIASQGLDHEVLFTVYGISVALSAWFSGVIAETIGVRRTMLLGYLVYLVGMAGFAGIGMMGLNYPVLLVTYAIKGLGYPLFAYTFIVWIAYRVDKSRLSSAQGWFWFVFTGGLNVLGAYYGAYAMERIGVVPTLWSSLVFASVGAVLALWVNKCDDRNLFVGAERPSSGTSKFRELLSGLAIMKREPKVLVGGIVRVINTTSQFAFVVFMPLYLKDYGIGDTQWASIWGSIFLFNILFNLIFGIVGDHIGWGRTIVWFGGVGCAVSVLLFFYAPVICNNFWFILACGALWCIMLAGYVPLSALVPSLVDKDKGAAVSVLNLGAGLAAFVGPLIVALFRNAIGYVGIVWFMAGLYILSAVMTYCIAPRNR
>NZ_AP019735.1|WP_141412324.1|1074610_1075156_+|hypothetical-protein
MKLFHYLPVGAYAAAAALLLASCGVSKRSLKQSNRALTAALQASAQKEQAEALKLYSDTSIPQGEARKSVSRDNPGQTALEQTIIRWAIDSDPQGARVFYRVLSSIPAVVKNTNETYLMTTPYEETRAFNILGLTYENSRDVQIEIKVVKTGYEAQVKRFNVRQAIDQQEISSFFMLVPKE
>NZ_AP019735.1|WP_019131622.1|1071808_1074184_+|BamA/TamA-family-outer-membrane-protein
MRRLYPIAVAALCILCTACSVVRKLPEGSYLVQKVTIEDDRNVPKKERITASELDRYVWQSPNKRFLGTNFYVWVYNQSNPDKDNWWNRFKRKIGEKPVVYDPALTLKSAENLKAYMESHGFFSSRVRYHVDTTSRRKRAIITYRTEQGPPSRYGKINYEFNDKFIEKIILQDTASTLIRPGGIFNSATLDAERERITRYLRDRGYYNFSVNNISYRYPYDTVGSRVGDLTMVVKQYLTGYNDRGEPVMENNKVYRISEINMLPGYDPTVSFTDREVRYDTVAYRGLNVVYDGKHNVRPRVLRQAIPLYPNYLYNAEQINRTYNNIMSLGYFKSTRITFDELPAPDSTNLVSYIGNADDSLATQYTQEGYLRCNILGTPQLKQSYKIDLEGTTTSSFYGLKASVGYQNRNLFRGMESFDIAFSIGHEFMKSRDSGKRNAKEFGVTAGLAFPRFLLPFFSSRYRPSLVTPRTRLELSFNYQDRPYYRRTLTSMTWTYSWSNEKYSSFAVRPVDLNLVDMSYINQDFFEKLQNLYLRNSYTSQLVAGISGSYTYNNQLKNPGRNATLVRFNWETAGNLIGGLEHLFSSPAKGKDYYEIFGIQYSQYFRVDLSASRKIMLGEKAAIAGRLYAGCGLAYGNSTSIPFDRLFYCGGSNGMRGWIPRMLGPGSVPVDPDKVTYPVQLGDMKLEANLEFRFPIWGIFHGATFFDVGNIWFMGNSAEEYPPEAVFHIRDFYKQLGFNTGLGIRLDIKFAVLRLDWGIQLHNPNNPAGKRWIHDFKWSNTALNFGVGYPF
>NZ_AP019735.1|WP_141412323.1|1071055_1071802_+|nitroreductase-family-protein
MIKEIANHRSIRKYKSSPIDEEVLSDILHSAARASTCGNMQLYSLVVTLDARVRAELAPCHFNQAMVTEAPCVVTVCADVHRFSKWCEQRDAEPAYDNFEWFLNAATDALLAAENLALAAEAHGLGVCFLGTTLYTARDICRILHLPKGVIPLTTVVIGHPAEQPPLTDRLPLDAVVHYDRYKDYTDAEIDELWAEKEASPETSALLAENGLPNLAQIFTRNRYRREDNIAISRAYFELLREQGFFNQ
>NZ_AP019735.1|WP_141412322.1|1070040_1071063_+|diaminopimelate-epimerase
MKIYDYILCSGSGNRFLLFDTLRSDLSGLNIAAFAAEELHRFGVDGLLLLTRDGRGRFGMRMFNTDGSEAEMCGNGIRCVARLARERYPEATGERFAVTSGGREYRITCEEPIFGALPTFGAEIPLSLHGDDFPPSLPAEGFVGQPVPELDEGLAFTFLQPGNPHIVALVAPDSAWLFGSDGRLDTRRLAELGERANRMRGVFPRGINVSLFCRLDEGRIFAATYERGVGITSSCGTAMTSCATAAALLGLAGFDTTVEVWNRGGRVRCLPRRTQQGIVTRLTGDASFETAGRLRLDGKECIATGDASPLDPPCDRLRLTEETLRELHEKYGLTIADDHD
>NZ_AP019735.1|WP_019131619.1|1069685_1069895_-|hypothetical-protein
MKADRNFRRNGSADAEEVFKRATKLAPNRKSGKERHSLYTQFDEEEEDAAFGYKAKQESVLDYYDDGEE
>NZ_AP019735.1|WP_141412321.1|1068739_1069600_-|alpha/beta-fold-hydrolase
MIEKFIMAGRTALHVCDSQQGERCVVLLHGYLESMFVWDDFVPLLYKRVRVVTLDLPGHGISEVRGECHSMEYLADVVRDALQALGIARCTLVGHSMGGYVALAFCERHPEMLDGLVLFSSTPNADTEEKRENRRREIALVRAGKKEQLARVAPGAGFAADNRQRMADAIADLTEQVYLTEDDGIVALLNGMIARPDRNEMLRRSPVRQLFVFGRKDEYIPAAVAEQLAAAHPQAQVVWLADSGHMGFLEEPEAAAEALLRFVGAEPDGQTAASVAGASEMPAAEA
>NZ_AP019735.1|WP_019131617.1|1068089_1068653_+|OmpH-family-outer-membrane-protein
MKKILKIVLTVAFVAGSTSVFAQKLGRINMQELVFAMPETAEMQKNLEAYQKELQDQLETIGVEFNNKLNEYTKQVSDKNSTMSDSVRQLKEKELNDLKTRYDEFVQVSQQDMQKKQGELLEPIIVKAQDAVKEVSKAGGYTVVYDTSVNAVAYFDEAVVTDILPAVKTKLGIKDTPAAAPAAPAAK
>NZ_AP019735.1|WP_141412328.1|1084788_1085394_+|signal-peptidase-II
MNFKKITILLLVLLVADQALKIWIKTHMTLDEAIMVVPTWFQLRFIENNGAAFGMRLATGGAFDWGKLALSLFRLAMIGLLGYYLRYLGKRKTPAGVLVGLTLILAGAIGNMIDSAFYGLIFSASTPTEVAHFGGSYAPLMMGRVVDMFYFPLFQWNGVPGWLSFLVDSRNYFFGAIFNLADAYISVAVVYLLIFQYKFFK
>NZ_AP019735.1|WP_019130949.1|1085496_1086882_+|hypothetical-protein
MKKILLCLALFCLATGPISCGDSNTDDGTEQGGGGNGGDGGGTGPEPEPGNPEITPEQHKAKLETIGKEVAAQFNPEDSKAAIESLTALEELLAFDDEDVAPSPAPKTYAVATAKSLAAVAAGPDVHALTSLIVRATTTEKYTLDEWAGDYVIEDGEPVKKGELANQYRLTWADAAGTQSEALFTYSAGGVEYTRVDGYAIVIPQDWNLSLKVAGHEELSVVGKSNVSADGLTLAPEVTVTLNGGYVAAAKVNADPKQVTANASFTKNGTQIVDAYAKMVCDGLTDPDNWIVEEEYDWNGDGVIDDTDTYIDPEDHIVDHVKTGEGYVTVMGLKLTLSGDIAKIIQQVNAIADTSTATGSQQEADAYNTNAKAKLAYTADNSTMADVKMQSYSYKDYIYVWNPDTQTGDNQVVTRYDIEPVLEFADGSKIAIEEYVETGFDSLTKTFEDLADAYMDLIDGK
>NZ_AP019735.1|WP_162502270.1|1086947_1089068_+|TonB-dependent-receptor
MTNTLTRLLLTAALCGLFLLSEAQERNAVSAPDPAAPRMPADSISRDYRLDGVVIGTQRPPSPLGSIAEGRFRLLMRNSSALPRFAGSIDPMRILQLMPGVQTAAEGNSGLYVRGNDAGQNLILLNQAPLYAHAHLLGFFSVFNPGQVASFELSKTGGGRIETAMQPATVVVQSREETGVRWGVEGDLGIIASQATVTAPLTDRAALFLSGRRSYTGWLIGALSPKGEDDLNYRLQDYDATLAWQIDDHNKLIVNSHYGDDRTHITYNEGLLGGRLQWYASVSSATLRSELSPTTHMENALYYSRLDTRLTASTTGISAQAPSSIGDLGYKHSTRWHIGRLQLAAGLQYAYRRIRPQHIASDYGGIADAGRGPRYDTHELAPFLAATIPLTHSLTCDAALRYGFYLLQGDGRIASYRHASPQPSLSLDWQVARGSRLRASYNYITQYIHKVPSSNISFSTDFWMAPTRRTPPQHTHHAALGYFAEAAGGRLNFSAEAYYQRMYRVLEYNAPLTGMVNNRYELEQYLHSGDGEAYGMEFMVSYAGRKFNGWISYTLGKSVRQFAALNNGLPFPASLDRRHDLSLAASYMPGERWELSTVFVYASGGAYTPTRDLYIAGGSFVRGHGSYNGARLPDYHRLDLSVTYWLRRKPWRSGINLSLFNLYAHRNPLYISWPVLVDEEKHEYQIHPRRHYLYTVIPSVSWIFKF
>NZ_AP019735.1|WP_141412330.1|1089075_1089954_+|DUF4249-family-protein
MKRSVILLFTLLGSCLGKVSTDTEYHRQLVVEGRIEAGGPAEVMLSENLPFLDVITEQTLEAAVVRYAKVTVTSDDGQSEILTGYYDRNYPTRFVYRSARLHGRTGGTYTLTVDYRGRTCTAVTTVPEPIPLRELRAEPVCDSLFTLQALFDDPPAKNAYFAECRTTDPGAYSPALMGVVDDSVLDNGGSVTLTVNRPLQYLKIKDYKQYFRPGETVDVRFSHISSPTFNFWSRLENEMLNAMNPVFPAYENLPSNIKGDARGIWSGYGSSYYRITMPQKNDCKETTVFPPA
>NZ_AP019735.1|WP_019130946.1|1090595_1091195_+|RNA-polymerase-sigma-70-factor
MKAEESILIERLKKGERTAFNELYGIFWAPLVNYAELIVGDENADDVVQEVFVRIWVGRDKLRNDGSLRGYLLRAVYRTALNVLRSKNYASSYRSQTKLQIEQQLCTYYDPDENEIIRNLYARQIADELDAVVETLSPKCREVFRMSHFEGLSNREISERLNISVSTVENHINNALRQLRGKLGHLKMFLLLTIYILGQ
>NZ_AP019735.1|WP_141412331.1|1091264_1092296_+|FecR-domain-containing-protein
MKNEDSQHPFDERIIWKYFDGTATSEEEQELSQWLATSEKHRCEVAELRAVRQRFAKWRSTLYGPARFIRSLNRLNSRIDALENAPCTAQRPHRLSNLFGHIRIHSLLRTAAVVAVVALTGMFAWRTALMPAPITYFNADTTIMHVAMPDGSDIWLTPGSTLCYDETFPTDERRVHLDGEAYFDVEHDAKHPFDVVTPNLRVRVLGTVFSVRSLRGDHMAETTLAEGAVSLQRADGSNLIRLHPGQRAIYDTQDEQLEIKEVPVGDHLALSYGIITLDGVPLRQIADRIEELYGVKLRLVDDDAPDANYNFSFQKDTPIEDVIELLQFISGTRFEILRYPDSD
>NZ_AP019735.1|WP_141412332.1|1092410_1095977_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKKIGLSLTGWCRMLLCVGLAALPSASLGARGELLADQRLNLNLSFSSASLREVVSAFTEQTGVVFSYETSLGKRTLSDVHVVIQDASLEEMLNTLFYDTGISWKIKDHVVALTAIPSSKKNTSTGPAPSPSANRKPVVTGRVVNEEGEPLVGVNVLVKGTTQGTSTDIDGIYSIAVADDDVLQFTYLGYGSAEWRVGTQTRIDVVLKEDKQMLDEVVVVGYGTVKRRDLVGAVDQVDSKVFSERSNPSISRSLQGAIPNLNISMRDGKPSRAATINIRGTGSIGSGGGALVLIDGVEGDLETVNPQDIASVSVLKDASSAAIYGARGAFGVILVTTKSAEEGETKVTYNGSFSLHARTVKPQLVTDGYEWTTGYINAWNGYYNGQNPLPSYINNIAPYSDSWYKELARRSTDPSLERVRINDKNQYEYFANTDWMDAFYKDFNYSHEHNISVSGGNQNADYYVSGRFYDQDGIYRVGDERYKQYNVRAKGNIRIRPWLRLNNNMDFTVVDYHQPMLYYSLQLPQRMIEHGGQPINPITNPDGTWTYAAVLNGYAGFAEGSSYQQDDKFTMKDKLGIEIDVVKDVLKISGDLSYLFARNKRERVTNMYTGYRGPDTPITVNESQGSTLENLRQDTNYLSSNIYGEYTPKLGDDHTLKLLAGWNLETKKYRGTTIKREGLTVPSKPSFGLMDGLTSDPVVSGYDWSYVGAFFRANYGYQGKYLAEFSCRYDGSSKFPENSKWGFFPSASIGWRLSEEKFMEWSRNWLDNFKIRLSAGSMGNGNIDPYKYIDYMTIKTSTVVIGDALGSYTTAPGAIPLSLTWETATTYDVGFDMDLFRNRLSIGFDWYRRYTTDMYTVGVSLPSVYGTDAPKGNNASLKTNGWELSVGWRDSFELGGKAFSYNVKAMVWDARTWVTEYINPTGALGDYYEGKELGEIWGYRVEGLFRDQEDIDSHAEQSFLQTLDKVTRPGQVKFADLNQDGKIDRGAYTTADPGDLTVIGNETPRYCYGINLGFNWNGIGISTFWQGVGKKDWYPRYDSGFFWGQYNRPFGYMLKQHTGDKVYREELDNWDTAYWPRYTTYQTHQSSVNRPLTINNDRYMQDVSYIRLKNITVDYTFPDRICKKLHIKGLKVWVSGENLWTYSPMFEHCDNYDPEVINAGDSDFRTSEGDGYSYPMLRTVTLGVNLSF
>NZ_AP019735.1|WP_141412333.1|1095996_1097784_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKIFMLLASVALFGSCEDFLSKEDPNKIDAPSYFRNETDLQTYVNGFLQTMSPTAASVATGDARTDCLAWRGEYQFLTDNFDADDQSGWGTSDWEDLRNINYFLDNFRQAAVSETTLAHYEGVARFWRAYFYWNKVKTFGAVPWYDSTIDSNDHEALYKPRDSREYVMRKVLEDIEFASTYCTSSSALEVNSVQITRYVALALKARICLYEGTFRKYHANDPSTGKPWTADEAETYLRAAVSACNELMTSKKYSLVSDPANVSTQYRKLFTSESVFTQEVIWARVYNAELNATHNLNSNFIVQQYGSYSLTKQFINTYLNLDGSRFTDKPGYEKTAFIDEFENRDYRLMQTVRYPGYTRKNNGTDTRYAPDFGYCVTGYQPIKWVIDDTSLDSNTSPCSTSIPIIRYAEILLTYAEAKCELDEFDETVWNETIKPLRERAGVDGTMPATADPYMIEYFLGTVTDNALLEIRRERGCELILENVRWDDDMRWGMGKLAERPWYGVYVGELDKAYDMDGDGKDDVCFVRKEPERPQAGITYRVLGDDFSLTDGDSGYIECYIRMTRKWDDKKYVRPIPTTALNDNPALGQNYGWEK
>NZ_AP019735.1|WP_141412334.1|1097812_1099126_+|BACON-domain-containing-protein
MKRINKWTLLLTASYCVLAVGCKDDEGSYLVRETDVIQFSSNLASSQRITLRCNGAWRSVVPEDAQWLSTTPSEGVGTGEFEWITVSATHNRSAERTATLYLECNGVQYPITVTQANGAIIYGTPTLDGNLIEGEASEASIRFTYSNAYGDETIAVKCTPSGDCDGLSVAGTSFELTNGGATLALDIEGTPTKPGYATFAVSVDDQPIGEVRAKVYSVSEMPVEGLPVQWRFSEIMGGDPEKTDLQKRQPEWTTDKHTLNSDVGSATITVVEAEGKTATALNSWGYNNGHAYIKGLYYNDYWLMTIPVKYVASGTVLNAKGCFGGSGSAAAFFLLEYSADGLTWHQADGAKTETFTIKEKPVEAIYHVQACDVPKFPDDAACSFDCTFPVEVDIPNGNLYIRLRVSANIRITQNNTITTGGGGSNRLAKTWSVSVVE
>NZ_AP019735.1|WP_019130941.1|1099145_1100507_+|Ig-like-domain-containing-protein
MKKQIIATLLLLTTTASNIGCTDDSPAQITSLKLNRTELTLQPGETFQLEATTRPADAGVPIKWSSSNEAVAAVDERGLVTGTGYGAALVTARYGSYSAKCSVTLNAEQVWDPSQALAAPLSSDIVHSKNVLLYAPRRILQGFDILPNGEIYYSQVGSNAYTLNICRAAGPNQNAQDEVMILKHFGHGTQIVAEKASDGKTYIWLNSNASVDDSGEYGNNWSFSRVEFVPGTNEADGYAGDTFFLNKEQQYDQQVAVDFDARRLLVGSRKSGVRHFWIFDLDEVLALPLKEMTVSVTVGGGTGDGEKQTVERKIMGHDLNDCRVLGNFSFSSGTDKEHDVYSYSHQGHEINGDYIYFYEGNAVENSDDPGTYQSKAYVTVFNYNGRIVVPRTEVAAISDVNGLASEGFTQTGYAEGECIKVKEGKLYLGMACRDGSSSNRYANILVYDCVKKQ

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Crispr_ID: NZ_AP019735_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_8

1575761-1575859

Orphan

Consensus_repeat	Method
ATTGCCGAGGCGGAGTATCTTCGGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_8

>merge|NZ_AP019735|8|1575761-1575859|CRISPRCasFinder
ATTGCCGAGGCGGAGTATCTTCGGCGTCGGCCAAAGTACGATTAAGCGAGGGCAATGTCAAATTTATTTGAACATTGTCGAGGCGGAGTATCTTCGGCG

>NZ_AP019735|8|8|1575761-1575859|CRISPRCasFinder
ATTGCCGAGGCGGAGTATCTTCGGCG	TCGGCCAAAGTACGATTAAGCGAGGGCAATGTCAAATTTATTTGAAC
ATTGTCGAGGCGGAGTATCTTCGGCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141412561.1\|1573634_1574951_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380191
NZ_AP019735.1\|WP_141412565.1\|1578682_1579879_-\|ComEC/Rec2-family-competence-protein	unknown	unknown	gnl\|CDD\|377126
NZ_AP019735.1\|WP_019130595.1\|1571411_1571603_+\|exodeoxyribonuclease-VII-small-subunit	unknown	unknown	gnl\|CDD\|376855
NZ_AP019735.1\|WP_141412569.1\|1582923_1583913_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413588.1\|1572790_1573618_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412562.1\|1576331_1576922_-\|HD-domain-containing-protein	unknown	unknown	gnl\|CDD\|372434
NZ_AP019735.1\|WP_141413587.1\|1564612_1566007_-\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_AP019735.1\|WP_019130590.1\|1575114_1575711_-\|GTP-cyclohydrolase-I-FolE	unknown	unknown	gnl\|CDD\|236472
NZ_AP019735.1\|WP_141412563.1\|1576925_1577318_-\|RNA-binding-S4-domain-containing-protein	unknown	unknown	gnl\|CDD\|224109
NZ_AP019735.1\|WP_141412559.1\|1567680_1568979_+\|PAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|227333
NZ_AP019735.1\|WP_141412564.1\|1577496_1578672_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|225174
NZ_AP019735.1\|WP_019130596.1\|1570153_1571407_+\|exodeoxyribonuclease-VII-large-subunit	unknown	unknown	gnl\|CDD\|272979
NZ_AP019735.1\|WP_141412568.1\|1582390_1582864_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412560.1\|1571599_1572364_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|369777
NZ_AP019735.1\|WP_141412567.1\|1580707_1581181_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412566.1\|1580307_1580733_-\|phage-holin-family-protein	unknown	unknown	gnl\|CDD\|377457
NZ_AP019735.1\|WP_019130597.1\|1569424_1570150_+\|DUF3298-domain-containing-protein	unknown	unknown	gnl\|CDD\|378702
NZ_AP019735.1\|WP_141413589.1\|1579901_1580306_-\|structural-protein-P5	unknown	unknown	gnl\|CDD\|222880
NZ_AP019735.1\|WP_141412558.1\|1566328_1567684_+\|sigma-54-interacting-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225114
NZ_AP019735.1\|WP_141413590.1\|1581183_1582407_-\|phage-portal-protein	unknown	unknown	gnl\|CDD\|273680

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141412561.1\|1573634_1574951_+\|hypothetical-protein	gnl\|CDD\|380191	NF033187, internalin_J, class 1 internalin InlJ. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface-anchored proteins with an N-terminal signal peptide, leucine-rich repeats, and a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin J (InlJ).	1.86701e-19
NZ_AP019735.1\|WP_141412565.1\|1578682_1579879_-\|ComEC/Rec2-family-competence-protein	gnl\|CDD\|377126	pfam03772, Competence, Competence protein. Members of this family are integral membrane proteins with 6 predicted transmembrane helices. Some members of this family have been shown to be essential for bacterial competence in uptake of extracellular DNA. These proteins may transport DNA across the cell membrane. These proteins contain a highly conserved motif in the amino terminal transmembrane region that has two histidines that may form a metal binding site.	2.11473e-37
NZ_AP019735.1\|WP_019130595.1\|1571411_1571603_+\|exodeoxyribonuclease-VII-small-subunit	gnl\|CDD\|376855	pfam02609, Exonuc_VII_S, Exonuclease VII small subunit. This family consist of exonuclease VII, small subunit EC:3.1.11.6 This enzyme catalyzes exonucleolytic cleavage in either 5'->3' or 3'->5' direction to yield 5'-phosphomononucleotides. This exonuclease VII enzyme is composed of one large subunit and 4 small ones.	5.0171e-07
NZ_AP019735.1\|WP_141412562.1\|1576331_1576922_-\|HD-domain-containing-protein	gnl\|CDD\|372434	pfam13023, HD_3, HD domain. HD domains are metal dependent phosphohydrolases.	1.9306e-49
NZ_AP019735.1\|WP_141413587.1\|1564612_1566007_-\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	6.55662e-36
NZ_AP019735.1\|WP_019130590.1\|1575114_1575711_-\|GTP-cyclohydrolase-I-FolE	gnl\|CDD\|236472	PRK09347, folE, GTP cyclohydrolase I; Provisional.	9.91376e-109
NZ_AP019735.1\|WP_141412563.1\|1576925_1577318_-\|RNA-binding-S4-domain-containing-protein	gnl\|CDD\|224109	COG1188, COG1188, Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog) [Translation, ribosomal structure and biogenesis].	5.6348e-18
NZ_AP019735.1\|WP_141412559.1\|1567680_1568979_+\|PAS-domain-containing-protein	gnl\|CDD\|227333	COG5000, NtrY, Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms].	2.60701e-42
NZ_AP019735.1\|WP_141412564.1\|1577496_1578672_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|225174	COG2265, TrmA, SAM-dependent methyltransferases related to tRNA (uracil-5-)-methyltransferase [Translation, ribosomal structure and biogenesis].	2.11772e-13
NZ_AP019735.1\|WP_019130596.1\|1570153_1571407_+\|exodeoxyribonuclease-VII-large-subunit	gnl\|CDD\|272979	TIGR00237, exodeoxyribonuclease_VII_large_subunit, exodeoxyribonuclease VII, large subunit. This family consist of exodeoxyribonuclease VII, large subunit XseA which catalyses exonucleolytic cleavage in either the 5'->3' or 3'->5' direction to yield 5'-phosphomononucleotides. Exonuclease VII consists of one large subunit and four small subunits. [DNA metabolism, Degradation of DNA].	2.78509e-113
NZ_AP019735.1\|WP_141412560.1\|1571599_1572364_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	3.07372e-13
NZ_AP019735.1\|WP_141412566.1\|1580307_1580733_-\|phage-holin-family-protein	gnl\|CDD\|377457	pfam05105, Phage_holin_4_1, Bacteriophage holin family. Phage holins and lytic enzymes are both necessary for bacterial lysis and virus dissemination. This family also includes TcdE/UtxA involved in toxin secretion in Clostridium difficile. The 1.E.10 family is represented by Bacillus subtilis phi29 holin; 1.E.16 represents the Cph1 holin; and the 1.E.19 family is represented by the Clostridium difficile TcdE holin. Toxigenic strains of C. difficile produce two large toxins (TcdA and TcdB) encoded within a pathogenicity locus. tcdE, encoded between tcdA and tcdB, encodes a 166 aa protein which causes death to E. coli when expressed, and the structure of TcdE resembles holins. TcdE acts on the bacterial membrane. Since TcdA and TcdB lack signal peptides, they may be released via TcdE either prior to or subsequent to cell lysis.	0.000418891
NZ_AP019735.1\|WP_019130597.1\|1569424_1570150_+\|DUF3298-domain-containing-protein	gnl\|CDD\|378702	pfam11738, DUF3298, Protein of unknown function (DUF3298). This family of bacterial protein C-terminal regions is highly conserved but the function is not known. Several members are annotated as being endo-1,4-beta-xylanase-like, but this could not be confirmed, and the structure can be defined as a heat-shock cognate 70kd protein 44kd ATPase.	1.32475e-15
NZ_AP019735.1\|WP_141413589.1\|1579901_1580306_-\|structural-protein-P5	gnl\|CDD\|222880	PHA02564, V, virion protein; Provisional.	5.82939e-31
NZ_AP019735.1\|WP_141412558.1\|1566328_1567684_+\|sigma-54-interacting-transcriptional-regulator	gnl\|CDD\|225114	COG2204, AtoC, Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domains [Signal transduction mechanisms].	3.64547e-170
NZ_AP019735.1\|WP_141413590.1\|1581183_1582407_-\|phage-portal-protein	gnl\|CDD\|273680	TIGR01540, Phage-like_element_PBSX_protein_XkdE, phage portal protein, PBSX family. This model represents one of several distantly related families of phage portal protein. This protein forms a hole, or portal, that enables DNA passage during packaging and ejection. It also forms the junction between the phage head (capsid) and the tail proteins. It functions as a dodecamer of a single polypeptide of average mol. wt. of 40-90 KDa. This family shows clear homology to TIGR01537. The alignment for this group was trimmed of poorly alignable N-terminal sequence of about 50 residues and of C-terminal regions present in some but not all members of up 180 residues. [Mobile and extrachromosomal element functions, Prophage functions].	4.60953e-09

>NZ_AP019735.1|WP_019130590.1|1575114_1575711_-|GTP-cyclohydrolase-I-FolE
MEKKLYEKQEIYDPATIAELSEHYAAILRLLGEDPTREGLLKTPERVAKAMAFMTKGYAEDPRDILLSAMFREEYRQMVLVRDIEVYSLCEHHMLPFYGKAHVAYIPDGYITGLSKVARVVECFARRLQVQERLTVQIRDCIHEALHPLGVAVVIEASHMCMQMRGVEKQESSTTTSAFTGIFLRDHRTREEFMELIR
>NZ_AP019735.1|WP_141412561.1|1573634_1574951_+|hypothetical-protein
MKKRSILLSGLFVLTMCLAGYAAADYPPNVADAIPDREFRTLCLRIADTDGDGAISREEALAVTKIRCPSYKTYGKTISSLEGLHYFANLETLDCSSQNLTSLDAGGCSALELLICETCELECLRLPRTAALKKLDCSSNRLASLDVSGCPALRRLTCYDNPFTELNVDACPDLELLDCSCLVTSDLRHHEKLYELHCGGLPCVRLDLSEFKQLSHLSITHSRISEIVFGDSDLLISFALNDVDFTSLDLSGCHQLMYLTLTDMPLRELTLPETELSSVELRKLPLERLEVKGYVKIGKLAVSDCGRLKCIDGSGQVMNFDCCNCSNLTMLNMDAFRYVGDFRCTGTALTSLDFSRCNGNRYAEIDCSDNRLTTLVLPPEIYTLSCQGNLLEELDISGCSINWIECRPMETLRRIRLRRDQNNYRLGGTKGIELVYVD
>NZ_AP019735.1|WP_141413588.1|1572790_1573618_+|hypothetical-protein
MLLCLALLAGCSDDDEQPDPQLPPLVWPDDVATAIPDEGFREYCLERYDRDKDGRLSKDEVLAVKKMIHFPDVSGRFLSLEGIEYFSNLENFAWEYSGPKEIDLRYNSRLQKISCLYNSNLIRFRGPVGYTPLEIELYSLFNLEELDLSGCGNVQELRLFVDSFSEVKLSSVNLPDPSHLQYLAFAAANAGCYDALLADGANLKKLYYNFYPSEVLDLSHCPKLADLIIHVRAGSELKKIRMHKNAPIAIYGGGIDIRDEKGNDCSFSVEIEYVE
>NZ_AP019735.1|WP_141412560.1|1571599_1572364_+|methyltransferase-domain-containing-protein
MKRLIRWALNHVPRPLLQRLAGWAVPVAGLFYVGRGRECPVCGARRRRFLPYGYVAPRADALCPSCLSLERHRLLWLYLTRETDLLRRPQRILHIAPEVCLMKRLRHRAADYTTADLESPLAELHFDVLRIPLPDASYDVLICNHLLEHVADDRRALGEFYRILRPGGWGILLSPVDRSRAATFEDDSITDPAERTRIFGQYDHRRIYGRDYGGRLREAGFEVREIDYAARFSAEERRRYALPDDWIYVVRRPL
>NZ_AP019735.1|WP_019130595.1|1571411_1571603_+|exodeoxyribonuclease-VII-small-subunit
MDKKELTYDEAMAEIEAILAKFRNEEMSVDALAAEVRRATTLIAFCRKRLLKAESDVKKITGE
>NZ_AP019735.1|WP_019130596.1|1570153_1571407_+|exodeoxyribonuclease-VII-large-subunit
MIAAQYITLSELQRRVRQALEERFALPLWVSAEIAEVKVNYSGHCYLELVEKGEGDGVPKAQARAVIWRSQYARIAAYFEAETGQRLAAGMRILAKATVNYHELYGFSLQLLDVDPAYTLGDMERQRQQTIARLQAEGVWEMNRQQAMPAVVQRIAVVSSSRAAGYQDFCNELAKSPYRFCLTLFDAVVQGAAAEDSIVDALSRIAAAGEAFDAVVMIRGGGSSSDLNCFNAYRLCNHVAQFPLPVVTGIGHDKDTSVADLVAHTALKTPTAVAAWLVERMAQADGYLAWAGLQLGNAALAITHSAAVGLERLGAALAQQSQRLLQEGRSRLDRAEETLLAAPADLLRGHDRRLAAASELLLSYSVERVLRRGFAVVRRGGEALRSAEGLSPGDRLDITLADGEVQAAVVACTKKKR
>NZ_AP019735.1|WP_019130597.1|1569424_1570150_+|DUF3298-domain-containing-protein
MKLPALVLLAAFAAGMAGCCRRAAAPQFAERSLDTVVRCGAVPCDLSYRFLTIANADRSEALAAIENANVNYFFALEDFTGTAEEAARRFIERFAADNACDTLYMPDMRYSLSVAAAQAPVDTLTVYTIRRESYTGGAHGMRTTEYHNYWTKGGYELSLGDLFPEEQLPRLTERIKAKLREQYGAADDEELAQRGFFPETIAPTENFEVTPEGIVFHYNPYDIACYAIGEVDVPFTKEELK
>NZ_AP019735.1|WP_141412559.1|1567680_1568979_+|PAS-domain-containing-protein
MKYGGDLFRLVSHVVVLIAVTAAAAALSAAGRYAFALLLLPFGGIAVYRLVRLYDASMRRVTFLLDAVENNDLNFRFCEGAASGGERALNVALNRIREIIVRAKLRAEERERYYRLIMECARTGLLTVDDRGSVYQVNDEALRIFGLPRMTHVRQVEPLLPEACRALTAIRSGERLRVRCRTESGEVNLSLTCSEITLDRRHLRVVAVSDIDDYLSAVQVESWSKLTRILTHEIMNSLAPITSLSDTLLHLGRRLDADVERGLDTISSTSRRLTAFVETFRRFTRIPEPRKSAFEVRGMLERAVMLAGVSDVVRLDVEPSQMLIYADEGLVEQVAVNLLKNAREAAEGLSDGRIEVVARISADETVRIDFGDNGAAIPAEVSDNIFTPFFTTKSDGSGIGLSVSRRIMQLHGGSLRLTSNVDGKVTFTLFFA
>NZ_AP019735.1|WP_141412558.1|1566328_1567684_+|sigma-54-interacting-transcriptional-regulator
MAKEGNLLIVDDNSSILGALRLLLERHFAKVTTLTSPKLLDTVLRGEAVDAVLLDMNFTAGVNNGNEGIYWLRRIRDIRPDVKVVLFTAYADVDLAVRSMRDGAVDFVVKPWDNERLVASLRNACELARSQREVKRLREIRRELTVDETMFWGTSPAMERIREIVEKVAATDANILITGENGTGKEMLAREIHRRSHRSGGPMVAVDMGAVPETLFESELFGHVKGAFTDARTDRAGKFEVADGGTLFLDEIGNLPLHLQPKLLTALQSGAIVRVGSNLPVKVDCRLISATNRDLFGMTAGGSFREDLLYRINTIHIDLPPLRQRREDILLLARTFLVRYAGKYRKPIRDFDAAAQHELVAHAWAGNIRELQHTVEKAVILCDGTEISPATLLLRPVAQGPSPAAFTTFEEMERAMIEQAMERHGGNLSAVAQQLGVTRQTLYNKIKRYGL
>NZ_AP019735.1|WP_141413587.1|1564612_1566007_-|TolC-family-protein
MTPSVARQRIAASETPPAADTVARTEPPASDGTAALPRPAADTVSAMTLDACMAYAVEHNPNVRQQIYANRNYRQEYIASIAALVPSISASASATTSFGRSVDPETNTYTTVANLDNSYSLSGQIPVFAGLSGINTVRAARVMRLMGIEELQQARDEAALNAMQAYFDVVYYTESVRLAREQRQTSAANLHKSRKLYELGLKSAADVAEIESQCASDDFLLTQQENNLALAKISLCEAMNYPSGCCPEIVAEIAVGTPTGAAAYGEVLAYALEKHPKAQQAAYNVQQMRLKYSVAKGKYYPSVSVGGGYSTNFFMSLDDRSLYAPFGSQLRDNRGYYFSARLSIPIFGGLTKRTSVNRARNNWRIAELQRDATLRTLQSEVAQAYQQMLGAGKEFVQASKKAEAARLAYEAVAGKYERGMVSTLDLQTASDKLLQARAERIRTRLQYIIKTRLVEYYNGEPLIR
>NZ_AP019735.1|WP_141412562.1|1576331_1576922_-|HD-domain-containing-protein
MRPERLFEILAVAERLKCNTRHSWTSTGRRESVAEHSWRLALMALLVADEFPDVDCGRVVRMCLVHDLGEAFTGDIPAFEKRRQDETHEAALLARWVETLPEPLRAEWRSLYAEMEALATPEARLYKALDKLEAVIQHNEADIATWLPLEYDLNIAYGADEVAWNGYLRRLKEAANEISRQKIAAAKEQAPDDAGK
>NZ_AP019735.1|WP_141412563.1|1576925_1577318_-|RNA-binding-S4-domain-containing-protein
MDDVRLDKYLWAVRIFKTRSDAAEAIRTNRVTVGGATCKPSREVRIGDVIAVKRMPVVYQYKVLNLVTSRQPAKNVPAYCLNITPQEELDKLDAPRETIFVFRDRGTGRPTKKERRELDSLMDNMLYEEE
>NZ_AP019735.1|WP_141412564.1|1577496_1578672_-|methyltransferase-domain-containing-protein
MTREEFDTLCRDDVRRAVEENLGRDPLAVALDRRTPHAALVATQVKYLERARTKLPSYYAARCILPPRAFEQASSEACAAHKEPAGDTALDLTCGLGVDALALGRRFRRVVALERDPVLAAVAARNLRLLGAANVEVVCASAEEYLAATTERFDWVAADPDRRSRTGRKLVRLEECSPDILRLLPAVRRVGARLCLKNSPLFDVDEALRLFPTARIEAVSVHGECKELLVYDDGTGPLLRATALGGGSVTLPPATAPTPPPPPFDPTAYAYLFLPDVALQKMRLVRRALEGRADVWSENGFAFAHRPVEGVPGRTLAIGAIGPFDAKALRRELRGEGIEIFKRDFPLTPEEIHARTGTHAGSRQRLAFTRIGGKLWTIRLAAEAPETEREG
>NZ_AP019735.1|WP_141412565.1|1578682_1579879_-|ComEC/Rec2-family-competence-protein
MGDTPLHPPHSQSRPLRKAAGPYPMAWVLLFTAAGVAVARYATLPAGFLAAAFAAATLMAFITYRRRIGNGYIAIALLLLGMALPALRPQPAYGPAGMNRLHEAASERIRRLHLPPDAEAVALAMAAGDQTELTPERRAPYARTGTAHVLAVSGLHVGMVFLYVNLLLGALALLHRGHLLRNAAAIAVIWLFAAAAGLSPGTIRAAVMFTALQLALATTSRYAGVNILSAAAFGMLLWRPSYLFHVGFQLSFLSVAAILLWGIPLYRRLRTPWRAANAAVGMLVVGAVASTATAPLVSYCFGQIPLVGLAVNPPVILLTYGVVGVSLLWLAIPWPPLSVVVRPLLEGLLWLQNRLVAEAAALPCAAIDYRMTAAQTAVVYLFFVIFTLAVYRPWLKNR
>NZ_AP019735.1|WP_141413589.1|1579901_1580306_-|structural-protein-P5
MPRGLRNRNPGNIRRSAVRYKGETESDDAAFKTFASTAWGYRAMFVLLHTYRVRHRIATLRGMIARWAPPSENDTGAYLRTVVRRSGVDPDAEIDTRDGPTMTRIAAAMARVENGVEPDEAEIAEGWRLFSADF
>NZ_AP019735.1|WP_141412566.1|1580307_1580733_-|phage-holin-family-protein
MENLYRPVSGAAAALAGWFAPIVPLVACVFGFIAVDFLTGVAASRAVARREGRPWWFESAEAWRTVQKLALVATGIVMAWAVDRHVLDFMDLHAARLFTGFACGVEFWSFLENAAQLSDAPLFRWLKRYVRRRMRKEAGNV
>NZ_AP019735.1|WP_141412567.1|1580707_1581181_-|hypothetical-protein
MQTLITPTVVVARAFADGEYVAPETVSEAAIVAAQETYLRPVTGDALFERLLAGDHADFTDEYLAAPLALYVRYLIAPQLDLRHGQGGTVQPRSDGFAAASDATLRRSRRALLKTARRLLRRASDYLESHAAQFPLYDPQANVLNRCSIDGKLVQTR
>NZ_AP019735.1|WP_141413590.1|1581183_1582407_-|phage-portal-protein
MMKKIKPKTALAVGNRTDPYLTLGAGTVQSDRFWRWGDDNLFPAALALMSRRSTTHRRIINDKADYISGKGVVCDTASPLLARFIETVNGDGESLRQLLNKLAYDKSLFGNAFLEVVTDARRSFLSLYHQDASRCRLAKDSAHVLLHHDWAAFRAEEARTLPLYPSFEKQADGTLRAAVHYKDYEPMFTHYGVPPYIAGFGVSAIAYKTDRWNISRLDNSFQLSGVMMLDSTVDSEAEAERVVRTAEERFAGNPGQVMFVLKEGSENDHSRFIPIASQNDGDWKALHDQAVSDIVVAHSWFRSLSGLDYASGFSAERILHEYEVALNTVILGEQAELLEPIRALLRRTLGVDAASLQIVNRPPTRSKPLYMKVWEARKADGLDYDPDDERQQRYLSEITRYNLTHID
>NZ_AP019735.1|WP_141412568.1|1582390_1582864_-|hypothetical-protein
MDNAQNSSTLPRKPVGGICRVRLASARAFSPQSRFAEYELIDDRSAYVETLTADEGLLRVRHTLTLVFDKHQADAWFDRRWLERCATDGVVAAIETAAGERLRIGRSDRFGCEQALRLERFTFASGAAPGDRPTATLVLASEDTDRAQTDTDDYEED
>NZ_AP019735.1|WP_141412569.1|1582923_1583913_-|hypothetical-protein
MSFIENAKTYTGRDLETIFFRPMLSGQSALDLGVRILYNMPAPTTVQLWERSGDILQQYTAAGWTGGDPARKLQKTIDMSKVKAELGYSAADYFSMIYELITNRADVNMDDLTGTELEQAETELFKRAIAESLRVTMWIGDKEAGAGTEYATFNGFIKRIYELLVENKITAAKTYAAADLEKAAAAVDIFDAAWTEAAEELTDLKPDGQLVYFVTSDLYHLYEKYLDSFANTEAAYIGRTEGRPVLTYHGIPVVDLHLSSYLRDTTYAQSFCLLTDRRNLVLAVNTSDFPGNEIRMWYNPDLMENRQRAVFMAGCEVLDEKLVSFAYKE

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Crispr_ID: NZ_AP019735_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_9

1693446-1693545

Unclear

Consensus_repeat	Method
CTCGGCTTAACGAAAACGGTGAAT	CRISPRCasFinder

1 spacers

cas3

The CRISPR arrays of NZ_AP019735_9

>merge|NZ_AP019735|9|1693446-1693545|CRISPRCasFinder
CTCGGCTTAACGAAAACGGTGAATTTTTTTCTTCGTTTTCTCGCCTCGGCAAAGCTCGCGCAAGCGCGGCTCTGCACTCGGCTTAACGAAAACGGTGAAT

>NZ_AP019735|9|9|1693446-1693545|CRISPRCasFinder
CTCGGCTTAACGAAAACGGTGAAT	TTTTTTCTTCGTTTTCTCGCCTCGGCAAAGCTCGCGCAAGCGCGGCTCTGCA
CTCGGCTTAACGAAAACGGTGAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_019130483.1\|1694365_1695148_+\|alpha/beta-hydrolase-fold-domain-containing-protein	unknown	unknown	gnl\|CDD\|223730
NZ_AP019735.1\|WP_141412618.1\|1685879_1686959_+\|TIGR04133-family-radical-SAM/SPASM-protein	unknown	unknown	gnl\|CDD\|200384
NZ_AP019735.1\|WP_141412615.1\|1682030_1682630_-\|WbqC-family-protein	unknown	unknown	gnl\|CDD\|378083
NZ_AP019735.1\|WP_141412619.1\|1687092_1688052_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412616.1\|1683883_1685371_-\|(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate-synthase	unknown	unknown	gnl\|CDD\|179361
NZ_AP019735.1\|WP_141412626.1\|1699315_1700182_-\|HAD-IIA-family-hydrolase	unknown	unknown	gnl\|CDD\|319858
NZ_AP019735.1\|WP_141412621.1\|1691243_1693355_+\|ATP-dependent-DNA-helicase-RecG	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|236794
NZ_AP019735.1\|WP_019130482.1\|1695199_1696135_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019130492.1\|1682752_1683874_+\|acyltransferase	unknown	unknown	gnl\|CDD\|224748
NZ_AP019735.1\|WP_026074911.1\|1693565_1694363_+\|DUF3108-domain-containing-protein	unknown	unknown	gnl\|CDD\|378635
NZ_AP019735.1\|WP_141413598.1\|1700500_1702045_-\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|379837
NZ_AP019735.1\|WP_141412620.1\|1689481_1691236_+\|DUF4091-domain-containing-protein	unknown	unknown	gnl\|CDD\|379121
NZ_AP019735.1\|WP_141412623.1\|1696794_1697268_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019130476.1\|1702148_1703948_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_AP019735.1\|WP_141412614.1\|1680067_1682107_+\|beta-galactosidase	unknown	unknown	gnl\|CDD\|225789
NZ_AP019735.1\|WP_141412625.1\|1697781_1699176_-\|C10-family-peptidase	unknown	unknown	gnl\|CDD\|366737
NZ_AP019735.1\|WP_141413597.1\|1688056_1689286_+\|acyloxyacyl-hydrolase	unknown	unknown	gnl\|CDD\|378181
NZ_AP019735.1\|WP_141412622.1\|1696277_1696781_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412617.1\|1685446_1685878_+\|radical-SAM-associated-putative-lipoprotein	unknown	unknown	gnl\|CDD\|200385
NZ_AP019735.1\|WP_141412624.1\|1697280_1697766_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_019130483.1\|1694365_1695148_+\|alpha/beta-hydrolase-fold-domain-containing-protein	gnl\|CDD\|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	1.18279e-17
NZ_AP019735.1\|WP_141412618.1\|1685879_1686959_+\|TIGR04133-family-radical-SAM/SPASM-protein	gnl\|CDD\|200384	TIGR04133, coenzyme_PQQ_synthesis_protein_E, radical SAM enzyme, rSAM/lipoprotein system. Members of this protein family are radical SAM enzymes with an additional 4Fe4S cluster-binding C-terminal domain (TIGR04085) shared with PqqE and many other peptide and protein-modifying radical SAM enzymes. All members occur in the context of a predicted lipoprotein that usually is encoded by an adjacent gene.	0
NZ_AP019735.1\|WP_141412615.1\|1682030_1682630_-\|WbqC-family-protein	gnl\|CDD\|378083	pfam08889, WbqC, WbqC-like protein family. This family of proteins are functionally uncharacterized. However it is found in an O-antigen gene cluster in E. coli and other bacteria suggesting a role in O-antigen production. Feng et al. suggest that wbnG may code for a glycine transferase.	2.32907e-39
NZ_AP019735.1\|WP_019130492.1\|1682752_1683874_+\|acyltransferase	gnl\|CDD\|224748	COG1835, COG1835, Predicted acyltransferases [Lipid metabolism].	8.11538e-34
NZ_AP019735.1\|WP_141412616.1\|1683883_1685371_-\|(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate-synthase	gnl\|CDD\|179361	PRK02048, PRK02048, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional.	2.99664e-127
NZ_AP019735.1\|WP_141412626.1\|1699315_1700182_-\|HAD-IIA-family-hydrolase	gnl\|CDD\|319858	cd16422, HAD_Pase_UmpH-like, uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily. This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	3.99198e-86
NZ_AP019735.1\|WP_141412621.1\|1691243_1693355_+\|ATP-dependent-DNA-helicase-RecG	gnl\|CDD\|236794	PRK10917, PRK10917, ATP-dependent DNA helicase RecG; Provisional.	0
NZ_AP019735.1\|WP_026074911.1\|1693565_1694363_+\|DUF3108-domain-containing-protein	gnl\|CDD\|378635	pfam11306, DUF3108, Protein of unknown function (DUF3108). This is a bacterial family of putative lipoproteins. Structure 3fzx, the first structural template for this large family including several homologs in the human gut microbiome and in metagenomic datasets, folds into a beta barrel that topologically looks like a small-scale porin (such as FepA). Bacteroides fragilis glyA is a putative exported protein, and this fold is of the YmcC-like type, with a predicted signal peptide SpI cleavage site AGAMA\|QNQDC, and a Phobius server prediction of non-cytoplasmic localization for amino acids 21-236. The possibility of it being a membrane protein can be ruled out by the hydrophilic nature of the solvent exposed surface outside the barrels. Analysis of sequence conservation suggests that an area near Glu172/Trp206 is potentially interesting. These two residues are also conserved in Dali hit Structure 2in5, a hypothetical lipoprotein classified as a new YmcC-like fold in SCOP (SCOP:159271, with a 12-stranded meander beta-sheet folded into a deformed beta-barrel) despite large structural differences between the two structures, suggesting similarity in function.	1.31241e-47
NZ_AP019735.1\|WP_141413598.1\|1700500_1702045_-\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	gnl\|CDD\|379837	pfam16370, MetallophosC, C terminal of Calcineurin-like phosphoesterase. This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.	4.80744e-50
NZ_AP019735.1\|WP_141412620.1\|1689481_1691236_+\|DUF4091-domain-containing-protein	gnl\|CDD\|379121	pfam13320, DUF4091, Domain of unknown function (DUF4091). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length. There is a single completely conserved residue G that may be functionally important.	3.23064e-26
NZ_AP019735.1\|WP_019130476.1\|1702148_1703948_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	2.21336e-39
NZ_AP019735.1\|WP_141412614.1\|1680067_1682107_+\|beta-galactosidase	gnl\|CDD\|225789	COG3250, LacZ, Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].	2.20501e-42
NZ_AP019735.1\|WP_141412625.1\|1697781_1699176_-\|C10-family-peptidase	gnl\|CDD\|366737	pfam01640, Peptidase_C10, Peptidase C10 family. This family represents just the active peptide part of these proteins. Residues 1-120 are not part of the model as they form the pro-peptide, which before cleavage blocks the active site from the substrate. The catalytic residues of histidine and cysteine are brought close together at the active site by the folding of the active peptide.	1.2391e-14
NZ_AP019735.1\|WP_141413597.1\|1688056_1689286_+\|acyloxyacyl-hydrolase	gnl\|CDD\|378181	pfam09411, PagL, Lipid A 3-O-deacylase (PagL). PagL is an outer membrane protein with lipid A 3-O-deacylase activity. It forms an 8 stranded beta barrel structure.	4.18277e-06
NZ_AP019735.1\|WP_141412617.1\|1685446_1685878_+\|radical-SAM-associated-putative-lipoprotein	gnl\|CDD\|200385	TIGR04134, hypothetical_protein, putative lipoprotein, rSAM/lipoprotein system. Members of this family are Bacteroidetes lineage putative lipoproteins that always occur in pairs with a radical SAM enzyme, TIGR04133, from a branch of the radical SAM superfamily in which many members perform peptide or protein modifications. In some members, the region distal to the Cys of the putative lipoprotein cleavage motif is duplicated.	2.72012e-23

>NZ_AP019735.1|WP_141412621.1|1691243_1693355_+|ATP-dependent-DNA-helicase-RecG
MGNWYTDDVKYIAGVGEARAKLLDKELGIATVGDLLYHFPFRYIDRTKIYRIAEIGASGQTLVQFRGRVTGVAYAGAGRKRRFTAYVADATGQAELVWFQGIKWIEKRIEVGREYLVFGRPSFFRNELSLVHPEVETVEKALSRRAESGLQGIYSSTERLSSVLGTKGFHTIVSNAWRIAGERIGETLPPEMRRQYGLATLREALYNIHFPQSPEALRQAQYRLKFEELLGVQLNVMARRSERLARNDGFYFARVGESFNTFYREKLPFPLTGAQKRVVREIRQDTVTGYQMNRLLQGDVGSGKTLVALLSMLLAVDNGFQACMMAPTEILARQHYATLTRLLDGLSVRVAILTGASKARERRAALEGVASGEVQLLVGTHALIEDRVRFANLGLVVIDEQHRFGVEQRARMWTKNEQPPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRRPVRTVHYTDAARLRVWGFLRQEIARGRQAYVVYPLIEESESMDYKDLQDGYEAISRDFPLPEYVVEVVHGRMKPEDKEAAMRRFKSGEAQILVSTTVIEVGVDVPNATVMVIESAERFGLSQLHQLRGRVGRGAEQSYCILMSGEKLSKEARARLDAMCQTNDGFRLAELDLKLRGAGDIAGTQQSGMAFDLKIANPTLDVQILQLTRDAAGGVLAADAALAAPEHAGLRELKRRYSGEKSIDFSMIS
>NZ_AP019735.1|WP_141412620.1|1689481_1691236_+|DUF4091-domain-containing-protein
MKRTLSFLLPAAAMLLAACGGANDRPSFPDFQEMADPAAAFADWSAAGDTPCASFVTTDRRFGKSQLPDVEPRTACRLTAWRGERVSAQLLVWSAQPVERLVCTAGVLTSDEGRLPESAVRTRFVRYVMSDEFACGCCKRKPQDFAAVLTADMLDERPSMALEACTVRPVWITVDVPQDAAPGLYRTPVTVACDGDEQRLELAVEVTGRTLPAPSEWRYHLDLWQHPAAVARVEGTEMWSDAHFEALRPVMKPLADAGQKVVTATLNKDPWNNQCYDAYADMIVWTKGADGAWTYDYAAFDRWVEFMEGLGVDKQINCYSMLPWNNMLHYRDAATGEWVDVKAEPGQPAFDEMWRPFLADFVRHLEEKGWLAKTCIAMDERSPEQMEIAVAFLAEHAPQLGIALADNHDSYKRYPQLHDICVSARQEVAPEDIAARRAAGQVTTYYVCCSHRYPNMFTFSDPVEATVAAWYAVANGYDGFLRWAYNSWTEDPLRDSRFRTWPAGDTYVIYPGGRSSIRFERLREGIQDAEKIRILRAEAGRGNSAGADEKRARLEAVIAPFASREPAADLHERLAEAKRVLNEL
>NZ_AP019735.1|WP_141413597.1|1688056_1689286_+|acyloxyacyl-hydrolase
MRVISASFAAVLLCLTVVSLPAPVRGESLRRPTPDSLARPEALVHKFGLDVSPGALFRTDDFFKGANAAGKEFGTTLSVHLKYAFQFGPETRFGRNYPFTYQGVGLGYNTFFNSAEVGTPVALYVFQHARIAALTERLSLDYEWNFGLSFGWKPFDEQTNPFNTVVGSKINAYINLGLMLNWRFAPRWSLTAGVGLTHFSNGNTRYPNGGVNLIGGRVGVMRTFGRDAADDRRAAVRRSDPFRPYVSYDVILYGALRKKGFLQESRAYLIPGSFAVAGLNFTPMYNFSRFFRAGLSLDAQYDESANLKDHIANDYPLADELKFHRPPFKEQFAVGVSIRCEVVMPIFSINLGIGKNLIGRGDDTNSFYQVFALKADVACNVFLHVGYQLYKFRNPNNLMLGVGYRFNGR
>NZ_AP019735.1|WP_141412619.1|1687092_1688052_+|hypothetical-protein
MRKLFSRYALSAIVAPLLAVGCNDGVFIDDFLPEAPSVTVGPDDTSATIRFEAGNWDILSVEGPTTSLRGDIYDAEGNLLYGNHLLYGDGLLRMTYDDGLLDFGIERNDYRTLRITLGESLRDEPWETRILVGNDYESETVSVTFAPTEKYRVDSVVYRWDEFESWDNSIELQDAFTIDNTASSEPASVVVSPFRNAKRTVRFWPDDFNDRREEIFGVPLPEIVIPDMADGAPVVAESSARFARNDQQLPLSFPDDEQVTVTAKPHERLNVEVYLSLEQFRVPYTVYASGPAGRQRTFTGTLHSSLPYDYLILKPKTDE
>NZ_AP019735.1|WP_141412618.1|1685879_1686959_+|TIGR04133-family-radical-SAM/SPASM-protein
MDGRHLSLRKRLGLELYRRLHREAVERHELRTLFWECTLRCNLRCGHCGSDCTASPDCQDMPAEDFFRVLDRQITPRVDPHRVMVVLSGGEVLVRSDLERIGRALYDREYPWGMVTNGMALTPQRFDGLLGAGLHSMTVSIDGFEAEHNRLRRHPLSFVRAAEAVRMAAAEPSIAFDAVTCVTPALVPRLDEFKEYLLSLGLRSWRLFAIFPAGRAAEDPALQLSDGQFRALMEFVRRTRREGRIACSYACEGFLGGYEMEARDHFYHCDAGVSVASIRVDGAISGCTSVRADYAQGNIYRDDFWQVWTERFEPFRRREWMRRGACADCAAWRYCEGGPMHLRDADGGMMHCSYRRLCR
>NZ_AP019735.1|WP_141412617.1|1685446_1685878_+|radical-SAM-associated-putative-lipoprotein
MNKLWMLLLSLLGFAGCDEPQEDMYGTPYAEYTVKGRVTDAAGTPIAGIEVRRSSWGSDPSAVRTDTRGAYTFEADGNVLYMPPVLTFTDTDGPAGGGDFAGKEVEVAFAESDRTGPGEGNWMYGRFERSGVDVVLAEKTGEE
>NZ_AP019735.1|WP_141412616.1|1683883_1685371_-|(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate-synthase
MIDLTQYRRRATHEVRIGACTIGGTHPVAVQSMTNTDTRDTAACVAQIERIARAGAPIVRLTAQGVREAENLRDITERLRADGNTTALVADIHFLPEAAAVAAQYVDKVRINPGNYRLDRGELEALVARCRERGVALRIGVNHGSLSKRIFDEWGDTPEGMVAAAMEFLHVCRREAFDQVVVSMKSSNTRVMVAAYRLLVEAMEREGMTYPIHLGVTEAGNGLEGRIKSAVGIGALLADGIGDTIRVSLTEAPENEIPVARLLADHFRERPGTFEVKHPERYSPTVYRRRSSVQTPVVRDEITSAFRLLESTSQNPTAELRAAILSLDGDEPAAVVRRYDDTDLTTLAVKAAADLGPLFLDGLADGIRILDDRFTEAQLRDVELMILQAARVRFSHTEYIACPSCGRTLYDIEGTLAQIKARTSHLKNLKIGVMGCIVNGPGEMADADYGYVGAAPGRITLYKGRTVVERNIPQEEALDRLIALIRENGDWQEPE
>NZ_AP019735.1|WP_019130492.1|1682752_1683874_+|acyltransferase
MPQTSLPSAAYADSKPHYDILDGLRGVAALLVVVFHLCEAHATSHFDQLLNHGYLAVDFFFALSGFVIGYAYDDRWGRMTVGGFFKRRLIRLQPMVVLGMAVGAALFYFQDCDMWPVHAVPVWKMLAVMLVGMTLLPVPVSMDVRGWQEMHPLNGPGWSLFYEYCANILYALVVRRFPKWLLGVLVAVSGAALIRFALTSPSGDIIGGWSLTAEQLGVGFTRMMYPFFGGLLLSRLVRPGHVRRAFWWCSLGLVALLAVPRVGGTEHLWQNGLYDALVVVVLFPLIVWTGASGTVTGRSARVCEFLGDISYPIYITHYPLVYTYTAWVRNHGLTLGEAWPAAAGTVVVSVLLAYAALKWYDEPVRRWLRREFM
>NZ_AP019735.1|WP_141412615.1|1682030_1682630_-|WbqC-family-protein
MTILPAAYLPSIEYCARWAQGPCVVDGGEHFVKRSERNRTHILTAGGVLALTVQAVRANRPRTPMRDVRIDYSKRWQHQHWTALVSAYKASPYFDHYAPRFEPFYTRRYEFLFDYDLRLMETIAELLGLPMPAVSEAYLTADEGDLDLRPKRKEGADFASPPYIQVFSDRLPFTPNLSIADLLFCEGPQSPALLKQCRL
>NZ_AP019735.1|WP_141412614.1|1680067_1682107_+|beta-galactosidase
MKRYLLLISMLAAFVAESAAREVYRLNDDWTFYFRSENSADDARNITLPHTWNLDALAGNSEYQRTTGNYMRRLYIPADWASKRLFLRFDGVQTVADVFVNGYHVGEHRGGFTAFTFEITGRVKFGAENRLLVVVSNTFQNDVLPTSTEQNVYGGIYRDVDLILTDRVAVSPTVWGTDGLFVEQVSVDDDAVEGRAAVYVSAPKDCQGMITLTVRDPDGYVVVEKTQKNNRTAGEPVTIPFTVDAPRLWSPAAPNLYTVTARVACDSLSDEVTVRTGFRRIAASGRGLLVNGDTVRLHGVALYHDRASVANAFTAADYDEDLAFVHDVGANAVHSVSGPHDQYLYDRLDERGLMAWIDLPLMRSPYLGDVFYFPTERFRANGREQLREIVAQNFNHPSVVMWGIFSLVWQRGDDVTPYIRELHTALKRVDPSRPTVALSNQDGELNTITDLIALKQNVGWMRGTTDDVGYWCETLHKSWGNLLAAPCYGVPGYPSQQDDLLGRPTPGTHWLPERWQTRFHEEYARRIVSDPAFWGEWVNAMFDFGTARGANDRYACGMVTLDRRQKKDIYYLYRTLWNRREPTLYIAERRWRVRPSAEQRIKVYSSGEDPVLLVNGDSVALTKYAEGQFRADCKLLPGENRIEARCGELRDSVALRVGTALKARDFEALRKTKGLRSKD
>NZ_AP019735.1|WP_026074911.1|1693565_1694363_+|DUF3108-domain-containing-protein
MKRILILFLLTGGIFSAAGQIYVPGEELFYRVSYRAKLVPNTEVATVVVRTSEVELDGQTVYNVFGQGKTLASFRWFFSLDDRYNIWVDTATLRTVRFTSDIHEGGYTFRSRFDYDWPARRVATRWQRRTLPENRKEMALTDVSMDAVSLFFNMRSADAASFRVGEQRVLQMVLEDTIRHLRYRFEGREVKKIRNMGKFNTLKFACQIGTSESFSFTDGSEFFIWLSDDENKIPLHLESPIRVGSVNAYITGYKGLKYPLTSKIR
>NZ_AP019735.1|WP_019130483.1|1694365_1695148_+|alpha/beta-hydrolase-fold-domain-containing-protein
MKLTQIDLAEGRGGSQREVSASEAVARAEEACGGTLLLFEPDGAPRAAVAICPGGGFGKVNTEHEGVAFAEWFVAHGIAAGVVKYRLPEGDPALPQQDVERAAELLRNRFDGVKTGVLGASIGGYLAACAALAQPAARRPDFQLLFYPVVSMEEEFAHRPSMLRMFGRELHGLEAKRRSPLYRIDRAAPPAFLAAAADDGAVTPLGACRYAECLLAAGAGAALHLYPSGGHGFGLRREFAWREALVGELRMWLDATIGTV
>NZ_AP019735.1|WP_019130482.1|1695199_1696135_+|hypothetical-protein
MEENKDYNPSQYEDDDRMEAPKSAKSIRGYQTIIVILAVILAALSILYFNIHRQQQEEYDLLLVDRDSIKSNLSHLMEDFDNLQISNDSISQSLGLERSRADSLMERLTKERSWSYAKIKKYEKEIGTMRTIMRGYLRQIDSLNTLNKNLIKENVSYRKEISSANLRAEVAEEKASELSTKVRQGAVIRARGIRLVPLNARDKEVSRVKNASRLRVEFTLAGNDLAEPGERTVYVRITSPDGYVQSNASAATFEFEGERLTYTASRDVDYQNEDLAVGVYYNDGAGFTAGTYRVEVYADGRLAGQSDIVLR
>NZ_AP019735.1|WP_141412622.1|1696277_1696781_-|hypothetical-protein
MKKIFAILIALSALSNFSCKEKEEEYTEGGLVFGGIYMLDGQQLVETDGYILELPAEQNTVELRIVSKGVQEFGIGGYSMSGLGEYKVEGFTIKVTPDPASEKLEIYDYIDVEYKGEQHCVPRYLQTLHLGADTNTGQQKEIRIRFITNIPNYWMEWSQLTVRQAGR
>NZ_AP019735.1|WP_141412623.1|1696794_1697268_-|hypothetical-protein
MKKLITVLLALGAMLSTSCKDDVDFEGGVYLAHDVFLLDGDELILLHEHTIDIDSKQRDVDLQIVSEGAVKIEKLDQSPEITLTILTGFTGDDAVIYDYIPIKVDGETRNIPRYVQTLRIIAETNGQKQARDCRFRIITQNPMPECADITIRQAGAK
>NZ_AP019735.1|WP_141412624.1|1697280_1697766_-|hypothetical-protein
MKKHTTISIALLALLCCACEEKQVGGDWDFHDAYILDGENLIEAHGYTVELPAQQCTVDLQIVSSGIYNQQSIDLDHFGMNLPDAISVTLTKKLEEAEIYDYTVDSWGVVHKDRPRYLQTVSISAKQNAFKLPRIVKFRIWTPGALDSSAADITVRQAGTK
>NZ_AP019735.1|WP_141412625.1|1697781_1699176_-|C10-family-peptidase
MKPNKTLFGAFVISVTLIIGACQQTELSDSAPTPSLPAPAAEFVADDSDLSAGDAAAVARIFRNGNRPTRAGSGAVVRNVVTIRDAAGRPAIYAVNLQEGYLLISATKRCYPILAQIDRGTFTLDREPSGLDVVLQEMTETIEAARDSAAVFDCRSAWLPYEERTRPERVQTRMTDDEFYDIQNEWYGKWFAEGADTYRLAIKPDDMPEDAYQRFCETAIGDDAWVDTPYNCMESGIITVKYHESGTKKGPFLTTKWRQYAPYNSQIGGEKPLGCVTIAVGQLMRYYQHPAYFNWSDMPDETSNSTLSSFLAQLHGELRVSDSGSSNIDHAKRVLESYGYSCSKRSHNASTVYTMLNSNLPVYTDGQDRARDKGHAWVIDGSNSITAYTEYKLYALNNGLPRPWYIELDSERVYHAQNVFFHMNWGQYANQDGWFLDSSIQFPNKNNEICNYSSDRQDLLITGF
>NZ_AP019735.1|WP_141412626.1|1699315_1700182_-|HAD-IIA-family-hydrolase
MATIDSYRSPFPHEELLERARRIRHVALDMDGTIYMGMSLFPWTKRFLSDLTEMGIGYSFLTNNPSKSIADYLHKLETLGIEATREEMYTTALATIDYIRSHYPTAKRLFLLGTPSMISEFEAAGFESTADSADDVPDVVVAAFDMTLTYPRLCRAAWWASQGIPYIATNPDRVCPTDQPVVLVDCGSICKCLEHATGRTPDIVLGKPDPNMLTGIKERFGLRADEIAMVGDRIYTDVAMARNAGALGVLVLSGETTEEVASAADPQPDVTALSLKEFGELLKEAHGK
>NZ_AP019735.1|WP_141413598.1|1700500_1702045_-|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein
MLFAAGALFAGCSDDDTQAPLNTPIQEGNNLYGVVTDPNGAPVGGIVVSDGFSCVATDANGVYQMPRHADAFHVFYRIPADREIPMSEGRPCFWQRLSKTQERYDFVLMPQQAVETDFKLVCIADPQVQKDTDLARFKEESVPDIRAHVSTLEGPVYGITLGDIIFNERSKDVTNQMMPPIALAMRESEIGLKLFQVMGNHDNCMTPTVTDESSNFDLAGRRNFEYKFGPCDYSFDRGNAHIVAMDDVLLTDEKHNPSDYEGGFTDAQVEWLRQDLSLVPKEKLVIFCVHIPLRNATSFNRETVRNLLKEFDNVHIMAGHTHYAQNYIDGDVYEHIHGAVCGAWWKSTINVDGTPNGYGVYDISGSKIENWYYKPTRLSKDFQIRMYRGETTFAGGYKFTYTASDEIVANIWNSDDRNWKVEVYENGNKTGEMTREKSLDAWGAGYHVGVLSANPDSHGKTTYDHFYHYKLKDAKAAVEIRATDCFGKVYTQNVFTTAAETDYPMVDNYPAIAE
>NZ_AP019735.1|WP_019130476.1|1702148_1703948_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKRIIYAALACLTFASCEDFLDKQPIEQIGTDEYFKDEASLEKYTNGFLNSYTPSSGDVTRGDGNCDIIEVKQTSSYLYQPVWNSSLQGGWSNSTWNFVYYINTFLERMHEAQGVSEAAFAHYEGTARFWRAWNYFELVKTFGGVPWYDHVVRSDSEEDLYKPRDSREYVMERVLEDLNYACEHCYTSEAWVNNQKINRYIALAIKSRICLFEGTYRKYHRVDPSTGKAWDPEYNKDNKWLREAADACEELMEAGVYSLVNSPADVATQYRSLFTSPSVLKQEVMWAREYNDEKNVRHDVTWYFTSGSMGQGWSLDADFVYTYLNRDGSRFTDRADYKSTTYAEQFENRDYRLQQTVISPEYRKLVGGTSKLFAPDLSVSYTGYQVIKFNIDDDSYEASGICWNCLPILRYAEVLLNYAEAKAELGEFDDAVWDKTIKPLRERAGVDGTRPTKIDEYLQNAYYSTDDGNPKITDCDILEIRRERAIELLLEGRRYDDLMRWHLGGLLNKQWYGIYIGEVDKAYDLNNDGVNDVCVTDKAGSEPGVKYIVRNSERALEDGASGRLVYNLQRYFNEQRYVHPIPKTALDKNPDLGQNVAWK

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Crispr_ID: NZ_AP019735_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_10

1736407-1736507

Orphan

Consensus_repeat	Method
ATTTCTTTCGTCCGTTTCTCGCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_10

>merge|NZ_AP019735|10|1736407-1736507|CRISPRCasFinder
ATTTCTTTCGTCCGTTTCTCGCCATGGCATAGCTCGCGCAAGCGCGGCTCTGCCCATTCGGCTTAGCGAAAACGTTGAATTTCTTTCGTCCATTTCTCGCC

>NZ_AP019735|10|10|1736407-1736507|CRISPRCasFinder
ATTTCTTTCGTCCGTTTCTCGCC	ATGGCATAGCTCGCGCAAGCGCGGCTCTGCCCATTCGGCTTAGCGAAAACGTTGA
ATTTCTTTCGTCCATTTCTCGCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141412641.1\|1738582_1739341_-\|triose-phosphate-isomerase	unknown	unknown	gnl\|CDD\|234589
NZ_AP019735.1\|WP_141412643.1\|1742269_1743769_-\|MBOAT-family-protein	unknown	unknown	gnl\|CDD\|224610
NZ_AP019735.1\|WP_141412638.1\|1729865_1731446_-\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|379837
NZ_AP019735.1\|WP_141412645.1\|1746174_1746921_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|187604
NZ_AP019735.1\|WP_019130453.1\|1739733_1741464_-\|lysine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234778
NZ_AP019735.1\|WP_019130454.1\|1739337_1739718_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412633.1\|1719170_1720388_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_AP019735.1\|WP_141412640.1\|1737000_1738188_-\|histidinol-phosphatase	unknown	unknown	gnl\|CDD\|213996
NZ_AP019735.1\|WP_141412644.1\|1743773_1745390_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238863
NZ_AP019735.1\|WP_141412642.1\|1741581_1742262_-\|phosphatase-PAP2-family-protein	unknown	unknown	gnl\|CDD\|239489
NZ_AP019735.1\|WP_019130459.1\|1731465_1733268_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_AP019735.1\|WP_019130464.1\|1724952_1725954_-\|2-hydroxyacid-dehydrogenase	unknown	unknown	gnl\|CDD\|240659
NZ_AP019735.1\|WP_026074907.1\|1745390_1746083_-\|zinc-metallopeptidase	unknown	unknown	gnl\|CDD\|377289
NZ_AP019735.1\|WP_141412634.1\|1723497_1724895_+\|efflux-transporter-outer-membrane-subunit	unknown	unknown	gnl\|CDD\|273830
NZ_AP019735.1\|WP_141412635.1\|1726247_1726706_-\|Hsp20-family-protein	unknown	unknown	gnl\|CDD\|223149
NZ_AP019735.1\|WP_141412636.1\|1726995_1728081_-\|TIM-barrel-protein	unknown	unknown	gnl\|CDD\|224007
NZ_AP019735.1\|WP_141413599.1\|1746999_1748241_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|226957
NZ_AP019735.1\|WP_141412637.1\|1728151_1729837_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412639.1\|1733282_1736372_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_AP019735.1\|WP_019130466.1\|1720397_1723511_+\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141412641.1\|1738582_1739341_-\|triose-phosphate-isomerase	gnl\|CDD\|234589	PRK00042, tpiA, triosephosphate isomerase; Provisional.	3.11099e-141
NZ_AP019735.1\|WP_141412643.1\|1742269_1743769_-\|MBOAT-family-protein	gnl\|CDD\|224610	COG1696, DltB, Predicted membrane protein involved in D-alanine export [Cell envelope biogenesis, outer membrane].	2.15407e-82
NZ_AP019735.1\|WP_141412638.1\|1729865_1731446_-\|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein	gnl\|CDD\|379837	pfam16370, MetallophosC, C terminal of Calcineurin-like phosphoesterase. This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.	1.32236e-42
NZ_AP019735.1\|WP_141412645.1\|1746174_1746921_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|187604	cd05346, SDR_c5, classical (c) SDR, subgroup 5. These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	1.92393e-112
NZ_AP019735.1\|WP_019130453.1\|1739733_1741464_-\|lysine--tRNA-ligase	gnl\|CDD\|234778	PRK00484, lysS, lysyl-tRNA synthetase; Reviewed.	0
NZ_AP019735.1\|WP_141412633.1\|1719170_1720388_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	1.4494e-84
NZ_AP019735.1\|WP_141412640.1\|1737000_1738188_-\|histidinol-phosphatase	gnl\|CDD\|213996	cd12112, PHP_HisPPase_Chlorobi_like, Polymerase and Histidinol Phosphatase domain of Chlorobi like. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. Chlorobi PHP is uncharacterized protein. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. The HisPPase can be classified into two types: the bifunctional Hisppase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.	4.47419e-114
NZ_AP019735.1\|WP_141412644.1\|1743773_1745390_-\|hypothetical-protein	gnl\|CDD\|238863	cd01825, SGNH_hydrolase_peri1, SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.	8.91876e-27
NZ_AP019735.1\|WP_141412642.1\|1741581_1742262_-\|phosphatase-PAP2-family-protein	gnl\|CDD\|239489	cd03395, PAP2_like_4, PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.	1.19233e-22
NZ_AP019735.1\|WP_019130459.1\|1731465_1733268_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	7.90125e-51
NZ_AP019735.1\|WP_019130464.1\|1724952_1725954_-\|2-hydroxyacid-dehydrogenase	gnl\|CDD\|240659	cd12183, LDH_like_2, D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains. D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.	0
NZ_AP019735.1\|WP_026074907.1\|1745390_1746083_-\|zinc-metallopeptidase	gnl\|CDD\|377289	pfam04298, Zn_peptidase_2, Putative neutral zinc metallopeptidase. Zinc metallopeptidase zinc binding regions have been predicted in some family members by a pattern match (Prosite:PS00142), of the characteristic HEXXH motif.	9.01872e-103
NZ_AP019735.1\|WP_141412634.1\|1723497_1724895_+\|efflux-transporter-outer-membrane-subunit	gnl\|CDD\|273830	TIGR01845, Outer_membrane_protein_OprM, efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family. Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins].	1.02951e-78
NZ_AP019735.1\|WP_141412635.1\|1726247_1726706_-\|Hsp20-family-protein	gnl\|CDD\|223149	COG0071, IbpA, Molecular chaperone (small heat shock protein) [Posttranslational modification, protein turnover, chaperones].	5.64995e-28
NZ_AP019735.1\|WP_141412636.1\|1726995_1728081_-\|TIM-barrel-protein	gnl\|CDD\|224007	COG1082, IolE, Sugar phosphate isomerases/epimerases [Carbohydrate transport and metabolism].	2.1581e-10
NZ_AP019735.1\|WP_141413599.1\|1746999_1748241_+\|ABC-transporter-permease	gnl\|CDD\|226957	COG4591, LolE, ABC-type transport system, involved in lipoprotein release, permease component [Cell envelope biogenesis, outer membrane].	9.1071e-57
NZ_AP019735.1\|WP_141412639.1\|1733282_1736372_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_AP019735.1\|WP_019130466.1\|1720397_1723511_+\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0

>NZ_AP019735.1|WP_141412639.1|1733282_1736372_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKKLLHPLTRLLLAVGLSAFSVVAFAQKTAVNGIVTDAEGAPLVGATVIVMQNARPEGGGTTTNTEGKFTVNASQGQQLAVSYIGYREATVEVTSKTFYEIALQSDSEQIDDVVVVGYGTQKKVNVTGSVSTIDASTFEKRPVVSASVALQGMAPGVTVTTPSGAPGADGGAIRIRGINSFGGSSTAPLVLIDGIEGSLDSVDPVLIESISILKDAASSSIYGSRAANGVILVTTKRSSTERFTVTYKGTVGWQSPTDLPETVNALEYRELTNAMNLQDGNAPTYDDESMALYRKNMGKDPDLYPNTDWQDAVLTGSGLSHSHTVSLGIGSERVRMLTTLGYVDQNGIIETTDFQRYTFRNNADVKFNDKLSMKLDLSFSNGDRRSSPYQGTIFNYMNTRSADIPNQFSTGLYNGLGLQGNNPVALMLEGGQNKNNTLRLSGAITLTYEPVEWLSLQGMLAPRYATTNKHNWKKPVTTYQDMEGTATLTSTPYATLTESGSRAFYGNYNFLMTFKKNFSGHDLKLILGAERNTYDYKYLSAYRQVFNYPDYDQIDVGEIENMDNSGHRYEWAIQSYFGRLNYNFKERYLLEANLRIDGSSRFSKSNRWGYFPSVSGAWRISEEPFMENAKHILDGLKIRASYGTLGNQNLAGGDAASYYPTTPNLALGHISMNGTPASLVTLNTLANPDIKWETTTMLDVGVDVTLFSKLNITADWYRKNTDDILMKLDIPAGVGLNAPYQNAGKVRNTGWELSIGYNNRWRDFTFGVQANVSDVKNEIVDMRGKTSTSGVLRNQEGYSIGSIYALESLGIIRTQEEADWVNANCPQFKETVQIGDIRYADIDGSNTIDENDKTIVGSTIPRYTYSLNLDFGWKGLRLSMLFQGVGKTDGYLNTYYVMPSNQGGTFRKEHIDFACAANPGGVTPRLTSANKNNWYDSSFWMKSAAYLRLKNIQLGYDLPKSWMRKIGLKSAYVYVNAQNLFTATNFWDGYDPEVGYDGDASGDFDLVKLGSANNYPQVKLVTIGLDLKF
>NZ_AP019735.1|WP_019130459.1|1731465_1733268_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKIILGAALCGLLAAGCSLDKSYLNGPNALTFPASKAEVEAGVFAAYKGLTLIDASSTPFPGIQDNASDIGASRLNAANYNYQQQSKLPTDNAWVEKVYNNIYKTAARANLVLDGIDKVRDLMSEQEYNMYKAELLLTRAYVYEWGCQLYGDIPYIDHVLGLGDSYTRTPRAEVIDKILNEDLKDEMLDFLPLRHNKATYGSTRLGRVGAYGLKARICLNWGFFEEAAKYADKALTLAKDAGYALEPYDTRFCGEDYTKGEPSATNLFGLSGHANSDEWIWALQYNAMISGNQHNAGYYAAPRIAGGCSYFSPTQMFIDAIQCTDGKSIAESPLFDYKEPWKNRDPRLDLFCVRPGSRVLGMQFETNPSVQKIMNYNDKEEGVLVANSEAYGTKSEYGANGSKGPCGYLWRKYLDIEEYRTNNGFGTKSVCTLSYPLMRLAELYLIRAEANIEWAGGDLGVAKADIETIRGRAHMPVLTVSDRNGLRSALRYERMVELCNEGFRWFDIRRWGIAEEVISGTLYAPASDGSMSNAIPTIDENWHVTYKGDTFDGKKINLRKFIDMAFDPMKDYLWPIPESERIALPQITQNPGYAGFAAE
>NZ_AP019735.1|WP_141412638.1|1729865_1731446_-|calcineurin-like-phosphoesterase-C-terminal-domain-containing-protein
MTSILKYLNRALLVLLLAAFAACSDNEGGNESNGNGDDGNTETPADGDTYGYIKDTNGNSVEGVVVSDGYSCTATDAEGRYALTRNADAGFVFYSLPSAYKVSVDKTYKLPRFFARLQAGTARYDFTLEALAAPEKRFDLICIGDPQINEASHAVRFKEEAGREIREYAASAGVPCYGITLGDHVNNKWTLFTNMVVALQPEQTGVPVFATIGNHDHEFPTADEKAARAKYESYFGPVDYSFNRGDVHVVSMDNVIHSCKASADYEGGFTAAQYAWLKQDLSFVPKDKMVILCVHIPFRGGWGTNSAHADADKYYDEVLDLLSQYEYAAIMSAHTHSNINYIHRKNGKEIFEHVTGTTCGAWWRSTVCTEGTPIGFGLYRIDGNRMEEWAYRSVRHDEQFQIRLYRASDTFVGGAKYRFKQTGADQIVANIWNWDPSWTVNVYENDVLSGQMTRNSDIDAWTVAYHIGLLNNTDSYRKSSDHMFHYTLKNPAAAVRVEAIDRFGNKYEQTVFTDPAEHPGDFHADF
>NZ_AP019735.1|WP_141412637.1|1728151_1729837_-|hypothetical-protein
MKKYLFLTLLAAAFLAGGGCSSSDDDGWGVIELASPKLKVTTELATATVTWDAVAKTAGYAYALDGAADYTSVDAATTTVTLTALAEGGHTFRLKAVGDLDHTTDSAERTIDFEIDPTLPQPAPTYVKGDEIGSVVVSWPAVKGAAGYAYKFGEAASFTEVGADVLSVTQKGLSAEEPIRFTMYAVGQLPDSNDSEPVSLTFQLVDTSEGVWVRKSNGELFELTESEAKIYTGTVSVSAADSFEILVENVPYGFLSYSGNGGVGTVNNDRACVPFYTYPAAEYYVRRSLGRMASDPLNKFWINLTADARIDLRIDCTQDPFRYDLQLVEADDPALILAQYFDLMVYGGDWIQAGKNAKSGRMGQSTDTALIDGTEPGEKEASYTTFGAKIASEGEASPAYLANRGLTGWGIAHCFEFPGYIRLSNTANSSGNMYGILTTPKLTALSGPTSITLTFDAVRFASTSDIPVKVLGAGTIKTASVRIEEGTAETAITPAADGQSIAITSTHCPKHANDDFKKWSCFTLTIDGATAETQIRWDTTGVGAESKDGRICLDNIAIRKN
>NZ_AP019735.1|WP_141412636.1|1726995_1728081_-|TIM-barrel-protein
MKHIVFFLTAALLLNASCGSSDEGGKTDPPAAPVPVAPTTELGKADEAIENLQLKPGKLISINQVNAANCRRAVAAGMCIDIMASDKIVFASDMTDERLDGLFAECGEAIRSTKADFWGLHLPYQTYDISSTNENTRVTAVLKLKRLIELTIEHLRPQHFVIHPNTGTILTTGGDFAERTAQSRKSLAELQRHIESCNAQHGTKAILCVENCARSLAYDGDSLLDLLDAEGLEKVRVCLDTGHALIPLNGKYIDPVCNGDALDVLRRIGTRLGTLHIQQNPGALDPTDPKDKHLEPFSGGLIDWGEFYYELLKNNRYRGCFLYEVSFKQVYDGDGSTIESTKSNYTNLIYPAFVRTVAAKK
>NZ_AP019735.1|WP_141412635.1|1726247_1726706_-|Hsp20-family-protein
MMPVMRNQNWLPSLFNDFFGDEWMGMQHKHASVPAINIIENEKDFRVELAVPGTTKEDFKVNVNADNELVISLEKRSEKEEKEGDKDKKEGHRGTYLRREFSYTSFQQSFSLPDDVDRQKISAKVENGVLTIDLPKKEVTPAAPVSHQIEIK
>NZ_AP019735.1|WP_019130464.1|1724952_1725954_-|2-hydroxyacid-dehydrogenase
MKPIVTFFGTQPYEQESFDALNRDFGFEFRYFKGHLSRQTVVATHGAQAACIFVNDTADAEVMRELARNGVRLLALRCAGYNNVDLEAARTFNIPVVRVPAYSPHAVAEYTVAMMLSLNRKIPRASWRTRDGNFSLQGLMGFDMNGKTVGVIGTGKIARIVIRILLGFGMEVLAYDPYPDGVFARETGIAYVSLDELYRRSDIITLHCPLTNETKHLVNETSIARMKRGVMIVNTGRGQLIQTEALIEALKSKQVGAAGLDVYEEEGDYFYEDRSDSIIDDDTLARLLLFPNVIVTSHQAFFTAEAMHNITETTLQNIKDFFDGRPLVNAVTK
>NZ_AP019735.1|WP_141412634.1|1723497_1724895_+|efflux-transporter-outer-membrane-subunit
MKRDKIVYGALLCGVVLLCNSCMLGRRQIKSPELELPATVVADATDSLTMADMAWWNVYSDSTLTALIERTLERNKDMLAASARVRRMRALGRVARADQLPSVSGQLAADTEHNDYDGEAAKNDPEFDAKVSLAWELDLWGNLRWANRKAVAEYLATVDAQRALQMTLVAEVATAYYELVALDQELSIVRRTLQTRKEGVRQARLRFEGGLTSETALQQAKVELASTATLIPGLESRIALKEHQIALLAGAYPTLRIDRQTMEMHARLPERLKVGLPSELLKRRPDLRQSEQTLRAAEAAMGMASADRFPRITFSLTGGWENDDLKGLFSSPFSYVNGSLVSPLFSFGKKKAKYKAALAACDEARLNYEQKVLEAFREVNDAVVTYRNVRTAAALKRDLQQAAQKYVELAQLQYFNGVINYLDVLDAQRKYFDAQIGLSNAVRDEHLAMVDLYKALGGGWGVERE
>NZ_AP019735.1|WP_019130466.1|1720397_1723511_+|efflux-RND-transporter-permease-subunit
MKSDFFIDRPVFSTVLSVIIVIVGVIGLALLPIDQYPKIVPPVVKVSASYPGASAQTVTQAVATPIEQELNGTPGMLYMESSSTNSGGFTATITFDIDTDADLAAVEVQNRVKLAESRLPAEVVQNGISVEKQASSKLLTITLLSSDPKFDEIYLSNYATLNVLDMLRRVPGVGSVSNVGSRYYAMQIWVLPDRLANLGLTVQDLQRALKDQNRESAAGVLGQQPMTDLDVTIPITAQGRLSSVGEFEEIVVRANPDGSIIRLRDVARVSLEASSYNTESGINGGNAAVLNINMLPGANAMEVADAVKEAMEEISRNFPEGISYQIPFDMTTYISESIHHVYQTLFEALLLVILVVFLSLQNWRATLIPIVAVPISLIGTFGVMLVFGFSLNMMTLLGLILAIGIVVDDAIVVVENVERIMEQERLSPYEATKKAMASLGGALIAMSLVLCAVFVPVSFLAGITGQLYRQFTITIAVSVIISTVVALTLSPVMCAYFLRPDNGRRKPKLFRRINYWLRRGNTVYQRGIRGSLRHSRRMLAAFGILLVGIWLMNRITPQSFMPKEDQGYFTVELELPEGATLERTRRVTDRAMKYLMGLSDVEYVLNVTGSSPRLGSNQAHSQLTVILKPWGDRTSESIDELMEEVRDELSLYPESKVYLSSPAVIPGLGTSGGFEMVLEARGDRTYTDLQQAVDTLMYYAERRPELAGLSSSMQSDIPQLYYDVDRDKAQLLGVSMSDVFSTLKTFTGSVYVNDFNMFNRIYRVYVQAEAPYRAHQSNLDLFHVRGNGGAMIPVTALGTTHYTTGPGTIRRFNMFNAATISGEAAHGYSSGQAMEALEQIVREHLPANIGVEWSGLSYQEKHASGQTGLVLALALLFVFLFLAAQYESWSVPVAVILSLPIAGLGAYVGNWLCGLENNIYFQIGLVMLVGLVAKNAILIVEFAKEEVDRGGDLVQSALHAARLRFRPIVMTSLAFILGMLPLVFASGPGSASRQGIGTGVFFGMLVAISVGIVFVPFFFVWVYRIKDKFKRVSHEKR
>NZ_AP019735.1|WP_141412633.1|1719170_1720388_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MNPKVDKWVRKAGSWCEKACPQTRSGWIMIALTAVVIVAGVVWLLRPRSEAVHYPIVAVEPVATQNVEIYGEFVGRIRAQQFVEVRARVEGYLERMLFREGSYVKKGQTLFIIDPKIYRARVDKAKAQLNKDRALAQKAERDLKRIRPLYAQNAASQLDLDNATAAYESATANVLMSEADLMQAATALGYTTVQSPITGYISASNADIGTLVGPGGKSLLATIVKSDTVRVDFSMTGMDYLRSKERNVNLGQKDSTRRWNPYITVTLPDNSRYPLRGLVDFADPQVDPETGTFSVRAEMPNPDHILLPGQFTKVKLLLDVRENAVVVPSKAIVIEKGGAYIFVVRPDSVVEKRFIETGPELDNKTVVERGLLSGERIVVEGYHKLNHGMRVEAVEPRRDNGVASN
>NZ_AP019735.1|WP_141412640.1|1737000_1738188_-|histidinol-phosphatase
MKKLLFFCAALTATFTATGQHYYTDSANPDITRHSLRIAPQRVEFVLPEVGGYTVYKADLHTHSIYSDGDCTPEFRVREAWYDGLDVLAITEHVEYRRHEGKMLNFLKGYVPEGTEPVNYNIIAKPADEQGIRSDLNFPVKLAQETAAKYGITIIPGAEITREPIAYGHYNALFTTDNNAIYAADALQSLRNAKAQGALVMHNHPGWRRKSLEHPEFEVAAYGEGLIDGIEIMNGGEFYPKAISRAHAKNLFVSANTDIHDSATETYRAQGHRRNMTLIFAKENTLEALREAIEARRTLAYSFGTIAGDEQLLKDLFTASVRTSVLHTDAKGRRTVSLTNNSSVQYVLRLPGQNPFILNPFSTVTTTVAQNRPLRLTVENMWYSEQDHPQIELTL
>NZ_AP019735.1|WP_141412641.1|1738582_1739341_-|triose-phosphate-isomerase
MRKKIVAGNWKMNTLPAEGVELAKQVAAGKHTVCDCVSFIVCPPFTHLSEVSKTLEGTGIAVGAQNCAAEAKGAYTGEVAASMIAALGCKYVILGHSERRQYYGETSGTLNRKMEQAYANNLVPIYCVGENLDEREAGKHFDVVKAQIEEVVYNLTPEQFGKLVIAYEPVWAIGTGKTATAEQAQEIHAYIRKVLAAKFGAAAEECPILYGGSCKPSNAAEIFAKEDVDGGLIGGAALKAEDFLAIGKGFAK
>NZ_AP019735.1|WP_019130454.1|1739337_1739718_-|hypothetical-protein
MDRTRKLLLALAAAAVAATLLALRGWIAPATARWVLLALLGWYWVRFIVLPVDVIKRTKVLNAFAVTWWVNSFPILPAVTGAVLLWYGAPFERRVWGSLLLFIVVSALAGYLTIIRYNHKLKKSQQ
>NZ_AP019735.1|WP_019130453.1|1739733_1741464_-|lysine--tRNA-ligase
MAIELSEQEQLRRQSLAALRELGIDPYPAARFDVTATAREILDGYDEAKGNFADVRIAGRIMSRRIMGSVSFFELQDHTGRIQVYIRRDDICPEGDPTLYNTVFKKLLDIGDFVGIEGFAFVTKTGETSVHCRRLTVISKSLRPLPVVKEKDGQTFDAFTDPEVRYRQRYVDLAVNPQVREVFVKRSKIMAAMREFFNAKGYLEVETPILQPIPGGASARPFITHHNSLDVDLYLRIATELYLKKLIVGGFEGVYEFGKNFRNEGMDRTHNPEFTCMEIYVAYKDYLWMMEFTEQMLEHVALAANGTTDLTIDGKAVSFKAPFRRVTMTEAIREKTGYDITGQSEEQLREACRRLGVEVDETMGKGKLIDAIFGQYCEEELIQPTFVCDYPIEMSPLCKRHRDNPDLTERFELFVNGKELCNAYSELNDPIDQLERFQEQLRLLEKGDDEAMFIDMDFVRALEYGMPSCSGMGIGIDRLTMFLTGQSSIQDVLFFPQMRPEKKVQRDPDEAYAAIGVPAEWIPVIQKMGYLTVDALRKLPAGKFFNDLCGFNKKNKLGLKAPSIEEVKAWCAPAAE
>NZ_AP019735.1|WP_141412642.1|1741581_1742262_-|phosphatase-PAP2-family-protein
MIPLYTFDHALFLALNFDGGPVMDRLMTLVSGTAMWLPLYALILWLVWRREGWRRTLLFAAAIVLAIVLADMAAGIFKHSGPLKGLWADFPPRWRPMFTPSLEGLEIAPDTLMRWRFEGHATPGIVHVPEGALGGKFGTVSSHAATVVALLVLSAAEIRRRWFTFLMVAATLLICYSRIYLAKHFPVDLLLGAAVGALTGWAMLRVYRCIGRIRRPPLPEKRRRRA
>NZ_AP019735.1|WP_141412643.1|1742269_1743769_-|MBOAT-family-protein
MESLREIIDRVLPLLSYDPQAPMLFSSGLFLFLFSAFAFFYGFMRRTPALRIWYVIAFSLYFYYKSSGIYLLLLVGVSVSDFWIGRAIAHVSSRHAQRALVALSIAADLAVLGYFKYTNFFIEITRDLFGAGFLEFQNIFLPVGISFFLFQSLSYTIDIYRGSLKPVDRWGDYLFYLSFFPQLVAGPIVRARDFLVQIRQNPITVSREMFGTGIYLIAIGLFKKAVISDYISLNFVDRIFDDPALYSGMECLAAVYGYALQIYCDFSGYSDMAIGLALLLGFRFPKNFDAPYHSATITEFWRRWHISLSMWLRDYLYISLGGNRKGRLRTYFNLLVTMVLGGLWHGAAIRFVLWGTLHGVALALHKLWLSVVPGAKVSGYQMHPLSRLAGILVTFHLVCFGWLLFRADSMRTVQLMLHQITDNFHLQLLPQMLAGYGGVFALVGLGYLLHMLPGRADAAARRAVVASPFWVQVLLLASVAWGVMQIQSSSIQPFIYFQF
>NZ_AP019735.1|WP_141412644.1|1743773_1745390_-|hypothetical-protein
MAPQDYTRRSFQAAAALIAVLVCVAFIPPQTICGIPLRRANILSDVLRFDDKEAVDETLPELDDEFSGDFHRFAGQLDAGEAPLPADSIAAEPPAADTLSAAPQLAFEWTPADSEPPTEPPTGDTARLLTTLTPIEDFDTLADGPLYRFCARLADTARRTPVRIAVLGDSFIEGDILTADLREQLQLRYGGRGCGFAPMSSPLTGYRRTVGTRSAGWNSYNIMQRRTTPEALRGDYSVSGWLCRPADGATVRWTGSDFRRRLDRCGVARLLFISREPSRLELTLNDSLHRTFDIPASEALRQIVVRAPVASLALRVVRGGAGFTGYGVQFEDAAGVTVDNYSIRSNNGQALFGTNPSVNAQIDAFAEYDLVILQYGLNIMQEGVTNYSAYAARVEKMIAFVRSCFPEAAVLVLSTSDRSVKSDTGFAPMSSAPAMVDWQRRAARATGAAFWSVYDAMRAQGGMERFVANGWAGKDYTHINYAGGRQVAYALVDALDARVAAILRQRQQAALPEPVLDSSKIAALDETMNLRPQPIEPR
>NZ_AP019735.1|WP_026074907.1|1745390_1746083_-|zinc-metallopeptidase
MGSWILIIVIGIVGWIVQARLQSVFAKYARVPFPGGLTGAEVAEKMLRDNGIRNVKVTHVAGHLTDHFNPQTMTVNLSDSVYASRSVAAAAVAAHECGHAVQHARGYAPLELRSQLVPIVNFSARAATFVLIAGMILLATTDNAWVCWIGVGLIAVSALFSIVTLPVEYNASERALAWLESSRTMQGAELAQAREALTWAARTYLVAALSAIATVLYYAMLILGRGNNRD
>NZ_AP019735.1|WP_141412645.1|1746174_1746921_-|SDR-family-NAD(P)-dependent-oxidoreductase
MKKQALITGATSGIGRATALRLSADGWDVAATGRRAERLDALRREIEAAGGGCRTLAFDIRDEAACHAALDGLERIDLLVNNAGLAAGFEHLDRGSTADWNAMIDTNVKGLLYVSQIVARKMIAAGGGHIVNIGSIAGTEPYENGAVYCATKHAVHAISQSMRADLLSHGIKVSEVRPGMVETEFSVVRFHGDRTAADNVYRGVEPLTGDDIAEAIAWIAQLPAHMNVNEIVLMPSQQACQYYVHRKS
>NZ_AP019735.1|WP_141413599.1|1746999_1748241_+|ABC-transporter-permease
MNLEFFIARRTARTSPENRPGVMSRIAVVSVAVSVAVMLVALAVILGFKREVTARMVGFSAPVEVIDGAGIYAAESRPVAATARFEALLRAVDGVQRATPYAVKSGIVRTRDAMEGVALKGVDGSYDWSFFAGRLTEGRLPRVGDSLRTKELLLSARTARLLGVHAGDKVEMLFVAGDERPRRDRFKVSGLYSTGMEELERTALTDLRNVQRLSGWSSGEVSGYDLFLGDVRQADRLAEAVNDALLRSDLPETDGVVAVSVGERYPAVFDWLKAHDVNAAVVIAVMVAVAFFNMASALLILVLERTRMIGLLKAMGMENRRIRRIFLYRAAFIVGRGLLWGNLAAGLLCWLQARFHLLRLDPAGYMLSEVPVAVSAGWWLAVDVAAAGAILALLLVPAAFVARIRPDEAIKTD

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Crispr_ID: NZ_AP019735_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_11

1762140-1762247

Orphan

Consensus_repeat	Method
TTCTTCCATTTCTCGCCTCGGCAATTCGAGTAAACTCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_11

>merge|NZ_AP019735|11|1762140-1762247|CRISPRCasFinder
TTCTTCCATTTCTCGCCTCGGCAATTCGAGTAAACTCGGTTGCGCTCGGCTTGACGAAATGGTTGAATTTTTCTTCCATTTCTCGCCTCGGCAATTCGAGCAAACTCG

>NZ_AP019735|11|11|1762140-1762247|CRISPRCasFinder
TTCTTCCATTTCTCGCCTCGGCAATTCGAGTAAACTCG	GTTGCGCTCGGCTTGACGAAATGGTTGAATTT
TTCTTCCATTTCTCGCCTCGGCAATTCGAGCAAACTCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141412649.1\|1756001_1758554_-\|adenosylcobalamin-dependent-ribonucleoside-diphosphate-reductase	unknown	unknown	gnl\|CDD\|274168
NZ_AP019735.1\|WP_162851448.1\|1760131_1761793_+\|sulfatase-like-hydrolase/transferase	unknown	unknown	gnl\|CDD\|293763
NZ_AP019735.1\|WP_141412653.1\|1763644_1764229_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|183566
NZ_AP019735.1\|WP_141412654.1\|1765640_1767125_-\|proline--tRNA-ligase	unknown	unknown	gnl\|CDD\|236327
NZ_AP019735.1\|WP_141412657.1\|1770879_1771092_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141412658.1\|1771088_1771448_-\|DUF488-family-protein	unknown	unknown	gnl\|CDD\|225730
NZ_AP019735.1\|WP_141412660.1\|1773097_1773694_+\|flavin-reductase	unknown	unknown	gnl\|CDD\|224766
NZ_AP019735.1\|WP_141412648.1\|1752353_1753442_+\|DNA-replication-and-repair-protein-RecF	unknown	unknown	gnl\|CDD\|234608
NZ_AP019735.1\|WP_141412659.1\|1771539_1772892_-\|mechanosensitive-ion-channel	unknown	unknown	gnl\|CDD\|366370
NZ_AP019735.1\|WP_141412656.1\|1769157_1770279_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224429
NZ_AP019735.1\|WP_162502283.1\|1758747_1759212_-\|META-domain-containing-protein	unknown	unknown	gnl\|CDD\|377111
NZ_AP019735.1\|WP_141413601.1\|1754313_1755153_-\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|143586
NZ_AP019735.1\|WP_141412652.1\|1762791_1763181_+\|DUF4186-family-protein	unknown	unknown	gnl\|CDD\|372733
NZ_AP019735.1\|WP_141412655.1\|1767432_1769127_-\|transporter	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413600.1\|1753802_1754075_+\|DUF721-domain-containing-protein	unknown	unknown	gnl\|CDD\|377496
NZ_AP019735.1\|WP_019130440.1\|1751485_1752175_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_AP019735.1\|WP_019130441.1\|1750954_1751479_-\|6,7-dimethyl-8-ribityllumazine-synthase	unknown	unknown	gnl\|CDD\|376408
NZ_AP019735.1\|WP_019130428.1\|1764625_1765549_-\|cation-transporter	unknown	unknown	gnl\|CDD\|223131
NZ_AP019735.1\|WP_141412651.1\|1759483_1759864_+\|RidA-family-protein	unknown	unknown	gnl\|CDD\|129116
NZ_AP019735.1\|WP_141412647.1\|1750532_1750748_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141412649.1\|1756001_1758554_-\|adenosylcobalamin-dependent-ribonucleoside-diphosphate-reductase	gnl\|CDD\|274168	TIGR02504, ribonucleotide_reductase, ribonucleoside-diphosphate reductase, adenosylcobalamin-dependent. This model represents a group of adenosylcobalamin(B12)-dependent ribonucleotide reductases (Class II RNRs) related to the characterized species from Pyrococcus, Thermoplasma, Corynebacterium, and Deinococcus. RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. This model identifies genes in a wide range of deeply branching bacteria. All are structurally related to the class I (non-heme iron dependent) RNRs. In most species this gene is known as NrdJ, while in mycobacteria it is called NrdZ. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism].	0
NZ_AP019735.1\|WP_162851448.1\|1760131_1761793_+\|sulfatase-like-hydrolase/transferase	gnl\|CDD\|293763	cd16144, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	3.18026e-162
NZ_AP019735.1\|WP_141412653.1\|1763644_1764229_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|183566	PRK12513, PRK12513, RNA polymerase sigma factor; Provisional.	4.02576e-37
NZ_AP019735.1\|WP_141412654.1\|1765640_1767125_-\|proline--tRNA-ligase	gnl\|CDD\|236327	PRK08661, PRK08661, prolyl-tRNA synthetase; Provisional.	0
NZ_AP019735.1\|WP_141412658.1\|1771088_1771448_-\|DUF488-family-protein	gnl\|CDD\|225730	COG3189, COG3189, Uncharacterized conserved protein [Function unknown].	1.20995e-43
NZ_AP019735.1\|WP_141412660.1\|1773097_1773694_+\|flavin-reductase	gnl\|CDD\|224766	COG1853, COG1853, Conserved protein/domain typically associated with flavoprotein oxygenases, DIM6/NTAB family [General function prediction only].	7.64793e-39
NZ_AP019735.1\|WP_141412648.1\|1752353_1753442_+\|DNA-replication-and-repair-protein-RecF	gnl\|CDD\|234608	PRK00064, recF, recombination protein F; Reviewed.	5.97901e-98
NZ_AP019735.1\|WP_141412656.1\|1769157_1770279_-\|hypothetical-protein	gnl\|CDD\|224429	COG1512, COG1512, Beta-propeller domains of methanol dehydrogenase type [General function prediction only].	0.00185181
NZ_AP019735.1\|WP_162502283.1\|1758747_1759212_-\|META-domain-containing-protein	gnl\|CDD\|377111	pfam03724, META, META domain. Small domain family found in proteins of of unknown function. Some are secreted and implicated in motility in bacteria. Also occurs in Leishmania spp. as an essential gene. Over-expression in L.amazonensis increases virulence. A pair of cysteine residues show correlated conservation, suggesting that they form a disulphide bond.	8.48946e-28
NZ_AP019735.1\|WP_141413601.1\|1754313_1755153_-\|OmpA-family-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	1.54789e-25
NZ_AP019735.1\|WP_141412652.1\|1762791_1763181_+\|DUF4186-family-protein	gnl\|CDD\|372733	pfam13811, DUF4186, Domain of unknown function (DUF4186).	7.31346e-72
NZ_AP019735.1\|WP_141413600.1\|1753802_1754075_+\|DUF721-domain-containing-protein	gnl\|CDD\|377496	pfam05258, DUF721, Protein of unknown function (DUF721). This family contains several actinomycete proteins of unknown function.	9.11424e-13
NZ_AP019735.1\|WP_019130440.1\|1751485_1752175_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	1.34376e-07
NZ_AP019735.1\|WP_019130441.1\|1750954_1751479_-\|6,7-dimethyl-8-ribityllumazine-synthase	gnl\|CDD\|376408	pfam00885, DMRL_synthase, 6,7-dimethyl-8-ribityllumazine synthase. This family includes the beta chain of 6,7-dimethyl-8- ribityllumazine synthase EC:2.5.1.9, an enzyme involved in riboflavin biosynthesis. The family also includes a subfamily of distant archaebacterial proteins that may also have the same function. The family contains a number of different subsets including a family of proteins comprising archaeal lumazine and riboflavin synthases, type I lumazine synthases, and the eubacterial type II lumazine synthases. It has been established that lumazine synthase catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. The type I lumazine synthases area active in pentameric or icosahedral quaternary assemblies, whereas the type II are decameric. Brucella, a bacterial genus that causes brucellosis, and other Rhizobiales have an atypical riboflavin metabolic pathway. Brucella spp code for both a type-I and a type-II lumazine synthase, and it has been shown that at least one of these two has to be present in order for Brucella to be viable, showing that in the case of Brucella flavin metabolism is implicated in bacterial virulence.	7.93475e-68
NZ_AP019735.1\|WP_019130428.1\|1764625_1765549_-\|cation-transporter	gnl\|CDD\|223131	COG0053, MMT1, Predicted Co/Zn/Cd cation transporters [Inorganic ion transport and metabolism].	6.49838e-97
NZ_AP019735.1\|WP_141412651.1\|1759483_1759864_+\|RidA-family-protein	gnl\|CDD\|129116	TIGR00004, RutC_family_protein, reactive intermediate/imine deaminase. This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other].	1.38922e-56
NZ_AP019735.1\|WP_141412659.1\|1771539_1772892_-\|mechanosensitive-ion-channel	gnl\|CDD\|366370	pfam00924, MS_channel, Mechanosensitive ion channel. Two members of this protein family of M. jannaschii have been functionally characterized. Both proteins form mechanosensitive (MS) ion channels upon reconstitution into liposomes and functional examination by the patch-clamp technique. Therefore this family are likely to also be MS channel proteins.	1.04707e-21

>NZ_AP019735.1|WP_162851448.1|1760131_1761793_+|sulfatase-like-hydrolase/transferase
MKPVRKSLVGLSLLAPAAVLAKDDKPNIVFFLVDDMGWVDSSVAYGEEVYPNNLRFHTPNMDRLAREGVILTSAYACPVSTPTRTSLLTGMNAAHTGITNWTSTMRDTPSDATGGAVAMETGQIEENTGDRLIRPEWNINGMSPAPGVAHTQYATPLPQLLKDAGYFTIHVGKAHWASAGTPGASPYNMGFVVNVSGNVAGMPRSYQSEENYGNTPEKWNMLAVQNMTEYYGTGVHLTEALTREALKTLEYPIRHGEPFFLYMAHYATHTPIQPDKRFIQKYLDAGMDKGQARYASMVEGVDKSLGDLLDYLKEMGVEKNTVVVFMTDNGGNSENKQKGGVLHTQNKPLREGKGSCYEGGVRVPLMFRWPGRVAPNTRVNTPVIVEDLFPTLLEVAGVRNPRVVQAVDGESLVKLVTKGSEIAAKAAARGEIASQAEANRLVIPAEVSGLDPERVLVLHYPHKWKPYDLADIDYLSAVRKGDWKLVYRMQTGELELYDLSTDLGEQRNLAAEHPEKVKELAAELGSRLRGWKAPMPTVRRTGKPVAMPDELTN
>NZ_AP019735.1|WP_141412651.1|1759483_1759864_+|RidA-family-protein
MQKKVIASPLAPKAVGPYSQAIAAGTTLYVSGQLPIDAATGLMAEGIEAQTQRALENISAILAEAGYALSDVVKTTVLLQDIGDFAAMNGVYATYFTGALPARVCYEVARLPMGARVEIDAVAVKA
>NZ_AP019735.1|WP_162502283.1|1758747_1759212_-|META-domain-containing-protein
MQTRNRFRPLCLLLLLAAASACCPCRKYQKLYGAPLVGTRWLLIQLDGEEVANSDGRFSLRFEDAKRLSGRGGCNRYSASCDTEAGGHLRVGPIASTRMTCPEAQRERAFFAMLRSAVRYELDAKMLILSDSIGVRAVFQAAEEDQNTKNQKIN
>NZ_AP019735.1|WP_141412649.1|1756001_1758554_-|adenosylcobalamin-dependent-ribonucleoside-diphosphate-reductase
MSAKTTPKGLKEVTYNDAVARSKEYFGGDELAATVWVSKYALKDSFGHIYESSPEDMHHRIAAEIERIEKNYPNPLSRDEIFALLDHFRYVIPQGGPMTGIGNNLQIASLSNCFVIGHKKPADSYGGIIRMDEEQVQIMKRRGGVGHDLSHLRPTGSPVLNSALTSTGIVPFMERYSNSTREVAQDGRRGALMLTISIKHPDAERFIDAKVDTSKVTGANVSVKIDDEFMRAAIAGKPYHQQFPIDAEKPMYEQDIDARALWKKIIHNAWKSAEPGVLFWDTILRESIPDCYADEGFNTVSTNPCGEIPLCPYDSCRLLALNLYSYVDKPFTAEASFDFSKFRDHVGKAMRMMDDIIDLELEKVEQIIAKIDADPEEADIRYVESNLWKKVREMALKGRRTGLGITAEGDMIAALGMRYGSDKAVAFAVEVHKTLALAAYGASVEMAEERGAFPLYDAARELDNPMIARIREADPALYERMVKSGRRNIAMLTIAPTGTTSLMSQTTSGIEPVFRPVYKRRRKINPSDHNVKVAFVDDTGERFEEFYVFHHNFVEWARVNGHDTSTLATISDAELEKLVAASPYHKATANDIDWVAKVKMQGAIQKWVDHSISVTVNLPNEVSEELVADVYRTAWECGCKGVTVYRDGCREGVLLDKKQKKKGGDKGAADGSLKRPKSLPADIVRFKNGQEEWIAFVGLMDGRPYEIFTGKLEEDALYIPRKITKGNIIKVREADGKKRYDFQYTDRYGYTNTVGGISRLFDEEFWNYAKLISGVLRHGMPIDNVVSLIESLHLNSETINTWKNGVERALKQYIVDGTKSKEKCPSCGQETLVYQNGCLTCVSCGYSKCG
>NZ_AP019735.1|WP_141413601.1|1754313_1755153_-|OmpA-family-protein
MFVHTDLMINFSNWAGGYRADRAYYAVPFVGFGYMAMDFTDRAHDLGYGTNQELAFTAGLLNKFRIAKGWDLDIELKGMLFGEKDLPASLNSGGAYAVAYSATAGFTHRFNDRNWKRQMPQKYTDADIAAYTAAIAALEGSLAAARNNEKSLADQLAAANKALQDAKGKKEVFVNGACPAFFKINSAALSQRNKILLDLVADEINASPADKTFTVSGYADKETGSAAYNQKLSEERAQAVAEYLESKGVKADRLIVKGYGATVQPFSGNIENNRVVVIK
>NZ_AP019735.1|WP_141413600.1|1753802_1754075_+|DUF721-domain-containing-protein
MLMGDLLEEFFARPYVAAKVAEGRLPDTWREVVGDAVANLTTDLRLENRILYVRLQSSVVGQELFYQREALRDRINEVSKVRLVNAVIVK
>NZ_AP019735.1|WP_141412648.1|1752353_1753442_+|DNA-replication-and-repair-protein-RecF
MYLKRLSLINFKNIGQEEFPLTPGINCFVGDNGAGKTNFIDAIHYLSMCKSAFSMTDTQSVRHGEEFFLLEGSYERSDGRGEQIVCSFARRGGKTLKRNGKEYDRLSDHVGLVPVVIVSPADTALVSDAADERRRYLNGCISQLDRGYLSAVMRYNAVLSERNRYLKVGSDEDMLSIYDRQLAEHGQAIYEKRKAFAERLQPLVGEYYALLSGRREQVELTYRSELAEAPFTELLQRARQRDLANQFTTAGIHRDDLVLRIDGYPLRKYGSQGQQKSFLVALKLAQYRIVGADKGEKPILLLDDLFDKLDMGRVEQLIKLVSGEEFGQIVITDCNKVRLETILGRQGGNYRLYVVANGEIAK
>NZ_AP019735.1|WP_019130440.1|1751485_1752175_-|tetratricopeptide-repeat-protein
MAKIQNAANSTEESIGIAMSRTELFFEKNGKALTLGLIVLVLLGGLWVGYRNLVSKPRHEKAAELLAQAQNKFEADDADYTVALNGDDNGAGFLEVIERYGSTPAGNLAKHYAGICYLKEGDLKNAAAYLAKYTPVKGIPGSVVNAQNYGLQGDIAVDEGNYKEAVKFFEKAVEAADNNATAPIFLMKAGRAYKALGDTAKAKECFERIATAYPSSFEARDIEKYINSL
>NZ_AP019735.1|WP_019130441.1|1750954_1751479_-|6,7-dimethyl-8-ribityllumazine-synthase
MATKHRNLSQLNSPLPSAEEMKFGIVVAEWNPEVTEGLLSGAVHTLRSAGCPEHNIQIKYVPGTFELSLGAQFFAEYTDVDAVIVLGCVIQGDTRHFDFVCQGVTQGVMQLQLQWNMPIAFGVLTTNDLQQALDRSGGRLGNKGDEAAAAAIQMVHLQDEMDTEENALDRKAIN
>NZ_AP019735.1|WP_141412647.1|1750532_1750748_+|hypothetical-protein
MKKIYAFIVVVAAAAMVSCAGNANKQAAAEAGTVEVAVEEVSESCGECADSVKADSCCKAEAAVEVVEAAK
>NZ_AP019735.1|WP_141412652.1|1762791_1763181_+|DUF4186-family-protein
MDQNRKEYLMQASPFEALFARLAQSDFRSRFRLGSEEVACIERRGMAVIRRHAEDFVRRRLAPAFIPNDGRQTPMRGHPVFIAQHATACCCRGCLAKWHAIPAGRELTAREQRYVVEVLMAWIERQSAR
>NZ_AP019735.1|WP_141412653.1|1763644_1764229_-|sigma-70-family-RNA-polymerase-sigma-factor
MNVQVVSDQKLLNCYLSGDRNAISQLIERHSRRVRDYIQMMVKDGDVADDIFQETFIKAVRVIDEGRYTDNGRFLSWILRIAHNQVIDHFRAQKQNRQLNEAEAGYDVLGTLRLAERTVEDEIVCEQIASDVRRMVELLPDEQREVVMMRYYSGLSFKEIAEQTGVSINTALGRMRYALINLRKMIKEKNLILS
>NZ_AP019735.1|WP_019130428.1|1764625_1765549_-|cation-transporter
MTERTLGREQAIYRVTWIGFAVNLVLSAGKLAAGIWGHSAAMVADAIHSVSDFATDLVVLLFVRVSAKPRDDDHDYGHGKYETLATLIIGVALAGVGIKLLWSGGTAIRDFTRGLLPTQPGVVALWAAVVSIVAKEALYRYTARVGRRVNSPSVVANAWHHRSDALSSVGTLVGIGCAYFLGGGWRLADPAAAIVVALLILRVAWQLMKMGMDELLEKSLPREQEEHILSLIAADPAVASPHNLRTRRIGQNIAVEVHIRVDGAMTVTESHRLTVDIERRLRDAYGEGTIVSIHVEPRKQPPLNESK
>NZ_AP019735.1|WP_141412654.1|1765640_1767125_-|proline--tRNA-ligase
MAKELKDLTKSEENYSQWYNDLVVKAGLAENSAVRGCMVIKPYGYAIWEKMQAILDRMFKQTGHENAYFPLFIPKSFFSKEAHHVEGFAKECAVVTHYRLKNDPEGKGVVVDPDARLEEELIVRPTSETIIWNTYKNWIHSYRDLPILCNQWANVVRWEMRTRLFLRTAEFLWQEGHTAHETREEAIAEATKMINVYKEFAERYMALPVIVGHKSPNERFAGAEDTLTIEALMQDGKALQSGTSHFLGQNFAKAFDVQFTNKEGKLEYVWATSWGVSTRLMGALIMAHSDNNGLVLPPALAPIQAVLVPIYKGEEQMKTIVAKLDAIAAELRARGLSVKVDARDNVRSGFKFAEYELKGVPVRLALGPRDLENGTIELMRRDTLEKEVVPQEGLIDRVAALMDEIQQGIFDKARSFRDSMITPVDTWEEFVRTLDTKGGFVAAHWDGTVETEVAIKEATKATIRCIPLDAVDEEGACIYSGKPSHQRVLFARSY
>NZ_AP019735.1|WP_141412655.1|1767432_1769127_-|transporter
MRKLQIAIWAAALVATGSLQAQQRGTLAFGGAVLNQDGVLAGEMAQMSQPQALGTARSMALGGAFTSLGADLASMSINPAGLGMYRRNEIALTPMMTFQSSETPGTMSYAKNGKNRFSMANFGAALNAYEGTGTLTSFTVGIGLNRIADFNSRYSYKTDTPYAGGSVWAPTIADIFGQQLGQAGIFPNGNDELGYNVNPYYWPAVLGYNGFMISRHFYTDPETQEEKPTYVPDCIGSNASILHYMDVVNSGSINEFTISAGANLNNIVYIGATIGIQSVHKATGVYYGEDYRYDHGQAINSAGEELETQLDYADLYQKSVLDGSGVNFKLGVTVRPIESLRIGVAFHTPTYYSLERSYYGDITTQMYNNATEKTEINQDGTPYQDDMGSNSWCFTSPARLLFGISYTFGNFGLITVDYERDWYNGIRVKNTPDGFEPYPEEYKAEFKQAFQGTNTIRAGVEFKPLPTIALRVGAGYTDSMFKNREHYYDSPLTYETRYITAGVGFNLSRYVTLDLAYQNVTDKQTKYRLFYSIENATGDFFTTTGLFDTKSKRHNVAMSLIFRF
>NZ_AP019735.1|WP_141412656.1|1769157_1770279_-|hypothetical-protein
MKTMKTGIGLLLLALLTTGCSSAYYQSEGYAGDDLYGIHNKTKIAQREKAKAEAEKAEAEARRAKWEALMAQAQADDAENRYYGSNDFDDLVVDDYESAYERRLRGFESPTYKMPSSYWNLRYSGTFNYLTAYDPAFYNIIVMGDEVWVEPKYITSMFGTWGLATGFAAGYMAGIYGSWYSSWGYGWPYYGWGYGPYWGWGGWYNPWWNHSYWYGGYYPYWGHPHWGHPHYYRPRPNYRLNNNGSIPRNYRSYGTPSRNGSYRNYGTSGSGSRGGSYNSNRNNSGGVYYNSGGRSNNSSNVYRGNGNTYNNNSYNERENSYRSNSTYRNNSGSSFNSGSRGGSRSGSYNSGGGSRGGSGGGTSSGGSRGFRGR
>NZ_AP019735.1|WP_141412657.1|1770879_1771092_-|hypothetical-protein
MTYPLQENADGVFANRILRPEPEMQAIFTEIGLRTCGRGAFPLPAGLPCRRRQAKSRRQRRTFYLTRNSE
>NZ_AP019735.1|WP_141412658.1|1771088_1771448_-|DUF488-family-protein
MTRIAIKRVYEPATDTDGLRVLVDKLWPRGIRKEALHYDLWAKEIAPSAPLRRWFHADPQGRWEEFRRRYLHELAASPAVRAFVAKIEKEPCATLLYASKNAEENHARVLREYLERESG
>NZ_AP019735.1|WP_141412659.1|1771539_1772892_-|mechanosensitive-ion-channel
MNTNEFARTLLLGIKNLLSWIGIPRHLLDKLDEILFLVCIVTIAFVVAAVVHLLLVRAARKILKRKHLDFFDSLFRYSVFRKSTALIPPLIVSALLPFAFATDSAWFTVSERVTWIYFFIVLMISVNAILNTVGDTLKNDGQLKNRPIKGFIQIFQVIFSCVVVIVVVSILIDKSPVNLITGLGAFTAVLMLVFKDPILGLVAGVMISENDMLRIGDWIEMPQNGINGTVTDISLTVIKVQNFDNTIVTVPPYSLVSGSFVNWRGMSDSGGRRIMREYTLKLDCIKPCTPEFLERMKAFDEELAQFIAEKQRQAAEGKVANTENPDGLVNGTIETNLGLLRAYMALYLRRHPFVSRDLLLMVRTLPATENGLPVQIYCFSSDKNWPSYESIQAEIMEHFVAVLPAFELYAFQRTGARDVLLNGIAASGKADLATMETAPLHTDPSEKQGT
>NZ_AP019735.1|WP_141412660.1|1773097_1773694_+|flavin-reductase
MKESWKPGTMIYPLPAVLVGCGDAPDNWNLLTVAWTGTVCTAPPMCYVSVRPERHSHALIARTGEFTINLTTAAMARAVDWCGVRSGRDYDKFRETGLTPLRGAVVAAPALEESPVVVECRVRQILPLGSHDMFLAEVVNVLVDDRYIDSATGRFDLERAGLVAYSHGEYFRLGELIGHFGWSVRRRKIIVRERKGRR

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Crispr_ID: NZ_AP019735_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_12

2382915-2383011

Orphan

Consensus_repeat	Method
TCGGCAATGCTCAAATAAATTTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_12

>merge|NZ_AP019735|12|2382915-2383011|CRISPRCasFinder
TCGGCAATGCTCAAATAAATTTGCATTGCACTCGGCTTAATCGTATCTTTGGCTTGCGCCTTAGATACTCCCGCTCGGCAATGTTCAAATAAATTTG

>NZ_AP019735|12|12|2382915-2383011|CRISPRCasFinder
TCGGCAATGCTCAAATAAATTTG	CATTGCACTCGGCTTAATCGTATCTTTGGCTTGCGCCTTAGATACTCCCGC
TCGGCAATGTTCAAATAAATTTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141413006.1\|2374398_2375994_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413010.1\|2386375_2387074_+\|methyltransferase	unknown	unknown	gnl\|CDD\|226608
NZ_AP019735.1\|WP_026074813.1\|2372133_2372715_+\|OmpH-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|214922
NZ_AP019735.1\|WP_141413626.1\|2383531_2384125_+\|dephospho-CoA-kinase	unknown	unknown	gnl\|CDD\|234620
NZ_AP019735.1\|WP_141413007.1\|2377242_2379183_+\|molecular-chaperone-DnaK	unknown	unknown	gnl\|CDD\|234715
NZ_AP019735.1\|WP_141413011.1\|2387123_2388023_+\|DUF4831-family-protein	unknown	unknown	gnl\|CDD\|374372
NZ_AP019735.1\|WP_141413008.1\|2379735_2382750_+\|protein-translocase-subunit-SecDF	unknown	unknown	gnl\|CDD\|237276
NZ_AP019735.1\|WP_026074811.1\|2376513_2376756_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413627.1\|2384150_2384930_+\|dihydropteroate-synthase	unknown	unknown	gnl\|CDD\|273657
NZ_AP019735.1\|WP_141413004.1\|2369805_2370621_-\|DUF2490-domain-containing-protein	unknown	unknown	gnl\|CDD\|378471
NZ_AP019735.1\|WP_141413005.1\|2371424_2372015_-\|Holliday-junction-branch-migration-protein-RuvA	unknown	unknown	gnl\|CDD\|234645
NZ_AP019735.1\|WP_141413629.1\|2389793_2390837_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_AP019735.1\|WP_141413628.1\|2384944_2385598_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213222
NZ_AP019735.1\|WP_019129997.1\|2371228_2371369_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413013.1\|2388751_2389612_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378964
NZ_AP019735.1\|WP_019129988.1\|2383139_2383532_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413012.1\|2388019_2388667_+\|DNA-alkylation-repair-enzyme	unknown	unknown	gnl\|CDD\|132880
NZ_AP019735.1\|WP_034779517.1\|2373726_2374383_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019129994.1\|2372827_2373598_+\|TIGR00159-family-protein	unknown	unknown	gnl\|CDD\|224539
NZ_AP019735.1\|WP_141413009.1\|2385600_2386371_+\|TIGR02757-family-protein	unknown	unknown	gnl\|CDD\|378237

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141413629.1\|2389793_2390837_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	5.9457e-60
NZ_AP019735.1\|WP_026074813.1\|2372133_2372715_+\|OmpH-family-outer-membrane-protein	gnl\|CDD\|214922	smart00935, OmpH, Outer membrane protein (OmpH-like). This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.	9.56842e-13
NZ_AP019735.1\|WP_141413626.1\|2383531_2384125_+\|dephospho-CoA-kinase	gnl\|CDD\|234620	PRK00081, coaE, dephospho-CoA kinase; Reviewed.	9.30657e-65
NZ_AP019735.1\|WP_141413007.1\|2377242_2379183_+\|molecular-chaperone-DnaK	gnl\|CDD\|234715	PRK00290, dnaK, molecular chaperone DnaK; Provisional.	0
NZ_AP019735.1\|WP_141413013.1\|2388751_2389612_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378964	pfam12833, HTH_18, Helix-turn-helix domain.	1.15593e-17
NZ_AP019735.1\|WP_141413008.1\|2379735_2382750_+\|protein-translocase-subunit-SecDF	gnl\|CDD\|237276	PRK13024, PRK13024, bifunctional preprotein translocase subunit SecD/SecF; Reviewed.	0
NZ_AP019735.1\|WP_141413011.1\|2387123_2388023_+\|DUF4831-family-protein	gnl\|CDD\|374372	pfam16115, DUF4831, Domain of unknown function (DUF4831). This family consists of several uncharacterized proteins around 350 residues in length and is mainly found in various Bacteroides species. The function of this family is unknown.	2.72455e-30
NZ_AP019735.1\|WP_141413627.1\|2384150_2384930_+\|dihydropteroate-synthase	gnl\|CDD\|273657	TIGR01496, Dihydropteroate_synthase, dihydropteroate synthase. This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid].	5.77316e-103
NZ_AP019735.1\|WP_141413004.1\|2369805_2370621_-\|DUF2490-domain-containing-protein	gnl\|CDD\|378471	pfam10677, DUF2490, Protein of unknown function (DUF2490). This is a bacterial family of uncharacterized proteins. They appear to belong to the outer membrane beta barrel superfamily.	2.14833e-19
NZ_AP019735.1\|WP_141413005.1\|2371424_2372015_-\|Holliday-junction-branch-migration-protein-RuvA	gnl\|CDD\|234645	PRK00116, ruvA, Holliday junction branch migration protein RuvA.	3.14687e-71
NZ_AP019735.1\|WP_141413628.1\|2384944_2385598_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213222	cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.	1.89722e-107
NZ_AP019735.1\|WP_141413010.1\|2386375_2387074_+\|methyltransferase	gnl\|CDD\|226608	COG4123, COG4123, Predicted O-methyltransferase [General function prediction only].	5.89634e-57
NZ_AP019735.1\|WP_141413012.1\|2388019_2388667_+\|DNA-alkylation-repair-enzyme	gnl\|CDD\|132880	cd06561, AlkD_like, A new structural DNA glycosylase. This domain represents a new and uncharacterized structural superfamily of DNA glycosylases that form an alpha-alpha superhelix fold that are not belong to the identified five structural DNA glycosylase superfamilies (UDG, AAG/MNPG, MutM/Fpg and helix-hairpin-helix). DNA glycosylases removing alkylated base residues have been identified in all organisms investigated and may be universally present in nature. DNA glycosylases catalyze the first step in Base Excision Repair (BER) pathway by cleaving damaged DNA bases within double strand DNA to produce an abasic site. The resulting abasic site is further processed by AP endonuclease, phosphodiesterase, DNA polymerases, and DNA ligase functions to restore the DNA to an undamaged state. All glycosylase examined to date utilize a similar strategy for binding DNA and base flipping despite their structural diversity.	9.41034e-05
NZ_AP019735.1\|WP_019129994.1\|2372827_2373598_+\|TIGR00159-family-protein	gnl\|CDD\|224539	COG1624, COG1624, Uncharacterized conserved protein [Function unknown].	4.28779e-69
NZ_AP019735.1\|WP_141413009.1\|2385600_2386371_+\|TIGR02757-family-protein	gnl\|CDD\|378237	pfam09674, DUF2400, Protein of unknown function (DUF2400). Members of this uncharacterized protein family are found sporadically, so far only among spirochetes, epsilon and delta proteobacteria, and Bacteroides. The function is unknown and its gene neighborhoods show little conservation.	1.22876e-111

>NZ_AP019735.1|WP_141413008.1|2379735_2382750_+|protein-translocase-subunit-SecDF
MQSKGAIKLLAILLAIACIYQLSFSFKTRSVEKKAAAYAAAYDGDERSEREQYYLDSVQNQPVYNLGFRKFTYKEIKEKELNLGLDLKGGMNVMLEIQVEDVVKSLAGDSKNDPAFIEAMAQAKEGLRTGKDFIGEFVRSYRTATNGAPLAAIFVSPDRKDITPNSTDAEVEKILRKETDDAIDASFNILRSRIDHFGVTQPNIQRLPNSNRILVELPGVKEPERVRKLLQGSASLEFWTTYNAGEIVPTLMRADQVVKQYLADTKPAVEETVAVAEAADSTADGGLIAEVATAETETAAEATGSYYDRDQNPLLALLNPQFAGGAAVGAVMAADTAAVNDYLALPAVKEMLPADLRFKWAIKGETQQPVDGRFYLYAIKVERPDGRAPLDGSVITDAREAYAQRGAEAEVSMSMNSNGISEWARLTADNVGRCVAIVLDGYVYSAPVVRQKIEGGNSSISGNFTIQEAKDLANVLKSGKVPAPAHIIQDTVVGPSLGQESINAGMVSFVIAFLLVLLYMGAFYKTAGWMADLALLFNVFLLMGVLVSFGAVLTLPGIAGIVLTMGMAVDSNVIIYERIKEELRAGKGLSLAIKDGFSNAYSAIIDGQLTTIITGIVLFVFGNGPVQGFATTLIIGILTSLFSSIFITRLLIEAIVAKFGHISFSRKWSENWLNNIHFDFVGKRKYSYAISGTVIVLSFISFAVFGLNRGVEFTGGRSYVVLFDQPVSVEQVRASVEDQFAQIENADNANVSLEIKQYGGDGDQVRIVTQYKYDDASDEATDEINRLLYDAVKKYYKTAVTFADFRNTQLSPYGIVSADKIGPSIAKDMTYNAIYAVFFSLIAIGLYITLRFKKWQWATGATLSLAHDALIVIGLFSMLYAVMPFNLEINQAFIAAILTVIGYSINNTVVIFDRIREYIALYPKRSLRDNINNATNSTMARTFNSSGTTLVTLLAIFLFGGETIRGFIFALLCGVAIGTYSSWFIATPLSFDLMPESIKNKGKE
>NZ_AP019735.1|WP_141413007.1|2377242_2379183_+|molecular-chaperone-DnaK
MGKIIGIDLGTTNSCVAVMEGNEPVVIPNSEGHRTTPSVVAFTEGGERKVGDPAKRQAITNPMRTIFSIKRFMGETYDQVRSEIERAPYKVVKGPNDTPRVEIDGRQYSPQEISAIILQKMKKTAEDYLGQTVDEAVITVPAYFSDSQRQATKEAGEIAGLKVRRIINEPTAAALAYGLDKKSADMKIAVYDLGGGTFDISILELGDGVFEVKSTNGDTHLGGDDFDHVLIDYMAEAFKAEHGVDLRQDPMAMQRLKEAAEKAKIELSSSTSTEINLPYIMPVNGIPQHLVMTLTRAKFEQLCDHLIHKTIEPCKQALRDAGLEAGQIDEVILVGGSTRIPAIQQIVKEFFGKEPNKSVNPDEVVAIGAAIQGGVLTGEVKDVLLLDVTPLSLGIETLGGVMTKLIEANTTIPTRKSEVFSTAADNQPSVEINVCQGERPLARDNKSIGRFHLDGIPAAPRGVPQIEVTFDIDANGILNVSAKDKGTGKEQKIRIEASSGLTEEEIQRMRDEAKANEAKDKEEKERIDKINAADSNIFATEKQLKEYGDKLPADKKSAIEAALGKLKEAHKNADVMAIDTAITELNAAWQAASQDIYAQQQAQGGANANANANAGAGASGAEAGAGAGSAAGDSSQPEDVEFEEVK
>NZ_AP019735.1|WP_026074811.1|2376513_2376756_-|hypothetical-protein
MVITFNELRRIKDKLPSGSSQRIADELGIDVDTVRNYFGGKHYDAKGNVGIHVEQGPDGGVVTLDDTTILDAAMRILNQQ
>NZ_AP019735.1|WP_141413006.1|2374398_2375994_+|hypothetical-protein
MRFSFGKIWAAAVCLLVFASCAKDTSESYAGIEQRSLDAWMKLHRPELLGNRQEARGFSYYVDVLDAGSTDKADTLIAETDCWVQYEFTARDLNGNVCMTRNAVQAKQQGTFTRYTYYSPYFRYSGSDYTTLLEGSYYALREPLTLSEEYIAEHPDRGLKNGMQARRGTELMLYLPSSLAYSSSGASSDAGYGGQYELDANRPAILHIKVTGRVSNPLAYEGETVDAFVEDNGTVCPVEEEEDKDDPKLASVRRSLRDAETDEPELPDTSVDPYKYTWYQAVDTVPQLYISHVFSPGREPATTYNWKNTYSVPYFPYNESMAALDKKINDVLVERFGAGTYKGDSIKSGETASIWYIGRFLDGFIFDTNIDEVKRLIYGEVQSEGSAYQYEVPEEGDTSTLETIYAWYYSIPQLRYGQWATIVTTSSFGYGASGKSGGSSTSGGSSSSSYLDYYNYYNYYNYYNNYYGGLYGNSYYDSYYNNYYGGLYNSYYYNNYYYDDYSSSGSTTTTYTTEIPAYSPLLFEIYIEPKE
>NZ_AP019735.1|WP_034779517.1|2373726_2374383_+|hypothetical-protein
MRVRWYMGALALAALVSCSDEEDILPQQQEKIVSYLTRSHTPTLLSEQDAAQSLDNDPPYYSTFGNTTYRYIADVYDEERLTRPEVSEGSRVELTFSLYDFTAYSTPKPNECLYSNDTTIINRLVEGGLNPRYWVECDLYGVPLRDEFGQFVPLRQTLQIGGGATLSGLQAALVGCREKDVVELYMTYNQAYGEKLIMGLMTKQCPVAFFCTINKVTK
>NZ_AP019735.1|WP_019129994.1|2372827_2373598_+|TIGR00159-family-protein
MGFVPFTFIDLIDILFVAYIMYWIYRTTKGTNAPYIISGIIVVYLLWVIVKTLNMELLSTILGHIISVGAIALIVVFQPEIRRFLQKIGMSQKRFNFISRIFNHGSKIAETNLQPLVVACREMSDTKTGALVVIGQQSDLSLITEGGICLDAKISSQLIHNIFFKNSPLHDGAVVIEGDRIVAARCILPVTQSDVPKSFGTRHRAAIGMSEISDAIILVVSEETGAISIANNGRINLNIPSDRLGAVLQKYLISKK
>NZ_AP019735.1|WP_026074813.1|2372133_2372715_+|OmpH-family-outer-membrane-protein
MKKILYVAAAAMFLIAGCKGNGATQPAENAPAQAVGSSDIAFVQVEAVLAQSDLFQSEGAALQEKTKKAQEGWAKKERDLQSKAAQLQEKYQKGLITTANAQSEQEKIQRQIANYQSVAQKEAQTLDEENYVFTNRAQDLIHRAVQELNADKKYKLILNATSLVDADSLLDITPLVLAKVNELYAADKKADKE
>NZ_AP019735.1|WP_141413005.1|2371424_2372015_-|Holliday-junction-branch-migration-protein-RuvA
MYEYIQGKLAELAPAYAVVETGGVGYLLHISLQTYSEIEGRSEVKLFTHFVVREDAQLFFGFSTKTERELFRQLISVSGVGGNTARMILSTYSPRELQSIITTENAVLLKNVKGLGLKTAQKIIVELSGKLTALFDGEDGPLPVAGNGDAVYDEATAALVMLGFPKAASDKVVRAILKEQPDISVEETVRMSLKRL
>NZ_AP019735.1|WP_019129997.1|2371228_2371369_-|hypothetical-protein
MATFLFIMIVLALLALVVTLVVFTLSQRKKARLQNPHDSYHGRYRA
>NZ_AP019735.1|WP_141413004.1|2369805_2370621_-|DUF2490-domain-containing-protein
MNLLRLFRQSLFSSGAACKRTLARNTRRLLPLAAALLFAATAQAQERRTTHDNDFRARFSFALTKQLGQRHSITLDEELRLKDNWSQLDRIYTTLSYAYDVRPWFKAAAFYVLIANDRGADRSMEMRHRFYLELTASYKTGAWNFSLRERPQATLHTAYVDPAVAAKTAWVLRHRLMAEYAVAGTGLKPYVFVELTQTLNAPETVGNYLEKVRSSLGAKYAFNKRSSLELYYRFDYKISDEPVFDDFPTVDYISSERESHHIIGLEYGYKF
>NZ_AP019735.1|WP_019129988.1|2383139_2383532_+|hypothetical-protein
MFDNLRQWLRKYISPVFVAMLVASFVLWYIAKLNYTYTTDKTVQVNVDGEEFEVVCVIEGLGTNLFSRMVYMRNSLRIPLSELDYAPSPDEEGYIVIDPQSLQNAISVHYSDVKVVAVRNIPPIKLPVEE
>NZ_AP019735.1|WP_141413626.1|2383531_2384125_+|dephospho-CoA-kinase
MRVGVTGGIGSGKSTVCRLFAERGVPVYDSDSEAKRLMGEDPSLRAALVEAFGDETFRDGVLNRRYLAATVFGDRHALARLEALVHPCVKRDFERWAAERTAEPYVVLECAILYESGMDAAVDRVVAVVAPEELRLVRVNARDGASAAEIRCRMAAQLSDDVLSARADYTIVNINREDLAADVAECDRRFRYEAAGN
>NZ_AP019735.1|WP_141413627.1|2384150_2384930_+|dihydropteroate-synthase
MTIVNVTPDSFFAGSRTPDWLDVERRVREAVEAGASVIDVGGYSSRPGADEVSPEEEWRRVDLGVGAVRSLSSDLPVSIDTFRSSVAARAIHKYGKVIINDISAGELDPLIVDVAAEHDVPYVAMHMKGDPRTMQSMTDYRDIVAEVVDYFRERTAQLRERGVRRIVVDPGFGFAKTLEQNYELLRGLHRLAELGYPVLAGVSRKSMIYKLLGTTPAEALNGTTALHWECLRQGAVILRAHDTREAVEVVRMFDQFMQA
>NZ_AP019735.1|WP_141413628.1|2384944_2385598_+|ATP-binding-cassette-domain-containing-protein
MIRAEGLRKRYGALEVLRGVSLEVARGEVVSIVGASGAGKTTLLQIIGSLTRPDGGRVTLGGVDPFALSDRELSRFRNRRVGFVFQFHHLLPEFTAFENVCLPGLIGGRDRREVGARAAELLDLMGLAARRDHKPAALSGGEQQRAAIARALINSPSVLLADEPSGNLDTHNREEIHRLFFELRERLGQTVVIVTHDESLAARADRTITMSDGRIVG
>NZ_AP019735.1|WP_141413009.1|2385600_2386371_+|TIGR02757-family-protein
MEREELHDLLERLWDRYDREEFISADPIAVPHCFASRDDREIAGFLAATIAWGSRPMIVRNGLRMMHFLDDAPHDFVRNASERELAKLSGFVHRTFNGGDLIQFVRSIRAICERHGGLGRFVEASYASTGDMRRVLAAFREEFFRTEHPERCRKHVSSIERGASCKRLCMYFRWMVRHDDRGVDFGLWRTIPPSALYLPLDLHTGNMGRALGLLARRQNDWRAVEEITAALRTFDADDPVRYDFALFGAGIDGFLK
>NZ_AP019735.1|WP_141413010.1|2386375_2387074_+|methyltransferase
MFRFKRFTIEQDACPMKVGTDGVLLGAWVALGAADRLLLDVGTGTGVIALMLAQRSPAAGVTALDIDAACAEQARANADRSPWGGRVTTCCAPVQEYRPEEPFDLVVSNPPYYDRSLLPPDAGRTTARHTVALTHGELIAAACRLLAPEGRLAVILPAVEAQRFREQARGRLALRRLTEVWSTPRSGVKRCLMEFVRGDAAELRTDRLVIEEAPGRFTEEYRRLTGDFYLKF
>NZ_AP019735.1|WP_141413011.1|2387123_2388023_+|DUF4831-family-protein
MKTLVSLLCCTALTVGSASAQSYRVARAGAFEENGRVEVGIPTSPLAVDLTVEKEVVTVGPYARYAQKFLGVRGALSDKTLYSVKAARVALLDRDATTASEVPAGEVRATSYLGDTETFSRVPFDKRSLVDESLETAARNAANTLFAIRRHRMELITSEAGEHVFGAGLQAALAELDRQEQAYTELFLGKRVTTTSVERITVVPDAGKQKYILCRFSPDRGLLPGNDLTGDVVLLQLDKESDGSFTLTPASPKAARTATYRVAADVVCTVYCGTEELTRATLPLFEFGRDVELALPSKK
>NZ_AP019735.1|WP_141413012.1|2388019_2388667_+|DNA-alkylation-repair-enzyme
MTNHTARMAALLGELRREMNGAVAESMQRGEGGYGLNYGVSIPTIRAIAGRVGTDHAFARFLYRQDVRELRMAAPTIADPASVTPDNVDEWFVGRMPEELIEELALRLLSRCGRPVLDTLCGRWLRAGSGAERYAALMALARARVQEFDAAAVVEAVPDAVAACPDDLRLARGAAAFVQSASARIAPERLARMIERLPDSRGGAYLRDELAWMIL
>NZ_AP019735.1|WP_141413013.1|2388751_2389612_-|helix-turn-helix-domain-containing-protein
MDTPVTPSIGLFHADKQTVEALGPVVQLAKSGFFYCTQGEMSLVLGNRAFEIHRGDIYIYPPLSKTYIRMLSDDLHGTVGVADFDFVFTLANSISNTQNHLYMRENPCISLNDEQRRRIEELIELIRRRERSQGSRSTNENNRLIYNQLLSSLGKALCCEIAEAYFFNHPIQPLKQDRKDRIFQSFIFSLSQNFRTHHSVSFYAAEQCLTPRYFSTIVREKSGRNALQWIMMFIIAEAKKLLSDPDPSIKEIAETLGFSNQSFFGRYFKQYVGLSPMAFRSSGTKE
>NZ_AP019735.1|WP_141413629.1|2389793_2390837_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MGMVCLLACCCGCSGRPEGAVRLPIVRIDTVGVYGTPRTVQFPGCVRAAQEVNAAFKVGGTLRTIFAEEGEFVRRGAPLAALDARDYRLQAEAAEAEYKRVKAEAERVMALYADGAATPDAYDKARYGLQQITAKYENSRNQLADTEIRMPFDGYVQKRLFDPSTVVGAGMPVLTVVSAEAPEIEINIPGSEYVRRSEFDGFEAAFDFWPGKRIPLRLRSISPKANANQLYTLRLGVPADLRPLPSPGMNTMVTIVCRPSGAAQVAVPAVALFDDGDRTCVWICREDSTVVSREVRVERLQTGGEAVVGAGLAAGERIVTSGVHRLREGEKVAPLPGVTKTNVGGLL

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Crispr_ID: NZ_AP019735_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_13

2400456-2400556

Orphan

Consensus_repeat	Method
GCCAAAGATACGAAAAAGTCGGGCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_13

>merge|NZ_AP019735|13|2400456-2400556|CRISPRCasFinder
GCCAAAGATACGAAAAAGTCGGGCGCAGAAGCAAGCGTCAGCTTGATTCTACCGAGACGGAGTATCTAAGGCGCAGCCAAAGATACGAAAAAGTCGGGCGC

>NZ_AP019735|13|13|2400456-2400556|CRISPRCasFinder
GCCAAAGATACGAAAAAGTCGGGCGC	AGAAGCAAGCGTCAGCTTGATTCTACCGAGACGGAGTATCTAAGGCGCA
GCCAAAGATACGAAAAAGTCGGGCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141413017.1\|2398156_2399308_-\|1-deoxy-D-xylulose-5-phosphate-reductoisomerase	unknown	unknown	gnl\|CDD\|235472
NZ_AP019735.1\|WP_019129969.1\|2403906_2404695_-\|polysaccharide-biosynthesis/export-family-protein	unknown	unknown	gnl\|CDD\|224512
NZ_AP019735.1\|WP_141413629.1\|2389793_2390837_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_AP019735.1\|WP_019129974.1\|2396823_2398146_-\|RIP-metalloprotease-RseP	unknown	unknown	gnl\|CDD\|272878
NZ_AP019735.1\|WP_162502323.1\|2390836_2393959_+\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911
NZ_AP019735.1\|WP_141413016.1\|2395357_2396731_-\|DNA-repair-protein-RadA	unknown	unknown	gnl\|CDD\|236994
NZ_AP019735.1\|WP_141413013.1\|2388751_2389612_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378964
NZ_AP019735.1\|WP_141413024.1\|2415239_2417615_-\|outer-membrane-beta-barrel-protein	unknown	unknown	gnl\|CDD\|379720
NZ_AP019735.1\|WP_162502324.1\|2406592_2407483_+\|WG-repeat-containing-protein	unknown	unknown	gnl\|CDD\|379719
NZ_AP019735.1\|WP_141413021.1\|2407606_2408515_+\|TPM-domain-containing-protein	unknown	unknown	gnl\|CDD\|377378
NZ_AP019735.1\|WP_019129971.1\|2400991_2401381_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413015.1\|2393955_2395296_+\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_AP019735.1\|WP_141413011.1\|2387123_2388023_+\|DUF4831-family-protein	unknown	unknown	gnl\|CDD\|374372
NZ_AP019735.1\|WP_162852315.1\|2409283_2411263_+\|glycoside-hydrolase-family-97-catalytic-domain-containing-protein	unknown	unknown	gnl\|CDD\|371140
NZ_AP019735.1\|WP_141413023.1\|2411390_2415053_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|318484
NZ_AP019735.1\|WP_141413018.1\|2401388_2403890_-\|polysaccharide-biosynthesis-tyrosine-autokinase	unknown	unknown	gnl\|CDD\|349772
NZ_AP019735.1\|WP_141413019.1\|2404845_2406141_+\|alpha-amylase-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|200452
NZ_AP019735.1\|WP_019129972.1\|2399337_2400201_-\|M23-family-metallopeptidase	unknown	unknown	gnl\|CDD\|366703
NZ_AP019735.1\|WP_141413022.1\|2408673_2409255_+\|LemA-family-protein	unknown	unknown	gnl\|CDD\|377192
NZ_AP019735.1\|WP_141413012.1\|2388019_2388667_+\|DNA-alkylation-repair-enzyme	unknown	unknown	gnl\|CDD\|132880

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141413017.1\|2398156_2399308_-\|1-deoxy-D-xylulose-5-phosphate-reductoisomerase	gnl\|CDD\|235472	PRK05447, PRK05447, 1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional.	0
NZ_AP019735.1\|WP_019129969.1\|2403906_2404695_-\|polysaccharide-biosynthesis/export-family-protein	gnl\|CDD\|224512	COG1596, Wza, Periplasmic protein involved in polysaccharide export, contains SLBB domain of b-grasp fold [Cell wall/membrane/envelope biogenesis].	1.14587e-16
NZ_AP019735.1\|WP_141413629.1\|2389793_2390837_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	5.9457e-60
NZ_AP019735.1\|WP_019129974.1\|2396823_2398146_-\|RIP-metalloprotease-RseP	gnl\|CDD\|272878	TIGR00054, Putative_zinc_metalloprotease_slr1821, RIP metalloprotease RseP. Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain. [Protein fate, Degradation of proteins, peptides, and glycopeptides].	6.34716e-56
NZ_AP019735.1\|WP_162502323.1\|2390836_2393959_+\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_AP019735.1\|WP_141413016.1\|2395357_2396731_-\|DNA-repair-protein-RadA	gnl\|CDD\|236994	PRK11823, PRK11823, DNA repair protein RadA; Provisional.	0
NZ_AP019735.1\|WP_141413013.1\|2388751_2389612_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378964	pfam12833, HTH_18, Helix-turn-helix domain.	1.15593e-17
NZ_AP019735.1\|WP_162502324.1\|2406592_2407483_+\|WG-repeat-containing-protein	gnl\|CDD\|379719	pfam14903, WG_beta_rep, WG containing repeat. This repeat contains an N-terminal WG repeat motif. The extent of the repeat is poorly defined. This repeat may form a beta solenoid structure (Bateman A pers. obs.).	2.06483e-11
NZ_AP019735.1\|WP_141413021.1\|2407606_2408515_+\|TPM-domain-containing-protein	gnl\|CDD\|377378	pfam04536, TPM_phosphatase, TPM domain. This family was first named TPM domain after its founding proteins: TLP18.3, Psb32 and MOLO-1. In Arabidopsis, this domain is called the thylakoid acid phosphatase -TAP - domain and has a Rossmann-like fold. In plants, the family resides in the thylakoid lumen attached to the outer membrane of the chloroplast/plastid. It is active in the photosystem II.	1.58551e-40
NZ_AP019735.1\|WP_141413018.1\|2401388_2403890_-\|polysaccharide-biosynthesis-tyrosine-autokinase	gnl\|CDD\|349772	cd05387, BY-kinase, bacterial tyrosine-kinase. Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.	3.73825e-49
NZ_AP019735.1\|WP_141413015.1\|2393955_2395296_+\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	2.14537e-49
NZ_AP019735.1\|WP_141413011.1\|2387123_2388023_+\|DUF4831-family-protein	gnl\|CDD\|374372	pfam16115, DUF4831, Domain of unknown function (DUF4831). This family consists of several uncharacterized proteins around 350 residues in length and is mainly found in various Bacteroides species. The function of this family is unknown.	2.72455e-30
NZ_AP019735.1\|WP_162852315.1\|2409283_2411263_+\|glycoside-hydrolase-family-97-catalytic-domain-containing-protein	gnl\|CDD\|371140	pfam10566, Glyco_hydro_97, Glycoside hydrolase 97. This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.	1.79877e-124
NZ_AP019735.1\|WP_141413023.1\|2411390_2415053_-\|hypothetical-protein	gnl\|CDD\|318484	pfam16255, Lipase_GDSL_lke, GDSL-like Lipase/Acylhydrolase.	2.45077e-25
NZ_AP019735.1\|WP_141413024.1\|2415239_2417615_-\|outer-membrane-beta-barrel-protein	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	5.22725e-99
NZ_AP019735.1\|WP_141413019.1\|2404845_2406141_+\|alpha-amylase-C-terminal-domain-containing-protein	gnl\|CDD\|200452	cd11313, AmyAc_arch_bac_AmyA, Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	3.24758e-167
NZ_AP019735.1\|WP_019129972.1\|2399337_2400201_-\|M23-family-metallopeptidase	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	6.33987e-20
NZ_AP019735.1\|WP_141413022.1\|2408673_2409255_+\|LemA-family-protein	gnl\|CDD\|377192	pfam04011, LemA, LemA family. The members of this family are related to the LemA protein. LemA contains an amino terminal predicted transmembrane helix. It has been predicted that the small amino terminus is extracellular. The exact molecular function of this protein is uncertain.	9.32536e-76
NZ_AP019735.1\|WP_141413012.1\|2388019_2388667_+\|DNA-alkylation-repair-enzyme	gnl\|CDD\|132880	cd06561, AlkD_like, A new structural DNA glycosylase. This domain represents a new and uncharacterized structural superfamily of DNA glycosylases that form an alpha-alpha superhelix fold that are not belong to the identified five structural DNA glycosylase superfamilies (UDG, AAG/MNPG, MutM/Fpg and helix-hairpin-helix). DNA glycosylases removing alkylated base residues have been identified in all organisms investigated and may be universally present in nature. DNA glycosylases catalyze the first step in Base Excision Repair (BER) pathway by cleaving damaged DNA bases within double strand DNA to produce an abasic site. The resulting abasic site is further processed by AP endonuclease, phosphodiesterase, DNA polymerases, and DNA ligase functions to restore the DNA to an undamaged state. All glycosylase examined to date utilize a similar strategy for binding DNA and base flipping despite their structural diversity.	9.41034e-05

>NZ_AP019735.1|WP_019129972.1|2399337_2400201_-|M23-family-metallopeptidase
MKGFSPISRAYRRLVRKHRLTLQNEVDNAEEWHMHISVVRIFAALLAFVLLLFILILSLVAYTPVLEFLPGYEANRSREMLLQNIMRLDSIERQMTQMRTYSDNIALIMEGKTPVVRNVGGLDSIKADKTLVMPSREDSLLRIQMEGEGPYGLGKSPSRKTLREAMAMTAPVEGIITEKFDTKLGQYGIRIAAAPGSQVSAVDNGTVVLSLWSPEEGYVVQVQHADNVLSIYKNLAQSMVSTGQRLRSGEVLGYSNDPQAEGTDSKLFGFELWSDGKPVDPEGYIVF
>NZ_AP019735.1|WP_141413017.1|2398156_2399308_-|1-deoxy-D-xylulose-5-phosphate-reductoisomerase
MKQRIALLGSTGSIGVQTLDIVRENSELFEITTLTAHRNWEALARQAEEFAPDSVVIADDSKYDALRRALADRPVKVYAGADAIRQVVQADTVDTVVNALVGYAGLLPTVAAIEAGKKVALANKETLVVGGDYVMRLAAERRVPILPIDSEHSAIFQCLVGEASPARRLIVTCSGGALRDVPRERLAEVTVEQALRHPQWRMGAKITIDSATLVNKGFEVIEARWLFGMPAERISVLIHPQSVVHSMVEFEDGAIKAQLGTPDMHLPIGFALLFPRRAARAAEQFSFADNPTLTFAEPDRQKYPALDMAYDCLRRGGTAACTMNGANEVAVAAFLAKRCGYLDIVRTIEHALEEATFVARPTLDDYAASDAEARRIAREFLKI
>NZ_AP019735.1|WP_019129974.1|2396823_2398146_-|RIP-metalloprotease-RseP
MDILIKVIQLFLCFTLLVGIHELGHFLMARVFGIRVEKFYIFFDPWFSLFKFKRGGTEYGVGWLPLGGYVKIAGMIDESLDTEQMKQPVRPDEFRAKPAWQRFLVMIAGIVMNILLAVAIYCGICYTWGEKYFANEDAVYGYTFNTAAQGLGFENGDKIISIDGEPIDDVNAIAMTLLLTESDRTVVVERDGREERFTIPFEQLVDFRRSKGYEEMLMLRTPFRIDSVASPAALDAGLRAGDEVVALNGERHIEFAEYVGLLADHKSSDVQLTVVRGDSTAVLTVPVNADGKIGVTVARHDYRLRTKEYTFWQSIPAGIRRTGSVIANYWEQLKLIVQPKTQMYEELGGFIAIGSIFPSAWNWQDFWSKCAFISIILAIMNILPIPGLDGGHAIFTLWEMITGRKPSDRFLEAAQYVGLAIILVLLVYANGNDIYRFFIK
>NZ_AP019735.1|WP_141413016.1|2395357_2396731_-|DNA-repair-protein-RadA
MAKVKKAYFCKECGYEAPKWMGRCPACGEWNSFTEEIVARESGSVPAAMTSALPRSTPQRVGEIRSNDRPRLDLGNAEVNRVLGGGLVPGSLVLLGGEPGIGKSTLSLQIALADNGLKTLYVSGEESAEQIKMRADRIGIGNDACMVYSETLLENIMAQLEEQRPDLVIIDSIQTIYTDLVESSAGSVSQIRECAATLLKYAKGSGTSIFIIGHITKEGAIAGPKILEHIVDVVLQFEGDNNQVYRILRGIKNRFGATFEIGVFEMLDAGLRPVGNPSEILLTHYDAPLSGIAVGASVDGIRPYLIEVQALVSNAAYGTPQRTATGFDYKRMSMLLAVLEKRVGMKMYTKDVFLNFAGGFKVADPGLDLAIIAAVISSYYDRPIGEGICCAGEVGLSGEVRPAPRTEQRISEAARLGFRRIVVSGYLPKGAKRPKGIEVVAINSIDQLPRALFINEE
>NZ_AP019735.1|WP_141413015.1|2393955_2395296_+|TolC-family-protein
MKRLLIILTLAGLPCTPFAQTRLTLDACIEQAEANNKALAAADRQLAAAQFDFRSARANFFPSFSATGTGLYSTADGGLDIAGGALPVLGVDGMPTGGTALFPGLNLAYEVGWVYGGGITLEQPLYMGGKVRTGYRMARIGSEMAEQNRRLTRSEVIVSTSRAYASVIRAREMRQVAERYHALLTELLRSVESARKHGLKPQNDVLKVRVKLNESELNLRRTENALRLATMNLCHLIGRPLTDRIEVADDLPDLPSTPVPAVDLMARPEYRLLDRKAELAREQLRLARSERLPQVGLVGNYGYLHGVELNGQNLLGGWAFTAGVQVSVPIFHFGGRSNKVRSARARFEQAQAERLDGGELLQLEATQAANNLDEAQLEIRLAESSLAAADENLRLSRRQYEAGVETLSDHLEAQAMWQQAHRTEVEARIDGYLRWLEYRKAAGLLD
>NZ_AP019735.1|WP_162502323.1|2390836_2393959_+|efflux-RND-transporter-permease-subunit
MDFGKWAFANRKLVYFVVAVLLVGGILSAYDMSKLEDPEIKVKLAMVIATRPGASAHEMELEVTDPLEKNIRTMGEVESVTSSSFNDLAILEVELKSTVRDADVEQCWDMLRRKASDVQRRLPSGTSVVVQDDFGLVYGMLYALTGDGLTERQLSDYAGLLKRELGDLDGVARVEIYGEREECIDISILPEKMAMLGVSPAEALATLNGQNNVYYAGYYDNGPDRIRVAVADKFRAVKEIESMVIQGHEDDQLRLCDIARVEHGYAEPVRNEMSYEGQRALGIAVAAASGSDIVKVGAEVERCLAELQAERFPAGVACHKIFYQPERVKDALGTFLINLIESVVIVVAILMLTMGFRSGMIIGISLVVTVVGSFLILGMADGTMQRVSLAAFILAMGMLVDNAIVIVDGILIDLKLGKPRREAMTAIGRKTAMPLLGATLIAILSFLPIFLSPDTAGVYVRDLFIVLAVSLLLSWVLALVHVPLMADAWLGQSAAPAGGATLYDSAVYRWLRAALGFGLRHRWSSIAVALVLVGLSVWGYGYMRQGFFPDMVYDQLYMEYKLPEGTNSTRVKADLEEIRRYLKSRPEIRSVAASIGGTPARYNLVRSIATPSLSYGELIIDFESPEALERNIDDIQQTLSDRYPDAYVKLKRYNLMFKKYPIEVQFTGPDPAVLHRLADSARCIMERTPEVCLITTDWEPRIPVLNIDYDQSAARRMGLSRQDIAVSMLSAAGGIPVGAFYEGTHKNTIYLKCTEADGKPVDNLENVPVFPMMPNLAGLFDEELLLKLKSGAIDRSELLESVLHTVPLKQVSRGVQVEWEDPVVPRYNGQRAQRVMCSPAPGIETEAARLAVAERIEAIPLPSGYALSWEGEKGASDETMRYLFKNVPLGVVLMIAILILLFGDYRKPAVILCCIPLLGIGVVGAMLLTGKVFTFCAIVGALGLVGMMMKNCIVLMDEIGAQIAAGADPASALVSSSESRLRPVMMASLTTILGMIPLLGDAMFGSMAATIMGGLLFSTFATLFFVPILYALFFKIRIDR
>NZ_AP019735.1|WP_141413629.1|2389793_2390837_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MGMVCLLACCCGCSGRPEGAVRLPIVRIDTVGVYGTPRTVQFPGCVRAAQEVNAAFKVGGTLRTIFAEEGEFVRRGAPLAALDARDYRLQAEAAEAEYKRVKAEAERVMALYADGAATPDAYDKARYGLQQITAKYENSRNQLADTEIRMPFDGYVQKRLFDPSTVVGAGMPVLTVVSAEAPEIEINIPGSEYVRRSEFDGFEAAFDFWPGKRIPLRLRSISPKANANQLYTLRLGVPADLRPLPSPGMNTMVTIVCRPSGAAQVAVPAVALFDDGDRTCVWICREDSTVVSREVRVERLQTGGEAVVGAGLAAGERIVTSGVHRLREGEKVAPLPGVTKTNVGGLL
>NZ_AP019735.1|WP_141413013.1|2388751_2389612_-|helix-turn-helix-domain-containing-protein
MDTPVTPSIGLFHADKQTVEALGPVVQLAKSGFFYCTQGEMSLVLGNRAFEIHRGDIYIYPPLSKTYIRMLSDDLHGTVGVADFDFVFTLANSISNTQNHLYMRENPCISLNDEQRRRIEELIELIRRRERSQGSRSTNENNRLIYNQLLSSLGKALCCEIAEAYFFNHPIQPLKQDRKDRIFQSFIFSLSQNFRTHHSVSFYAAEQCLTPRYFSTIVREKSGRNALQWIMMFIIAEAKKLLSDPDPSIKEIAETLGFSNQSFFGRYFKQYVGLSPMAFRSSGTKE
>NZ_AP019735.1|WP_141413012.1|2388019_2388667_+|DNA-alkylation-repair-enzyme
MTNHTARMAALLGELRREMNGAVAESMQRGEGGYGLNYGVSIPTIRAIAGRVGTDHAFARFLYRQDVRELRMAAPTIADPASVTPDNVDEWFVGRMPEELIEELALRLLSRCGRPVLDTLCGRWLRAGSGAERYAALMALARARVQEFDAAAVVEAVPDAVAACPDDLRLARGAAAFVQSASARIAPERLARMIERLPDSRGGAYLRDELAWMIL
>NZ_AP019735.1|WP_141413011.1|2387123_2388023_+|DUF4831-family-protein
MKTLVSLLCCTALTVGSASAQSYRVARAGAFEENGRVEVGIPTSPLAVDLTVEKEVVTVGPYARYAQKFLGVRGALSDKTLYSVKAARVALLDRDATTASEVPAGEVRATSYLGDTETFSRVPFDKRSLVDESLETAARNAANTLFAIRRHRMELITSEAGEHVFGAGLQAALAELDRQEQAYTELFLGKRVTTTSVERITVVPDAGKQKYILCRFSPDRGLLPGNDLTGDVVLLQLDKESDGSFTLTPASPKAARTATYRVAADVVCTVYCGTEELTRATLPLFEFGRDVELALPSKK
>NZ_AP019735.1|WP_019129971.1|2400991_2401381_-|hypothetical-protein
MAIRDAIIAVDFDGTVVTHAYPHIGNDIGAVPVLRELIGNGCRVILYTMRSGRLLDDAVAWFARNDIPLYAVNENPAQREWTDSPKVFADLYIDDSALGCPIKFEDGIKRPFVNWVKVRQRLVEEGFLD
>NZ_AP019735.1|WP_141413018.1|2401388_2403890_-|polysaccharide-biosynthesis-tyrosine-autokinase
MEENRNVNNVPAEGNEDSINFSIHDLIQMVIGNWFWFLLSTVVCLSCALFYIYTAPKVYNRTATILIKDGKKGSETDIAAFGDLLGATARRNVDNEIIVLKSRNLMTEVVRRLNLHVNYVVKHGLRTENLYRRSPIDVTFIDDNERQALAFELTPVDNEKFSLTKFVNRTSADSDKDKDSEIYEVEMTGRFNDTITTPCGLLVVTPTLYMSDDYFGDPISVSKQIVSSVASGYNKRIAIELVEKQANAISISLDDNIPRRAEDVINTLIARYNDESINDKNRIADYTADFIDKRLRIIGSELDAVDRKISTYKKDNEMYDITAQATQSLTESSQFKTAGLSVENQISMAQYIRDYLLNDTKLRDLIPANVAITNVSISDQIKNYNELMLRRDKLAGNASSNSPVIQDFDSELAALRRAIIASLQSHISTLEIQLNNIRREESLARTRIASATRQSTELLDNTRQQRIKEELYLYLLNKREENELTKAIADNNARIIDPAYGSSTPVAPRSVIILFIALLFGLATPFGIIYLMEILDTTIRGRKDIEDKLSIPFLGDIPEYHGSTRQGSVVVRDNGRDSVSEAFRLIRSNLGFMSVKSGKLQIIMVTSSNPHAGKTFVTTNLAMTLALADKKVVIVDLDLRRRTLSKQMGQRDNRNGVSGYISGTIANLNDIVFQSGLHENLDIIFAGLQPPNPAEMLLSEKFDEFMADLRKRYDYVVIDSVPAMAVADALITDRLADLTIYVIREGLLDRRQLPDIEKLYREKKFHNMSIVLNGSTGGARRGYGYGYGYGYGYGYGYGYGYGEDESQKSSAVIDSRYNLTQRLKDFLGLNDKK
>NZ_AP019735.1|WP_019129969.1|2403906_2404695_-|polysaccharide-biosynthesis/export-family-protein
MKHLGIFILGALLLASCATNKRAAYIQQVQTDIPTAIEQDYQIRIKPLDRLTVTINSKDPELAAPFNAASSYNSLNGLSSYSSSSNGNLQILTVDKEGKIQLPIIGEIDCDGLTRNELAKKIENTIRENGMVHDPIVIIQFADVKFSVLGEVARPGQFSITKDRISLFDALAMAGDLTIYGQRENVALIREENGMRTVHYFDLKNPDILTSPYFYLQQDDVVYVTPNKYKAQAGEINQNRSFYISLVSVAVSVATLLVTITR
>NZ_AP019735.1|WP_141413019.1|2404845_2406141_+|alpha-amylase-C-terminal-domain-containing-protein
MDETTHIPHPAWSYPAVIYELNVRQLTPEGTFAAAEKHLPRLRELGIDAVWLMPIHPIGETNRKGTLGSYYAVRDYCGVNPEFGTMADFDRFVSTAHGLGLKVLLDWVANHTARDARWVTERPADWYERDAAGEPVVPNGWDDTAKLNYANRAVWQGQIDAMRFWLAEHGVDGFRCDMAMLVPTAFWQEAAAQLREVKHNLFMLAEAEQADLFDRAFDACYAWEFHHIVNDIAQGRRRVWDLRNYLYADRDRYPRSAMRLMFTSNHDENSWNGSEFRRLGDAAGIMAALTFVLPQSMPLVYTGQEFGYDHSFAFFDRDPMVDPRPGRFTELYRLLCLLKHRNRALQAGERGGSFVEIENNAKDCLMTFVREVEGNRVLCVMNLSPYAIHADFNTGVYQGEYADALTGNRIVVPYRVEQDMAPWSYRILIRE
>NZ_AP019735.1|WP_162502324.1|2406592_2407483_+|WG-repeat-containing-protein
MLSGFTEFPDNLPADIAAVERKNGPKYDQYYFDAFYAKLLRFLDSRPVERAAAPFGEPAAGSSTLKIKSDTDCRIFVDDEERGTARAGSLFRLPLRGGSYLLRFVSVENPADAVEQTWRIEKDVEELYVVALAPVRRQREEREKREAAARAEEERRRREAYLLQLPDERFVTFKDNSGKYGFSDRENSELLIPANYGYAYSFSEGLAKVKKDGKLGYIDKSGKTVIPLIYNDAGPFRVGLACVQKDRKWGYIDKSGKTVIPFIYDDAYSFRVNLAYVKKDGKSGYIDRSGRWVKDA
>NZ_AP019735.1|WP_141413021.1|2407606_2408515_+|TPM-domain-containing-protein
MIRNLLLLVCLCAWLPAAAHPYAVEQIENVQSADRTRFTSNPDGILSQAAVARIDSICYGLRRRGAAQVAVVAVDAIAGGDPFTFAYELFSKWGVGRREDSNGVGILLVREQREIRFVTGRGVEGVLPDALCKRIQTNYMLPAFREGDYDRGMVRGVEAVAAVLAGSELETGVPDAVPQEDDTPWWVIALIVGGCVAVPLVAVVRMLRCPRCKRWFALRSQGERIVLRAEGWRMVEQTLVCRRCGETIRRRRREADGSDIGGRGGGMWIGGRGLFGGGFGGGHAGGGFGGGGFGGGGAGSKW
>NZ_AP019735.1|WP_141413022.1|2408673_2409255_+|LemA-family-protein
MKKSLWIVLAVVAVLAVWGYSVYNGLVEKEEAVHGAWSNVETQYQRRSDLIPNLVNTVKGYAAHEQQTLAAVVDARSKATSMNVDADDLTPERLAAFQQAQEGVRSALGRLIAVAENYPDLKANSNFQELQAQLEGTENRIAVARTAFNEKTQAYNVAVRRFPANLVAGILSFGQKPYFEADDSAAQAPEVAF
>NZ_AP019735.1|WP_162852315.1|2409283_2411263_+|glycoside-hydrolase-family-97-catalytic-domain-containing-protein
MKRFFLLTLASAALLGASAAPVKTYEVKSPDGRLALVLTAGERLSFTVARDGETLVAPSEMALTLSTGEVLGESPRVRSARRRAVTETIDAPLYRQSRFDAAYNELDLRLRGDYGILARAYDDGVCYRFYTERDGELTIVDETAQLNFEGDPSAYIPYSKTEIPMRTSFENTYEYAPLSKFRTQTVAFMPVLVDLGERGYVLYTESDVEAYPGVYLTYDKEAKGFAARFAEYPTETSLTKRFQDVVERSADYIARVDGRRSYPWRIVAYAATATELPVNDMVWQTAEASRVADASWVRDGKIAWDWWNNWGLYGVDFKSGINTETYKYFIDFAAANGIEYVALDEGWGVRDGDVMHVVPEIDLPEIVSYAREKKVGIILWVVAKVLDDKLEEACRYYSELGVAGWKVDFIDRQDQAAVERVYRIADAAARYRMIVDFHGVYKPTGLQRTYPNVVNFEGIFGLEQLKWTDKTDADMPAYDCTFPFIRQVAGPVDYTQGAMRNASRKNFRAVNNHPMSQGTRAHQVATYVVFDSPLVMLCDSPTAYEKEPETLDYIVRFPTRFDQTLIPAGEIGRYIVTARRAGDRWYLGALTNWDAREVEVKLDFLGDGRWKARIFRDGVNADRYGEDYLLEERTVTAADSLAMPMAPGGGYAVQFERVQ
>NZ_AP019735.1|WP_141413023.1|2411390_2415053_-|hypothetical-protein
MKREEIKKPDYTAGIRHTTVGSDRHDVRRENFRNKTVRTAKRRSGLIGRLFACSATLALALGACTDDAPVEQPKSGGVDLTCIVESDLTAALGSSTDNRHPWESGDRIGVYAVSSAPTLNAEASVTTNDGTSSIAFHVNRAETGDKLHAYFPYTKDNSSNDAKNVALSIAAVQSQSEAGAFDIANLPMVSYPQRLDAESLSEIPALQMHVLGGILRAKVFADGQYGDEKVQSIAFADENTPMAGAFKLDLTGLSDEASLIVTGLASRTAKTQLSIPYAVPSSQASAKDIYMILAPGTYDGTLSVTTEKAVYTQPFQCEMKRNACYDASINLSTAARESIDGWNGEGTAEAPYQVATAEDLQRLIALCNSDGGEYAEFADKHYLQIADIDMAQIAIQPIGLSEQSPFRGVYDGGGHTIGNFTLTNCESGACGLFGYLDGATVKDIHLEECEYSASGLHAGGVAGVAKQSVIRGCTFEGSLVGTAETEFDGYAVSDVGGIIGYALDSEIAGCTLKGSIRALTQIGGMAGYTSGTKISDCTVDAAATIDAETHFLGGIVGRARHNSTIENCTVGGKASAYNGNYVGGIAGHLTSGKISGCTIAASASLSSKGDHTGGIVGALQANEENADDGSNMTAVVEDCETDIMVFGADNVGGIAGYQGTATAEHTSIVRNCTSRESVTGYGYNTGGISGSITSYGDSFIENCQAYGDVSSSLHQVGGIVGYIVSKGETAVDGCIAYGNCRGQHSVGGICGYAKCNDAACIVDIVNSIYAGREVEATGNNGSNGYTLATGLVGWLQVGTGKAHIVNCASRVQTVKTVGKAGGYPSANNTLSGILGFQNGSPTAAELYGLYSTIGRNGFLTDGEPSTSIYCGGIYAKIHSGSYTITSLKHCYFDPSTQAGPGISNLTKADAATVKAYGEMSTLLADLNAAVAAYEGTCGRTLKNWTLDADGYPVIEGMTTLLPVSKTKRISVIGDSISTFRGFVPSGYSCHYPTSDHDLTSVSQTYWYRLAHDLMSDARIERNISFSGTAVARTTDPAYASQAWYGNDFCARFIAQGGVGQPDIVLIHGGTNDYAHNVDPLAPGLPIQSAEAPSEAALAELFAAADAAATRAEIEALDDTTFCTAYIKLLRLLKERYPDVKIVCIIGDYLSTGIERSTLAIARHYGARCVDLYAVNGFNDQTYMPKHDYNPATGKGCHPSSEAMKFIADKIYAELGSWLEE
>NZ_AP019735.1|WP_141413024.1|2415239_2417615_-|outer-membrane-beta-barrel-protein
MKQYLLRMPLLLLFAALAVDASAARQTPTTGRVVDPDGTAVAYATVVLLDAETQLAGTATAADGSFSLKVPAGRYRLTIQYLGYETLTRDVDTPGDLGEFVLHPASVEMQEVVVKTSLVRREADRFVMEIAGSPVALGKDGTELLKQAPGVWLTDDKIAINGASGVKVYINDREVRMSTEQLLNYLRGLKSEEIQRIEVIPQAGADYDADSAAGIIRITLRRQRDNGLTGDLSFSTRQSRQIEGYNPSLSLNGHAGRWTFNVSGWASVVPLHVTKTAEHTEYRAGGALLDASSEMRGRDNCGGGRAGAIFDISERHSIGAEADFYIDRDRSPNRSSTDFREAERLTRNESLYDGSERVNTFSATFNYIWRIDTLGSTLKVMADYSRNNRRHGNDSFVRSTAAGIVRDSTYDDRTRGLYNVAALNAALEKRLGEAWQLRAGAKYTYNDMHNEALYRYLRPEGWETLDTYSYVTDYTEHITAAYAAATLKKGHWNVVAGLRGEYTRTTGYGSDVRQRYFSLFPNANLTYAFDAAGLWSLTVQYARNISRPGFWALNPMRMQISDYTYQSGNPDLLPAYTDNLSLTAVFAGKYSLSAGAQLHHDEIAQVFGSDAADASITNLRFENLDRTEQYFAAANIPLQLTKWWTLNANLTGICRRDRITADAPLRTTWAAFANAATTFTLPRKFFIEAEYYAMSRFRQANLDMKSYHSVTLSLKKRLLDNRLTLTAQVANLFDRSQRFVAETETFVRDLRVSNDWQPRRFVLTVNYNFKTGKTFKARKVESGAGDEKGRM

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Crispr_ID: NZ_AP019735_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_14

2498651-2498768

Orphan

Consensus_repeat	Method
CAGCCAAAGACTACGAATAAGCGAGTGCAATGTCGAATTTATTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_14

>merge|NZ_AP019735|14|2498651-2498768|CRISPRCasFinder
CAGCCAAAGACTACGAATAAGCGAGTGCAATGTCGAATTTATTTGGACATTGCCGAGCGGGAGTATCTACGGCGCAGCCAAAGACTACGAATAAGCGAGAGCAATGTCGAATTTATTT

>NZ_AP019735|14|14|2498651-2498768|CRISPRCasFinder
CAGCCAAAGACTACGAATAAGCGAGTGCAATGTCGAATTTATTT	GGACATTGCCGAGCGGGAGTATCTACGGCG
CAGCCAAAGACTACGAATAAGCGAGAGCAATGTCGAATTTATTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141413058.1\|2496321_2496609_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_034779463.1\|2505166_2506096_+\|lauroyl-acyltransferase	unknown	unknown	gnl\|CDD\|153246
NZ_AP019735.1\|WP_162852316.1\|2486242_2488489_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_AP019735.1\|WP_141413065.1\|2509659_2510778_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019129902.1\|2496616_2497351_-\|SIMPL-domain-containing-protein	unknown	unknown	gnl\|CDD\|225414
NZ_AP019735.1\|WP_141413057.1\|2494653_2496186_-\|glutamate--tRNA-ligase	unknown	unknown	gnl\|CDD\|234953
NZ_AP019735.1\|WP_141413064.1\|2507099_2507834_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133062
NZ_AP019735.1\|WP_141413062.1\|2503043_2503769_+\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	unknown	unknown	gnl\|CDD\|381175
NZ_AP019735.1\|WP_019129894.1\|2507931_2509611_-\|glutamine--tRNA-ligase/YqeY-domain-fusion-protein	unknown	unknown	gnl\|CDD\|235424
NZ_AP019735.1\|WP_141413059.1\|2497451_2498552_-\|redox-regulated-ATPase-YchF	unknown	unknown	gnl\|CDD\|236583
NZ_AP019735.1\|WP_141413055.1\|2490352_2493466_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_AP019735.1\|WP_141413056.1\|2493946_2494654_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|185696
NZ_AP019735.1\|WP_141413634.1\|2488863_2490330_-\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	unknown	unknown	gnl\|CDD\|378943
NZ_AP019735.1\|WP_141413060.1\|2498890_2501410_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376626
NZ_AP019735.1\|WP_141413063.1\|2506083_2507103_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133029
NZ_AP019735.1\|WP_141413053.1\|2484841_2485558_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|187608
NZ_AP019735.1\|WP_019129898.1\|2503758_2505141_+\|TIGR00341-family-protein	unknown	unknown	gnl\|CDD\|377221
NZ_AP019735.1\|WP_141413066.1\|2510860_2511397_+\|RNA-methyltransferase	unknown	unknown	gnl\|CDD\|349970
NZ_AP019735.1\|WP_141413054.1\|2485665_2486238_-\|nicotinamide-mononucleotide-transporter	unknown	unknown	gnl\|CDD\|377432
NZ_AP019735.1\|WP_141413061.1\|2501806_2503039_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236766

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_034779463.1\|2505166_2506096_+\|lauroyl-acyltransferase	gnl\|CDD\|153246	cd07984, LPLAT_LABLAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.	9.91463e-38
NZ_AP019735.1\|WP_162852316.1\|2486242_2488489_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	2.08653e-35
NZ_AP019735.1\|WP_019129902.1\|2496616_2497351_-\|SIMPL-domain-containing-protein	gnl\|CDD\|225414	COG2859, COG2859, Uncharacterized protein conserved in bacteria [Function unknown].	4.05098e-22
NZ_AP019735.1\|WP_141413057.1\|2494653_2496186_-\|glutamate--tRNA-ligase	gnl\|CDD\|234953	PRK01406, gltX, glutamyl-tRNA synthetase; Reviewed.	0
NZ_AP019735.1\|WP_141413064.1\|2507099_2507834_+\|glycosyltransferase	gnl\|CDD\|133062	cd06442, DPM1_like, DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.	1.1194e-88
NZ_AP019735.1\|WP_141413062.1\|2503043_2503769_+\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	gnl\|CDD\|381175	cd11648, RsmI, Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase. RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.	2.78102e-125
NZ_AP019735.1\|WP_019129894.1\|2507931_2509611_-\|glutamine--tRNA-ligase/YqeY-domain-fusion-protein	gnl\|CDD\|235424	PRK05347, PRK05347, glutaminyl-tRNA synthetase; Provisional.	0
NZ_AP019735.1\|WP_141413059.1\|2497451_2498552_-\|redox-regulated-ATPase-YchF	gnl\|CDD\|236583	PRK09601, PRK09601, redox-regulated ATPase YchF.	0
NZ_AP019735.1\|WP_141413055.1\|2490352_2493466_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_AP019735.1\|WP_141413056.1\|2493946_2494654_-\|hypothetical-protein	gnl\|CDD\|185696	cd09019, galactose_mutarotase_like, galactose mutarotase_like. Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.	1.31087e-10
NZ_AP019735.1\|WP_141413634.1\|2488863_2490330_-\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	gnl\|CDD\|378943	pfam12771, SusD-like_2, Starch-binding associating with outer membrane. SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.	2.06172e-55
NZ_AP019735.1\|WP_141413060.1\|2498890_2501410_-\|hypothetical-protein	gnl\|CDD\|376626	pfam01835, A2M_N, MG2 domain. This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin.	0.00455122
NZ_AP019735.1\|WP_141413063.1\|2506083_2507103_+\|glycosyltransferase	gnl\|CDD\|133029	cd04186, GT_2_like_c, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	1.23492e-56
NZ_AP019735.1\|WP_141413053.1\|2484841_2485558_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|187608	cd05350, SDR_c6, classical (c) SDR, subgroup 6. These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	1.00347e-50
NZ_AP019735.1\|WP_019129898.1\|2503758_2505141_+\|TIGR00341-family-protein	gnl\|CDD\|377221	pfam04087, DUF389, Domain of unknown function (DUF389). Family of hypothetical bacterial proteins with an undetermined function.	2.36872e-60
NZ_AP019735.1\|WP_141413066.1\|2510860_2511397_+\|RNA-methyltransferase	gnl\|CDD\|349970	cd18097, SpoU-like, SAM-dependent rRNA or tRNA methylase related to SpoU. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	8.65291e-64
NZ_AP019735.1\|WP_141413054.1\|2485665_2486238_-\|nicotinamide-mononucleotide-transporter	gnl\|CDD\|377432	pfam04973, NMN_transporter, Nicotinamide mononucleotide transporter. Members of this family are integral membrane proteins that are involved in transport of nicotinamide mononucleotide.	2.2429e-45
NZ_AP019735.1\|WP_141413061.1\|2501806_2503039_+\|hypothetical-protein	gnl\|CDD\|236766	PRK10811, rne, ribonuclease E; Reviewed.	2.04191e-09

>NZ_AP019735.1|WP_141413059.1|2497451_2498552_-|redox-regulated-ATPase-YchF
MALQCGIVGLPNVGKSTLFNCLSNAKAQAANFPFCTIEPNVGVITVPDERLVRLAEIDRPKRVVPTTIEIVDIAGLVKGASKGEGLGNKFLGNIRNTNAIIHVLRCFDNGNITHVDGSVDPVRDKGIIDTELQLKDLETVESRLAKTQKQATSGGDKNAKRTVELLLQYKAVLEQGRSARTVELDKEGRKLVADLNLLTDKPVLYVCNVDERSAATGNAYTEAVRAAIADERAEMLVIAAATEADIAELEEYDERQMFLEEIGLQESGVARLIKSAYKLLDLQTFFTTGADETRAWTFRKGMKAPQTAGIIHTDFERGFIRAEVIKYDDYVTLGSEKACRDVGKIGIEGKEYVVQDGDIMHFLFNV
>NZ_AP019735.1|WP_019129902.1|2496616_2497351_-|SIMPL-domain-containing-protein
MNREHIKYAIIGIAIILSAYLLGRAYTYKYRSQDTVVVTGLGETEFESDLIVWSGVLTAEAAEAADGYRRIEQSKRKVSDYLAAKGIDAKQVVWNFVNVDKTYQTVYSANGNYAGQRFTGYSLRQEFSIESTDVDLVENVSREISALIAQGVSIEARQPDYYYTKLDDVKLSLIERASADARARAEKIAQNAGTGIGAVASARMGVFQITGANANEEFSAGGSFNTASRHKKARITMRIEYRIK
>NZ_AP019735.1|WP_141413058.1|2496321_2496609_-|hypothetical-protein
MNLSERILRIATSHWTERSCFALTLAAALTGDGRMWIAAGTAVALTVGAIVAGSIAPLREARHAARDFPHTPEYEAYARRRAANEADDRHRIELK
>NZ_AP019735.1|WP_141413057.1|2494653_2496186_-|glutamate--tRNA-ligase
MTRPVRVRFAPSPTGPLHIGGVRTALYNYLFARRHGGKMILRIEDTDSQRFVPGAEAYIIESLEWCGIHIDEGVGQGGPHAPYRQSERREIYLKYALQLVDAGWAYYAFDTADELNALRAQYEERGETFAYNASVRERLATSLALPADEVRARIERGDQWVVRFKMPADETVRMHDLIRGDVEVNTSTLDDKVLYKSADALPTYHLANIVDDHLMEITHVIRGEEWLPSLPLHYLLYRAFGWEATQPEFAHLPLLLKPTGGGKLSKRDGDKMGFPVFPLFWQSPTGETAHGYREDGYFPEAFINMLALLGWNPGTEQELFSMQELINAFSLERVSKSGARFQPDKAKWFNAQYMHRKSDAELAALYQPILRAHGIEVTDEVAGRAAGIMKERATFITDLWELTSFFFVAPTQYEEKQARKYWKGENPDRLREVREVLASIDDFSLENTERIVHAWIEQKGYPMGQIMNTLRLALVGAGKGPGMYDVTSFIGKEETLRRIDALLANLKPVE
>NZ_AP019735.1|WP_141413056.1|2493946_2494654_-|hypothetical-protein
MEIEQYLWGASAEGEGILLYTLRCAGGREVRLSNAGAAVTGIFAAGADGRPEALTPVFETPEALLADYADRGKTLCANRYGFGQRIWQSRVETDRIVMELPAGDDGLPALAVLFDLDDDGQFAVTHLARGATAAPFTMTTQLFWQGDWRPTLRTQEGPATDDGRFYPVEGWRRNILGEAARLDDPAAGRTIEILTSQPEIRIVRHDGQLALLCGDSRPAPLDDETLYCQKDVYRF
>NZ_AP019735.1|WP_141413055.1|2490352_2493466_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MINKILLSLIAVLCLDATVTAQNKQVSGTVTDPAGAPVVGATVLVEGTTIGSTTDASGHFSLNAPEDAKLNISFIGYEPQQVDVAGRTHIPVSLKEDSHTIDDVVVTAMGITRSEKTLGYSVSTVKSDELTKARDGNVLNALSGKVAGVNISSSSGTAGGSSRIIIRGQSSLGSSGQPLFVIDGMPVSNQSYDPGNAGSALSGAAVDPGNRMGDIASDDIESINVLKGAAATALYGARAKDGAVIITTKKGSKNQQTSVSINSTMRFESVLRLPDFQNSYAQGVPTTGAYSYGYQNGWGPKIEGQTVKNFLGQDVQLRAYKNNVKDFYQTGHTYINSVAVSGGDDKNDFRLGLTAHNQTGVIPNNEYDKYNVSFNGGRKFNDKLEARISFSYAHTTSQGRPAQGSNDVNVLVNQINAIPRTTDINWLKNNWYAQDGTTVTQASVDEAGKTGNLYWTVNKNKNTGTVDRMFGSAVISYKPVKGLTITNNLGTDFFEEQRRQIYAWGTVGLPDGQFNTNNITYRQINNDLMISYDTTFGKDWSFKAMLGHNINQNFTKYLDVTAKNLLVADIYSYANAESVITTNDQAKSRLIGVYGEIDLGYKDIVYLSVTGRNDWSSTMPKSHRSYFYPSVSAGFVFSQLIPQNDVLSFGKLRLSYANVGSDTVPYALDFLYTPESSIFLQYVGNNSIPHGGLLAYMAPATYPDPNLEPQNQSSFEIGTDLRFFNGRIRLDATYYYNKTTKNIVRLDVANSTGFFYMRKNAGTITNEGVEIMAGFTPVETRNFSWDLDVNFASNRQLVKKLDPSITSYTLSAGFNSLQIKAAEGEPFSLYGTYWMTDDEGNYIIKDDGTRAVSETTKNLGKVAPDWTMGISNTLRYRNLSLSFLIDVRYGGVMYSGTVSDLRVNGMAEETIGKNRTDIVDKGVKQDGTENTTAITPYQFWSNNYSSKVSEANVFDATFVKLREMVLSYQMPQRWFKNCFIGSLALGVEGRNLWLMKSNVPHIDPETNIFGPSAVGSGVEYSAIPTTRSWGFNIKLTF
>NZ_AP019735.1|WP_141413634.1|2488863_2490330_-|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein
MINKILFGLTLTGGSLGLHSCGDWLDINSNELAATKTEAGYLFNYAAINYSSKRVGGDQWLPIIYAAQVASDADNWFVGADMYNISTYATGNGWVTSYSSCGYNLLKAIEFATGENDSNSVAQCKILLANTVWESSMLYGDIPYSEAWNIEGTQTPKFDTQKDVFYSVIGLLDEALDGIDESNSKRIDKYDIYYTGDMAKWRRLGNSLKLKFYMYLANKEDVGDEIKAIIDGGELMNSSADDFVFPFYTTPGNQNPNYQLTVQYPDYYEYCFFANPTVLDPMKALDDPRIPIYFRANADGEYISLEASEKGSVVTDKEISEKPSLCTEAVFQKNNLLRADYPDVICSYAETMFYVAEAYVRGLGVAKDLAQADAAYRKGIEASCVYNGVAAATAASFAAGVPSLSTLGGDDKALEAIASQQRIEMMMRPLEAWSNQRRTGYPALEVPASIRNFYPGIMHRWPYPEREGSVNDNVPHVDGVWTKMWFEN
>NZ_AP019735.1|WP_162852316.1|2486242_2488489_-|TonB-dependent-receptor
MKRFLLPILTGVAAVAAHAQESDSVRMYRLQQIEVTATRATPRTPVAYTDLSHDAIARNSYGTDIPTVLALTPSMIATNETGIGIGGTSIRLRGTDATRLNVTINGVAMNNPDSHSMYWYDTPDLISAVGTMQVQRGAGLSTNGTGAFGGAVNMTTGALSTEFSGEASLSYGSYNTNKQAVGISSGLLGGHWAVDARLTHIGSDGYIDRGATDLKSYLFQGGYYNGRTMVKLLSFGGKAKTYLTYNGVTMEDMERYGRRYHDSGQYQTSAGPHVLADGSHVGYFDDQTDNYLQINNQLILNHRFNNRWALNATAFYTYGYGYYKQYKDDAELAEYVNLDTEIQEADLIREKIMRNHLGGLNASASYTSRALDLNFGGSWSYYTCPHWGELDWVDGMDAGAIGGRWYDNDVDKQDANLFARANWQAAHGLRLFADIQYRYIRYEAWGTNDNYIGQEGMPMQPIDVDKTYHFFNPRAGVSYRLGERNSFFFSFAVAQKEPTRGDFTDRYMFTADYTYPSSEKLYDWELGYTYTAPRLSLGVNLYYMKYKDQLVPMGRINDGYDALNDNVDDSYRRGVELSASWKVTGWFTASANATFSQNRIENYTELRTVYDNDEDWNVISDGPVALGTTKLAYSPETIANLILDFHYGGFEAAFHTQYVGEQYFANNENDALSLDAYCVTNLNLSYSFRTRNARRIRLGLQVNNLFNAEYENNGYGYSTWFRDSPSQHTALYFPQAPLNVLANVTVKF
>NZ_AP019735.1|WP_141413054.1|2485665_2486238_-|nicotinamide-mononucleotide-transporter
MDWKLALQLAGVVLGLLYLWLEYRADIRLWIVGLVMPLVHGALYYKSGLYADCAMQVYYILAGLYGLCVWAKKPKPAERETGRIARTPARMWFRMAAAYAAIHALLYLLLVCFTDSTVPFWDSLTTALCIMAYWMLSRKYVEQWLVWLAVDVVTVGLYLYKDIPLTAGLYLLYSALAVAGYRRWLRRIGQ
>NZ_AP019735.1|WP_141413053.1|2484841_2485558_+|SDR-family-NAD(P)-dependent-oxidoreductase
MKRAIVIGATSGIGRGLAEELAARGYRVGLVGRREALLREIAAADPAAYSCAVADVTQPDAALAALDGLVAVLDGLELCIVAAGTGDLNPDLDFTVEASAIRTNILGWTAVVDWACRLFERQRGGHLVVISSVGGLRGSGAAPAYNASKAYQINYAEGLRQRVAKSGLPVTITDIRPGLVDTAMAKGEGLFWVQPVAKTVRQILRAVERRRHVAVVTRRWRIAAWLLRHLPESLYLKM
>NZ_AP019735.1|WP_141413060.1|2498890_2501410_-|hypothetical-protein
MKSAGYILPLVCAALFLTAYRSTAQPSLYANPFIEQIEHYPQEKLHVSTDKDSYIAGDTIWLRAHCADAATHRPVAASRYVYVELRDDRGSLVRRIKLLSRDSVYSGYLPTQSLERFGDYSLTAYTLYMRNPGPEYFFKKPLTIRPYRESRRTQRNTSVRKVSDFDVSFFPEGGYLIDGYDCCVAFKALGDDGGSVEVAGVVKNDREEVVDTLRTLHGGMGSLRFTAHTGERYYAECTMEGGKTERFDLPASNNLACVLRVLQTERDFTVMVQSGRPLPKGLRLLVHCRGNLCYFREWNDDLPSLIFKRDKLPGGVLQILLLDKAGNALSERLVFNRGEELATTDMQVRGSLKQRTKVTLAVSATDPDGGPAAGDFSIAVTDRAAVPSAMSGSIYSTLLLTSELRGTIETPDWYFEGRDAARVAALDALLLTQGWRRYDVPAAVRGEYATPAYPLEVGQEIAGRINKGGLWNRKKKLDRYEMRMIAPRWHYSLQAPIDKEGRFALNGFDFPDSTLYVLRPAAAKGLLPEATVKVARDSFPEVGTLPRVPETDAASPYLAQARHYIEQRGQTDMRNILIDTVYVTHHKRLESTRPEHRLAAHTWDMQQIKEMGAYSIMEFVQRMPGMNFIGGRLSYHGANVSFMIDGVLDNTTTPHSADADFQAGSTIGQLIVTGTKKKSMTEIALERGGLEPDKNLTMPICTTWPMEWISRIDLIAGGNMFLWGVFDGAIVSITTKTGDELDQALAVAPAIDVSIASPLGYQTPAEFYAPAYATEKARRSMAPDYRTTLYWNPSVEFDETGRATVEFYTSDAPADYDISIEGVTQTGKIVQRRQRLRPE
>NZ_AP019735.1|WP_141413061.1|2501806_2503039_+|hypothetical-protein
MDLKTLRAELQKLAALAEGWDASHEIADIERDLALGKLRELYDAVRFGLDSAVQPSVEDELSPVDLPPMEIDLDAVIPLTAMSEPFGADPAAAPLEEPTIAPPVVESPVAGPSEAPFAAAPAVEPVGTPAEVPAEMPAETAVPAEIPLQAPAEAPVEERTEIPAEAVEGTVGAPVVEPTVDPIGEIPAEAVATVSEPSDATDSEGAPVVAEAPAVVAEPLSLFELDPVDVKRAKHRVVLSLYGDTDSVTPAPGKVEPAAEERPVPPPQAVPAVSPSSADVPQEEPAATSVPVGGAGHRAVPAENGAAVLGETLNSDVKTVSDLIAVTTPPAAVGQEPVADLRQALCNNDRFLLARDLFGGDMDACGRTIDRLNEFDDLDECMIYIAENFDWNPNSDGAKLLVDLIERKLA
>NZ_AP019735.1|WP_141413062.1|2503043_2503769_+|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase
MSKLYIVPTPIGNLDDITLRAVRVLREVDLILAEDTRTSSVLLRHLGIEKRLHAHHKFNEHATAAVVAETIAAGRTVALISDAGTPGISDPGFLLVRTCVEQGIEVETLPGATACIPALVQSGFPCDRFCFEGFLPQKKGRNKRLQELASEERTMVFYESPYRVVKCLEQFVETFGAERPVSVSRELTKKFEQTVRGTAGEVLEHFRRTEPRGEFVLVVAGRPKAGKARRDESENEEYDER
>NZ_AP019735.1|WP_019129898.1|2503758_2505141_+|TIGR00341-family-protein
MNDNETSLQHNGRPARHSWWESLRDDLADRFSLSEDSARQEETVDMICRGVEFRGTNLWVLIFATMIASLGLNVNSAAVIIGAMLVSPLMGPIMGVGLSLGINDFDLLKKSLRNFSLMVVVAIATSTLYFFISPLGTARSELLARTVPTTYDVLIAFFGGLAGIVAQSRKDRNSTVIPGVAIATALMPPLCTAGFGLATGQFKFFIGAFYLFFINTVFIALATYMVVRMLKYHKKKFLDPARERYVKRIMLLITLLTFIPSVVIGLHMVRVSFFESAVDRYVQQEFQFEHTRVIECKKAYKHGDRNSRIELLLIGEPLGEEIIGNARAQLYNYGLQDVELIVRQARTGDRVDLKSLQLSYSELLDEKNAQIDELKQRLSKYKMKNIEYDDISREAGAVVPDIQSISLSKCLSYDVGGTVQDTLLICVVKSRQPMTEADAERLRRWLEVRTKIAQVKLYTE
>NZ_AP019735.1|WP_034779463.1|2505166_2506096_+|lauroyl-acyltransferase
MKRVRSNLTLWQRAMASLVWGCCRLIGAMPHWLRYYVLQDTIYFIVYKCLRYRVGVVTENLRNSFPDRPMAEIKRIRRSFYHNLSEIFISTVSQAAMSDDDCRRRVRVKNLDEVLSDLRGRDALLSTAHFGCWEYDSFLALYTGEHYLAAVYHPLENKVIDAVYMRLRRRRNIRLIPMKEIIRYYIDHRLPAGAPGQRIGIGLIADQNPPLRPNSHWFRFLNQDTVFFDGIEKMALKFHMPVYFCRQRRLRRGYYELEFLRLYDGVEQVAPNEVTERYVRQLESDIVADPGMWLWSHRRWKHRRPQCPS
>NZ_AP019735.1|WP_141413063.1|2506083_2507103_+|glycosyltransferase
MSVVKIVILNWNGAAHLRCFLPSVVRTAPPGVEIVVADNGSTDGSAALVEREFPSVTLLRLPENYGFAGGYNRALERLEGDYWVLLNSDVEPAEGWLEPLIAELDAQPDVAVVGPKLLSCAERDRFEYAGAAGGFIDWFGFPFCRGRILRTLEKDRGQYDDTRDVFWVSGAAFCCRAEVFRRMGGFDAGFFAHMEEIDLCWRMQLAGWRVRVVPRSRVWHLGGGTLQNDSPRKLYLNYRNNLAMLFKCASPVQRVAVAVLRPLADAAAALVYLLKGQCAQAGAVACAYRDFLARHGELARQRRAVQQSKRRRAAHIYHGSIILRYLLGRRVFGERMQGL
>NZ_AP019735.1|WP_141413064.1|2507099_2507834_+|glycosyltransferase
MKKLVIIPTYNERENVSRMISKVMSLFGGYDLLIVDDGSPDGTAAIVRGRQEEFPGRVHLIERSGKLGLGTAYIAGFRWALAHGYDLVYEMDCDFSHNPDDLERLTAAVTGGADVAVGSRYSRGVNVVNWPMSRLLMSYYASKYVRIVTRMPVCDATAGFVCWSRRVLETIDLDAVRMVGYGFQVEMKYTAWKLGFRIDEVSIVFVDRTEGISKMSGGIFGEAFWGVLKLPWRRIRPKLPAARE
>NZ_AP019735.1|WP_019129894.1|2507931_2509611_-|glutamine--tRNA-ligase/YqeY-domain-fusion-protein
MAIETNEPAAKEKSLNFLEEIVKEAADRGVAIQTRFPPEPNGYLHIGHAKSICINFGLAQKYGGKCNLRFDDTNPTKEDVEYVDSIKRDIRWLGFDWALERYASDYFDQLYEWAKELIRKGLAYVDDQTQEQIREGRGTVSEPGKESPWRNRSAEENLDLFERMKAGEFADGEKVLRAKIDMAHPNMLFRDPIMYRIIHARHHRTGDKWCIYPMYDYAHGQSDSIEHITHSICTLEFDVHRPLYDWFIQALGIWPSHQYEFARLNLTYTMMSKRKLLKLVQEGAVMGWDDPRMPTICALRRKGYTPASVRAFAEMVGVAKRDNVIDLGKMEYCVREDLNKVAERRMAVLNPVKVTVTNYPEGKVEYFECVNNPEDPSAGTRQVPFSRELYIERDDFMENPPKKFFRLQPGGEVRLRYAYLIKCEEAVKDAEGNVVELRCTYDPQSGGGSSSDGRRVKGVIHWVSARHAFEAEIRLFNPLFTKENPDDCEEGQTWEDNLNPESMIVTKGWLEPSLAGAEPGRTFQFERVGYFCPDTDTTPGHPVFNRTVTLKDSWAKINK
>NZ_AP019735.1|WP_141413065.1|2509659_2510778_-|hypothetical-protein
MNIRQIFGLLAAIACAGSVQAQRVGWEADFKTRFDNREFTGSSCNESQTIFLADLSTAVSYNWLDRNTLRFGVQMQKDFGDNRDYFSEVRPLASYAYRAERLGADVGIFSRDELRGDYSHAFFNDSLRVYDPTIQGMAVRYRNPKGLRAELVLNWEGMYSEYSREKFRIFGAIHKDWSREADKRWYVGGGLSMFHFANSALTEGNVVDNMLANPYVGFASKAAEVVRRNADGRPTVERPFWYDFRAGFLWAPQRDRIADEGWKTPMGGELRVRLGWKGLEFENNLYVGENLMPLFGRYGSELYAGERWYGTRDRIYNRTRLGYERSFASETIRVQAGMIFHTDGTGLYTQQVVQVSVRLGKTLYDQRNHPQR
>NZ_AP019735.1|WP_141413066.1|2510860_2511397_+|RNA-methyltransferase
MRKITNEELHRPSVEEFAAMPKLPLVVVLDNVRSAQNVGSFFRTGDAFAVERIALCGITAVPPCRELHKTALGAEQSVAWTHHASTVECIDGLRAAGYRVLAVEQVEGAAMLDALAVDPQARYALVFGNEVEGVSQEAVDRCDGAVEIPQLGTKHSLNVSVSGGVVLWEFFCRIRSKA

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Crispr_ID: NZ_AP019735_15

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_15

2575647-2575746

Orphan

Consensus_repeat	Method
CGCCGAAGATACTCCTGCTCGGCAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_15

>merge|NZ_AP019735|15|2575647-2575746|CRISPRCasFinder
CGCCGAAGATACTCCTGCTCGGCAAATCGCAAACTGTGTTTGCATTTGCTCTCACTTATTCGTATCTTTGGCTGACGCCGAAGATACTCCCGCTCGGCAA

>NZ_AP019735|15|15|2575647-2575746|CRISPRCasFinder
CGCCGAAGATACTCCTGCTCGGCAA	ATCGCAAACTGTGTTTGCATTTGCTCTCACTTATTCGTATCTTTGGCTGA
CGCCGAAGATACTCCCGCTCGGCAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141413102.1\|2573738_2574434_+\|thymidylate-kinase	unknown	unknown	gnl\|CDD\|236133
NZ_AP019735.1\|WP_019129855.1\|2568426_2569014_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_026074781.1\|2585829_2588610_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379297
NZ_AP019735.1\|WP_162502297.1\|2589753_2590974_-\|DNA/RNA-non-specific-endonuclease	unknown	unknown	gnl\|CDD\|366523
NZ_AP019735.1\|WP_141413096.1\|2565253_2565877_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|131694
NZ_AP019735.1\|WP_141413106.1\|2584706_2585726_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413109.1\|2591033_2594783_-\|BACON-domain-containing-protein	unknown	unknown	gnl\|CDD\|271342
NZ_AP019735.1\|WP_141413099.1\|2570683_2571439_+\|Fe-S-cluster-assembly-ATPase-SufC	unknown	unknown	gnl\|CDD\|273907
NZ_AP019735.1\|WP_141413105.1\|2580989_2584325_-\|fimbrillin-family-protein	unknown	unknown	gnl\|CDD\|240525
NZ_AP019735.1\|WP_141413638.1\|2575885_2578855_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|224643
NZ_AP019735.1\|WP_141413097.1\|2565873_2566869_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|275228
NZ_AP019735.1\|WP_141413104.1\|2578857_2580756_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413098.1\|2567007_2567325_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|213190
NZ_AP019735.1\|WP_141413107.1\|2588621_2589662_-\|endonuclease/exonuclease/phosphatase-family-protein	unknown	unknown	gnl\|CDD\|197338
NZ_AP019735.1\|WP_019129854.1\|2569217_2570660_+\|Fe-S-cluster-assembly-protein-SufB	unknown	unknown	gnl\|CDD\|236990
NZ_AP019735.1\|WP_019129849.1\|2574426_2575539_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019129839.1\|2595511_2596471_-\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|133030
NZ_AP019735.1\|WP_141413100.1\|2571438_2572257_+\|SufD-family-Fe-S-cluster-assembly-protein	unknown	unknown	gnl\|CDD\|376550
NZ_AP019735.1\|WP_141413101.1\|2572259_2573477_+\|SufS-family-cysteine-desulfurase	unknown	unknown	gnl\|CDD\|131034
NZ_AP019735.1\|WP_162851478.1\|2595033_2595501_-\|DUF4293-family-protein	unknown	unknown	gnl\|CDD\|379484

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_141413102.1\|2573738_2574434_+\|thymidylate-kinase	gnl\|CDD\|236133	PRK07933, PRK07933, dTMP kinase.	4.21301e-38
NZ_AP019735.1\|WP_162502297.1\|2589753_2590974_-\|DNA/RNA-non-specific-endonuclease	gnl\|CDD\|366523	pfam01223, Endonuclease_NS, DNA/RNA non-specific endonuclease.	1.01596e-37
NZ_AP019735.1\|WP_141413096.1\|2565253_2565877_-\|hypothetical-protein	gnl\|CDD\|131694	TIGR02646, Hypothetical_protein_SMc04429, TIGR02646 family protein. Members of this uncharacterized protein family are found exclusively in bacteria. Neighboring genes in various genomes are also uncharacterized or may annotated as similar to restriction system proteins. [Hypothetical proteins, Conserved].	5.39188e-06
NZ_AP019735.1\|WP_141413109.1\|2591033_2594783_-\|BACON-domain-containing-protein	gnl\|CDD\|271342	cd14948, BACON, Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.	0.000872578
NZ_AP019735.1\|WP_141413099.1\|2570683_2571439_+\|Fe-S-cluster-assembly-ATPase-SufC	gnl\|CDD\|273907	TIGR01978, Probable_ATP-dependent_transporter_SufC, FeS assembly ATPase SufC. SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	5.76173e-140
NZ_AP019735.1\|WP_141413105.1\|2580989_2584325_-\|fimbrillin-family-protein	gnl\|CDD\|240525	cd13120, BF2867_like_N, N-terminal domain found in Bacteroides fragilis Nctc 9343 BF2867 and related proteins. Two structurally similar domains with low sequence similarity in a tandem repeat arrangement form a protein that may have a role in cell adhesion. This family overlaps with DUF3988.	0.00226551
NZ_AP019735.1\|WP_141413638.1\|2575885_2578855_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|224643	COG1729, COG1729, Uncharacterized protein conserved in bacteria [Function unknown].	7.01642e-09
NZ_AP019735.1\|WP_141413097.1\|2565873_2566869_-\|AAA-family-ATPase	gnl\|CDD\|275228	TIGR04435, ABC_transporter, restriction system-associated AAA family ATPase. Members of this family are AAA family ATPases by homology. They occur regularly in a conserved gene neighborhood with the restriction (R), modification (M), and specificity (S) proteins of an apparent type I restriction enzyme system, plus one additional uncharacterized protein. It is not clear whether members of this family contribute to restriction per se, or to another process such as transfer of mobile elements.	2.71226e-09
NZ_AP019735.1\|WP_141413098.1\|2567007_2567325_-\|hypothetical-protein	gnl\|CDD\|213190	cd03223, ABCD_peroxisomal_ALDP, ATP-binding cassette domain of peroxisomal transporter, subfamily D. Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).	0.00304114
NZ_AP019735.1\|WP_019129854.1\|2569217_2570660_+\|Fe-S-cluster-assembly-protein-SufB	gnl\|CDD\|236990	PRK11814, PRK11814, cysteine desulfurase activator complex subunit SufB; Provisional.	0
NZ_AP019735.1\|WP_141413107.1\|2588621_2589662_-\|endonuclease/exonuclease/phosphatase-family-protein	gnl\|CDD\|197338	cd10283, MnuA_DNase1-like, Mycoplasma pulmonis MnuA nuclease-like. This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.	9.59583e-09
NZ_AP019735.1\|WP_026074781.1\|2585829_2588610_-\|TonB-dependent-receptor	gnl\|CDD\|379297	pfam13620, CarboxypepD_reg, Carboxypeptidase regulatory-like domain.	1.53976e-09
NZ_AP019735.1\|WP_019129839.1\|2595511_2596471_-\|glycosyltransferase-family-2-protein	gnl\|CDD\|133030	cd04187, DPM1_like_bac, Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.	2.68122e-83
NZ_AP019735.1\|WP_141413100.1\|2571438_2572257_+\|SufD-family-Fe-S-cluster-assembly-protein	gnl\|CDD\|376550	pfam01458, UPF0051, Uncharacterized protein family (UPF0051).	7.87418e-66
NZ_AP019735.1\|WP_141413101.1\|2572259_2573477_+\|SufS-family-cysteine-desulfurase	gnl\|CDD\|131034	TIGR01979, Probable_cysteine_desulfurase, cysteine desulfurases, SufSfamily. This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0
NZ_AP019735.1\|WP_162851478.1\|2595033_2595501_-\|DUF4293-family-protein	gnl\|CDD\|379484	pfam14126, DUF4293, Domain of unknown function (DUF4293). This family of integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 136 and 154 amino acids in length.	1.61168e-36

>NZ_AP019735.1|WP_019129849.1|2574426_2575539_+|hypothetical-protein
MRNRAFKWLSHACRIVLGVTFIFSGFVKTVDPWGTAIKIQEYLSIYGLESLSGLRFGFSIWLCGAELMMGLMLLFKVRIRLISIFALASMIFFTVLTFLSATWLPVEDCGCFGDAVKLTPWETFAKNLVLLPLSVVVWWRYRRDRIFAFSKAEVGCTVLFFSLAMGLGIYCYAHLPLIDFRPFKVGVNIYEAMNAYSADPGPQAGKTVLIYRDRQTGRLHEFSLDDTEWQDAGRWEWVDTRTEELDEPKVDPTLSEFSLRDAEGDATESLLTRPGRVYMLCITDSEGLDAPCERRFRGVVERAAAEGALAVCLTPERLRGVTYRSFAGSAAVRCYNIDATTLKTMLRAFNGMVVLDDGTIVEKRNCRDIR
>NZ_AP019735.1|WP_141413102.1|2573738_2574434_+|thymidylate-kinase
MFIVLEGLDGAGKSTQIRMLQELFARRGVACRYLHFPRFDAPVFGDLIARFLRGELGTVEAVDPYLVALLFAGDRGDAAAEIRQWLASGEAVVLDRYVYSNVAFQCAKLSSEEERRALKRWILDTEYGYYRLPRPDVSLFLDVPFSFTERKLTQAREGGDRDYLQGAHDIHEASLDLQQRVRGVYLDAAREDAAFRVVDCCAPDGSMETPERIFSKIEAALAPLLNAAADA
>NZ_AP019735.1|WP_141413101.1|2572259_2573477_+|SufS-family-cysteine-desulfurase
MFDVEKIRADFPLLSTEVYGRPLVYLDSGATAQKPRCVIDTVDYLHRELNANIHRGVHRLAEEATERYEAARDRIRAFIGAAHREEVIFTAGATASLNTVAYAWGDTFLRAGDNIVVSEMEHHSNLVPWQAVALRKGAELRMLPFDDAGRLMTERLDGLIDGRTRMVAVTQASNTLGTRPDLRPIVEAAHAVGALVCVDGCQGIVHGGADVAALGCDFYAFSGHKLYGPTGIGVLYGRRELLDAMPPFLYGGDMVDRVSFGGTTYAPLPLKFEAGTANFVGAIGLGEAIRYLEQFDPAEIEAYERELLGYAAERLSAVDGLRIYGATPDKCAIVSFTVEGTHPYDVGMILDKLGIAVRTGQHCAEPVMTHYGVPGMCRASLAMYNTRGEIDALAAGVERAVRMLR
>NZ_AP019735.1|WP_141413100.1|2571438_2572257_+|SufD-family-Fe-S-cluster-assembly-protein
MERLDWIGGEGFEALRGQRAALVDGPVYTLLDPTEYAVAVGKGDRARLVIVHTKPESAILSIDVGENAKLSVVEMFIDEAFVECSIRQQGGSLCEVTMAELTSANVSYRIDLDGAFARSELDGLFLAADKEHCEVGVRVSHNVPDCSSRSLVKGVAGGEATGAFQGLVYVAPGAQRTDAQQTSRNVELSTGARIVAKPQLEIYADDVKCTHGATVGQMDDEAILYMRQRGLSEQQARRLQMEGFVAAIAAHCAVEPLCEELYRRIVAKLERM
>NZ_AP019735.1|WP_141413099.1|2570683_2571439_+|Fe-S-cluster-assembly-ATPase-SufC
MLSVKNLHASVDDKEILRGIDLDVKAGEVHAIMGPNGSGKSTLASVLAGNEKFTVTAGSVTFQGHDLLAMSIEDRARLGLFLGFQYPVEIPGVSMANFMKMAVQEQRKYRGEEPLTASQFLRLMKEKSAVVELDPKLMSRSVNEGFSGGEKKKNEIFQMAVLAPKLAILDETDSGLDIDALRIVATGVTKLRTSENATVVITHYQRLLDYIVPDYVHVLYKGRIIHSGDKSLALKLEKEGYDWLINDYREA
>NZ_AP019735.1|WP_019129854.1|2569217_2570660_+|Fe-S-cluster-assembly-protein-SufB
MSEQDNIIKEIEGREYKYGFTSDIETETIPRGLSEEVVRLISAKKGEPEWMTESRLRAYRHWLKMEPPTWAHLRIPEIDFQDIIYYAAPRVRPKLGSMDEVDPELKRTFDKLGIPLEEQMQLAGVAVDAVMDSVSVKTTFKETLSEKGIIFCSISEAIRDYPDLIKKYLGSVVPCTDNYYAALNAAVFSDGSFCYIPKGVRCPMELSTYFRINAEGTGQFERTLIVADEGAYVSYLEGCTAPRRDENQLHAAVVEIVVERDAEVKYSTVQNWYPGDKEGRGGIYNFVTKRGLCRQNARLSWTQVETGSAITWKYPSCVLLGDNSVGEFYSVAMTNHFQQADTGTKMIHIGRNTRSRIVSKGISAGRSENSYRGLVKVARSAEGARNYSQCDSLLIGSACGAHTFPEIACSNRTAIVEHEATTSKISDEQLFYCNQRGLSTEDAVGLIVNGFAKEVMAKLPMEFAVEAQKLLSISLEGSVG
>NZ_AP019735.1|WP_019129855.1|2568426_2569014_-|hypothetical-protein
MDTIERIARRNRLRAEEVIRDSRLAEIWRSVGAEVRQVGSLRSGLLMKHRDIDFHIYSSPLRLEESFAAMAQLAADPAVGRIECRNLLATDEACVEWHATYRDRDGDEWQLDMIHIVRGSRYDGYFERVADRIAAALTPVTRRAILQLKYDTPDDVKIAGIEYYVAVLRDGVRTYDAFAEWRRTHPLTGIVEWMP
>NZ_AP019735.1|WP_141413098.1|2567007_2567325_-|hypothetical-protein
MAPFRLYSVRINENNITTDNVTLISPRHSGGRQNEYSNYFSLIIGNNGTGKSRLLCSIAKLFKQIYKDKNSTKLFGSKANFNTVPNKVIALTNSLSDHFPLDSSF
>NZ_AP019735.1|WP_141413097.1|2565873_2566869_-|AAA-family-ATPase
MDIFFEYYSESEISGYYRHVFDYLDFEPILKLQYRIPYLFKQSKHISKEFLFTNTRTPMSITGQINEVDETKTQLIDLYGQELADFFNNTEFSPDGYREILINFSAKNTKRYTEDKQQYNNNIAEYRILNILRKLNIVRSYEVKVYKKGGFEFSFGEASSGEANILSTLLALLPLLEDNCMVLIDEPEISLHPIWQAKYIELLNNIFKHFHGCHIIIASHSHLLVTDLPPDRSTVITLQNRKKNIISEIINESTFGWSAEDILLNVFGLPTSRNYYLSQVLSKGLELLADHSRPNSELNAVRRQIEEYFPLMKDNDPLKSIAEIIINTTLR
>NZ_AP019735.1|WP_141413096.1|2565253_2565877_-|hypothetical-protein
MSDYINNAYQLTSQETSLIKKEFSTHTDWNKKIFDQLKKNIVLHLRKEQDNKCCYCKHELGFDIKDVEIEHIVPKSTFSKFTFCCKNLALSCPGCNTKKGTKNVLNKPIKNYPRSGNAFKIIHAHYDSYPQHIQIDNKSVYIALSSKGSETITICELFRLNKVEDNMKKFNAEQQSILAWLTEEIRTSKPEEQAAFIREIKRRIRNE
>NZ_AP019735.1|WP_141413638.1|2575885_2578855_+|tetratricopeptide-repeat-protein
MIAALGCLWCGADASVLTSGGRTHFDRGRELYALGRWADAREEFAAVCGAVPQTESSLCVEADYYMAMCAMELKEAGAEARLAEFLRRNPESVHVNDVEFALASLLCTAGRYDEAQRAFGKVDYATLSPEHRQQYDIRMGYIRFQQGDYDDALRYFRRIPSPSEYSDHALYYISYIAYVRGDNAMARAGFTELSRSAAYGAVAPFYLLQIEFNEGNYRYVVTTGGSLIDRAAGERRTELERIVAEGWFHLGDYGRTEEFLDAYRRSGGEMGRNENYLLGYSLYRQARYDEARPCLQQVCGADDALTQNASYHLADCYLRGGDKQRAMQSFAMAANEAFDAAIAEDALFNYGKLQYELGGGLFNEAIHVLNRYIAQYPTSERAVQARELLIAAYYNSRNYEAAYTALKHYPSPDGNLRAALQKIAYFRGLEAYSRGDLDGAAQSLSESAAINVSPKYGALARFWLGEIAFARGDYAEAERRYKEYLHRAPRTEDEYAKAHYNLGYCYFDRGDMSNAYASFARFNQLYSAADRYKADALNREADARYSLRQFSAALATYEKAAAVGTNEKYYADFQRAVTLGILDRGPQKIEALQRIIAADRGDYVDDATYELGRTYIAAERYDDGAKVLSKFVEENPHSPFFTPALSDLGLAYLNLGQPELSRRCYERVVESAPGSATARDALQGIREIYVADGNVDGYFAYAEKAGVECDTSVMARDSLSFAAARKIYLSGDTAAAEKSLRSYLRNYPKGYYTDDALFYLSDCHLKAKQTDAAIETLSELAARPTNQYSARTLGTLSKLTSEAGRHAEAAKAYRALYDVVQTADERAAAATGYFRSVEAGGDDAATLAAAAEVETLPDAGTTAQREAKFACATILRRGGKQAEALPLYRELSREVKTAEGAESAYRVIEATLAGGDAAAAETLIFAFAEKGSPHAYWVAKAYIALGDIYAGRDDSFQARATYQSIVDGYSPADDGIVAEAKARIEKLKK
>NZ_AP019735.1|WP_141413104.1|2578857_2580756_+|hypothetical-protein
MKRVLILSAAVLFCGVPLRAQVTKQVEVTKTYVPEVSKAVKLPIVPDMTDTVRLRPEIDYTVTPSALATNLSTEPFRPATVTYWEFNRPRPLYLKVGAGAPLNSVLDLYASTQNPGTGYAVGYLNHTGDWAEIRNDFGVRPVSWRMHNRMGAAAGKYLGRRLLEGKLDLTNRVYHNYGFDGAEALCTRYGNDGAASYYPFTKVSNDRQHYDDAMLHVRIGDDFTDLSRFNFNVELRGGYFLNVLQMQPVYYDWGVDRDRYHELSGGGGIRLARAFGLHEFEFKADFDGAWRNMLGYGSTQLLFGLHYAYRHDKLRWSVGLDYVRDGAEQEKVVGSDLSDPHAVYKESQTEHENRFLPAASIAYDPADGKFMLYAELTGKVRRNDMRTLSRLNPYVNPASIVPNTEEHRVAGGIKGAAGHGRFSYNLYVGYTHEKNALQWVARFIPNNVRDERADVGYMSFYIPYAMTLKDLSLNAEFAWRPSSRFTFDGELHMHSFKGAENVYYNNNQPYTLAYGRPQLTARLRGEYRARKVSLEVEAQMQSVRHWTTYTSVNEKPSEPDSDSGLNLGRRVIGLYDFKVPVTVDLAARFNWFLSRKVTLFAEGRNLCDAKLYDWAYYRDYGVGFTAGVKLQF
>NZ_AP019735.1|WP_141413105.1|2580989_2584325_-|fimbrillin-family-protein
MKRFVQFLGAATLLLSFTQCSEDATTDSAPSVQGSVKLTASINETRTELSGNDVLWKSNDRLGLFCGTKFVNAPFTTAAGGTTSADFTGDPTDPSGSEAEVFYAYYPYSAHAVLEGSVVSGLSIPAVQTFATKSFATELCPMATSGADYSRLAFRTIGTVLKFQVTGQKNVTKIELTGNDGEALAGDYTIDFVGETPEMKFSGTETTLTLTCSEPVALNDASATEFYFVLPAGIEFTKGITVKVYTDDNAEPMVKEYASPLTTRPNKLVTVKAFTYSVPVTSIEEANEALSKGTSGVTITSTTDLTAPSTLEIPNAFGHGTSTSVEIEQPVSTDLTISEKTTSDKELPETLSVEMETTASLIVDTPNLTVSLEGTYTTVEATTAENTLIVAKNTVIETLTVKKGNVKIYGTVGEIVNEGTGKIIRCIDAQDEVERTLADTRCDHILIEKPAGTLDFGGGTTTKQVCVEASVTIANLIVSPEKEHPVMVSGDNVKLTLDGVKLVCNAAKTYAVNCLDGANPDVTLSNSEIIALGTDCRAVSVVNTRATSDTSYITFDNTQARTSQTAIGNREYTADEIKYFTSRVADGNYYPRGISVGSTGGKVNIALRNNSCIEGFFYGINIAGITEPVDVAIDDSRLDGRAALNVHGQKCIFRVNRSTLVGRNYFGGPTEDFATVVLDRAVATSHSNTVTVADSEIYSYNKPQTATNHQYSIDIRSLHNTVELKGSTRLIEVGSTEYPARLNFMVCYDNSTDNVINVDPGVTVSGKEGAKVLPATVWDGSSVYAPAADADGDYPIYEAAELKWIADQINSGNYLYLEAKGRYAQVYLMNDIDLNNKPWTPMGCQNHSYTLSGVDKCAFYGEFHGTGHTVSNLNVDIVADAKGFIGKTLGKEASIKELTLKNVAIPLNDDAEIQGKWVGALVGCMGGDTNVSDCHVENVTIHAPGMYRIGGLVGVWTNTSRQNATATVENCSVKDATLTAGYAIGGFMGTIQPQKPAAGYNTIRNCSVENISITHKDQYCWGDDPNYAAYYPETGHYCYSSAPFAGDVNNVNLEKCTVGGSCTIADADGHNTYMSATWTKLPYMGEVGGNACIDGVKVSADPTPAEGYFTK
>NZ_AP019735.1|WP_141413106.1|2584706_2585726_-|hypothetical-protein
MNNILKIALTLAVGIVLAGCYNDFDNPAPAKVYTDKDFTETGAEIISIKDLKAKFYEKWGHDANGLGRRVVIEDDVVIKGKVISSDAEGNVYKSLYIYDGEQAIELRLMNDNYVNYPLGQIVYVKAQGLSLASYRYMLSLGAAPALEPDGTFPNDTPSEHDFSASGNSNIPTTEMVQQYVYRGELDTITEADVTVVDKDNYKTVLNDDLLGCLIRFEGLRSSYTTVDSNTYPNYLENVNGVYTNKYYQDEGLPITWAYNYDNTKYYGSSLFTYETTPTSLESGSYVVRVSGYARFALKELPADNAMVNITAIYTKYSSRTGGFITYQLLVSSYKDIEEL
>NZ_AP019735.1|WP_026074781.1|2585829_2588610_-|TonB-dependent-receptor
MKIKHLLTLLLTMATLPALAQGSGIKGKVVSRGDRAAIEQVKITLTPGERQATSDAEGRFRFDDVASGDYTLTFEADDYEPLEIKVRVDKLTKDVRSIALVPVYTEAFDDSIFAEFDTETANDTQSLPSSLSSSKDVFNNIASYKFGEMRFNLRGYDSQYTNVYFNGIRLNDALTGYTPWSLWSGLNDATRNQENTTGLQAADYGLGGIGGTTNINATASQIRKGLRVSLVNGNSMYRFRAMVSYASGLLDNGWSYAFSVSTRQGGNDWVNGIYYNCFGYYGSVEKRFNERNRLAFTILGAPTERGAQQASTQEVYDLVGNNYYNPNWGYQDGKKRNARVRNNHEPLMVVNYTNTPDDRTKIDAAASFRFGTNGYSALTWKGGADPRPDYYRNLPSYYMANNQFSNAAQIAELWRTSYDTRQINWDRLYDTNYRGEIDEGTYGAGHRSNYMIEERHTDQLDLNLTAQIARTFRDNSRLVAGILYRWNRTEYYDKVKDLLGGDYWVDIDKFAERDFVGEEEKQNDLHYYYEHGHARRVEEGDKFGYDYYANIRQAKLWAMYNFNIAGLDGTIGGEVGQVTMWRDGRYMKGTYPSNSFGNSEALDYFTYQAKLNLAYRFSAAHSVEFNAVALQNAPTFQNSFISPRTRNEVTPGLKAEKIWGVDASYNLSYRGIKARLSGYYTMIHDQTDIISYYDDLQSTFVNFAISGIDKKFFGLEFGMTVPLYMGLSLNGAVSVGQYTYDSNPTFVQLADNSSKILSDVDSSIVYWKDMRVESTPQTAVNVGLSYRSDNNWFASADLNFYDNNYLSMNPLFRTDEVLRAGATNAETAEMIRTMRAQEKFDSAFVLNASLGKNWYIKRNYTLGFSLEVKNILNNQDIKTGGYEQMRLNKIKADESNTSLVTSYERFDPKYFYMFGTTYYLNVYFRF
>NZ_AP019735.1|WP_141413107.1|2588621_2589662_-|endonuclease/exonuclease/phosphatase-family-protein
MRKKLIITAVLASVMVMCFAQKPHKIMFYNMENFFDTIDDPETNDEEFLPDGAKRWNTAKYDKKLRNMERVLFDIAAIDRNYPAVIGVSEIENRSILEDIASTRKLLPARYAICHYDSPDLRGVDVAFLYRPDVFKLEGSADIPVRIASLPNWRTRGIVTMWGTIDDEPFLFMVAHWPSRLGGQAASAFKRNAAAEQMRAIADSVLKVNPATKIVAMGDFNDDPTDESVEVHLGAKAKIKELQPGDFYTPFADMLKAGLGTLAYRDAWNLFDNIVVSENLATGSAGKLKLIKDPYKKTKFYGNIFKPSYLIQQEGQYKGYPLRTFVGNNFQGGFSDHLPVFIYIAK
>NZ_AP019735.1|WP_162502297.1|2589753_2590974_-|DNA/RNA-non-specific-endonuclease
MQTHLLRQWLRLAVAAVAVFFAACGDSDGDAATARVESCELERSSIVGGQIASGEETASLRVIVEVSGSGQLNYTATITSGDWLSLSARDFSAAGRQRQGTVDSGENLLFFYYKANASAQSRIATFTIAFDDGSAPYDFELTQLAPNATDNPYDTPKQWPELPAGKEEADYIYAAHYAKMNLKTVRNYSLCFDKKLRVAHWVAYPLHASYIGSLDRSEAWAPDPKIPQQYQPALWLGGYQNGNVYNRGHQIPSKDRTTVEEMNKQTFYASNMTPQRGQFNQNMWAALEAKVRSYVCPDTLYVVTGCYFANLDESTKDKAGNVCPVPTNYFKVLLRTRDGATGKRIADCKASELKAIGFWVANENGQQLGRQLCRSVAEIEKETGFTFFPDADTSVKAQNSPEQWGF
>NZ_AP019735.1|WP_141413109.1|2591033_2594783_-|BACON-domain-containing-protein
MKQLNIWKTSFYTMLAIAAGAFTACVDDDVDKQAPTLELSEEAVAFTGTATEDATVTVRSNRQWTVAYEDEETQKEWMYFKVSGNEVSEGIYNGDGTVKITVGESAQPHMGRLIFTLSNSYGELYRKYLTVTQGNYVPPTVGAVGKLVEYILGNSDLSGAVGSDKAMPLQYSESTIEAVILANDAAGNNNRKLYVGDNNGLERSAIVLYGADFAMANDPVTKYPAGRKVTLNLENAKYYAFNNVRQLTDVVVTVGDEEVELVVPSLSVEKFNTGDYQAQYVKLNNMTPAQSFVGKPWTATESQSVTLNDASGKTLTVYMNKAQFATGFADMYVADKTGTIYGVAETYRENAQLIPTKKTDIAALSTDQGGGTDPDPTPGDAIYYESFGTADVSDKPLIADYTGWAKTGSGAGEVSYTGEGNMSIRTSGKLSAGYDGASGKNKAFFGTNNPALIINKIKLDGAQDLQLTFGAQYSKTIDYDAGLYDNEFKPEKFHLALSADGTSWTTVEYTYAQADEFWVFATSKFKLKNKAAYLYVKYAVDEASVFAIDDVTLAEGEGGTEVDLGEGGEEPEPTPGEAITVNELYRLAETVTGKDKLVIDAENNRTLEAVVVTDVDGGNVSANNLMVMTEGATQAKNGILLFSSGQYTNPKDPAFPFKSGDKVRFTLVKGLAKVANFSNCYEVTCESSDAATWLTAEVIGKAQLTPVPLTSIDNLIDYQGMLVTVKNVTSPATAGNWAVGTTTFKVGSSDLTVYVTQDAAGFAGKQYAASKTGDLTGYVSLYKGAVQLCPRNMTDAAAFAEGGTDPEPADPAHIVLDFSVGASIFTPALPDKEAQSKTGSYLFDGNYAFNISASNIFYWFQNPYEDSPGYGTKSLFIGKAGSYIELPAIADKALTKVIISAAKGAGAYSIAITDAAGTPVQGGQAQEVTKQEGGEYTYTLSNTANATAYRIAVTTAGNAQLAKIELFYGEGGGSTPVQPTLSVNPTSLSFAAKDQAKTIACTVANADGYTVGASSSDPANFAASAAGTTVTVTPTENTGSARNATVTVYLTNDGGATKVAAKTVAVTQAAAGGSEPAGDTYDKITKVAELVNGMTGFIGCEPGGTYGLQLVTGFAAYGQGFTAAYTYDETKKTLSLTSGNYTAIEFTFEAVADGFNIKQGDKYLIGTGIIDNGKPKQGLVLADAPAQPWTFTEDASGVIATTSASGTVDGQAFNYPAIYMMCANSASSRFLRPYVQASYGKGFCFFKKN
>NZ_AP019735.1|WP_162851478.1|2595033_2595501_-|DUF4293-family-protein
MMIQRIQTLYLLLAAGLVACAAFLPLASFASGGEEFRLYAFGLRTADGETVQSTLYMGILLALALVLPLTTIFLFKRRMLQFRLGVVEMILLLGAQIVMGIYYFLSYRLFSSFEFHAQSVKLPLVLPLIAMIFTYLAVRAIFRDELMIRSMDRIR
>NZ_AP019735.1|WP_019129839.1|2595511_2596471_-|glycosyltransferase-family-2-protein
MEKRLDISVVVPLYNEEESLPELTAWIDRVARENGLSYEIVFVDDGSTDGSWETLERLKEHYPALRAIGFARNYGKSAALYCGFAAAEGDVVFTMDADLQDSPDEIPDMRRMILEEGYDMVSGWKLKRHDPIGKRWPSKFFNWTARTVSGIKLHDFNCGLKAYRRKVVKSIEVYGEMHRYIPILAKEAGFRRIGEKVVCHRARKYGSSKFGMERMVKGYLDLITVSFLSHFGRSPMYFFGGLGTLMFLLGGCSTIWIIAAKLYKQAHGLPLRAVTEQPLFYLSMLLVILGVQFFLAGFLGELIDRNASDRNKYLIDKNI

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Crispr_ID: NZ_AP019735_16

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_16

3031984-3032081

Orphan

Consensus_repeat	Method
AGTATTTAAGGCGAAGCCAAAGAT	CRISPRCasFinder

1 spacers

DEDDh

The CRISPR arrays of NZ_AP019735_16

>merge|NZ_AP019735|16|3031984-3032081|CRISPRCasFinder
AGTATTTAAGGCGAAGCCAAAGATACGAAAAGTCGAGCGCAGAAGCAAGCGTTAGCTTGATTATGCCGAGACAAAGTATCTAAGGCGAAGCCAAAGAT

>NZ_AP019735|16|16|3031984-3032081|CRISPRCasFinder
AGTATTTAAGGCGAAGCCAAAGAT	ACGAAAAGTCGAGCGCAGAAGCAAGCGTTAGCTTGATTATGCCGAGACAA
AGTATCTAAGGCGAAGCCAAAGAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141413356.1\|3026568_3027540_-\|flotillin-like-protein-FloA	unknown	unknown	gnl\|CDD\|378816
NZ_AP019735.1\|WP_141413354.1\|3024693_3025461_+\|CDGSH-iron-sulfur-domain-containing-protein	unknown	unknown	gnl\|CDD\|378163
NZ_AP019735.1\|WP_141413366.1\|3043097_3043493_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_026074706.1\|3022319_3022814_-\|3'-5'-exonuclease	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|99834
NZ_AP019735.1\|WP_141413355.1\|3025547_3026540_-\|4Fe-4S-binding-protein	unknown	unknown	gnl\|CDD\|224516
NZ_AP019735.1\|WP_141413361.1\|3033495_3034332_+\|metal-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224033
NZ_AP019735.1\|WP_141413365.1\|3040439_3042719_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
NZ_AP019735.1\|WP_019129438.1\|3035847_3037074_+\|bifunctional-3,4-dihydroxy-2-butanone-4-phosphate-synthase/GTP-cyclohydrolase-II	unknown	unknown	gnl\|CDD\|181774
NZ_AP019735.1\|WP_141413659.1\|3037469_3038453_+\|methionyl-tRNA-formyltransferase	unknown	unknown	gnl\|CDD\|234567
NZ_AP019735.1\|WP_141413359.1\|3031065_3031908_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413658.1\|3029623_3031030_-\|TrkH-family-potassium-uptake-protein	unknown	unknown	gnl\|CDD\|182698
NZ_AP019735.1\|WP_141413358.1\|3028088_3029636_-\|SPOR-domain-containing-protein	unknown	unknown	gnl\|CDD\|236462
NZ_AP019735.1\|WP_019129434.1\|3039862_3040027_-\|rubredoxin	unknown	unknown	gnl\|CDD\|238372
NZ_AP019735.1\|WP_141413362.1\|3037078_3037465_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319905
NZ_AP019735.1\|WP_141413353.1\|3022916_3024377_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|370579
NZ_AP019735.1\|WP_141413357.1\|3027566_3028043_-\|serine-protease	unknown	unknown	gnl\|CDD\|223961
NZ_AP019735.1\|WP_019129439.1\|3034328_3035831_+\|YjgP/YjgQ-family-permease	unknown	unknown	gnl\|CDD\|367632
NZ_AP019735.1\|WP_141413364.1\|3039288_3039672_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413363.1\|3038419_3038965_-\|FUSC-family-protein	unknown	unknown	gnl\|CDD\|226614
NZ_AP019735.1\|WP_141413352.1\|3020905_3022168_+\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|238624

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_026074706.1\|3022319_3022814_-\|3'-5'-exonuclease	gnl\|CDD\|99834	cd06130, DNA_pol_III_epsilon_like, an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with similarity to the epsilon subunit of DNA polymerase III. This subfamily is composed of uncharacterized bacterial proteins with similarity to the epsilon subunit of DNA polymerase III (Pol III), a multisubunit polymerase which is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. The Pol III holoenzyme is a complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.	4.34294e-78
NZ_AP019735.1\|WP_141413354.1\|3024693_3025461_+\|CDGSH-iron-sulfur-domain-containing-protein	gnl\|CDD\|378163	pfam09360, zf-CDGSH, Iron-binding zinc finger CDGSH type. The CDGSH-type zinc finger domain binds iron rather than zinc as a redox-active pH-labile 2Fe-2S cluster. The conserved sequence C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H is a defining feature of this family. The domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates, MitoNEET_N, pfam10660. The domain forms a uniquely folded homo-dimer and spans the outer mitochondrial membrane, orienting the iron-binding residues towards the cytoplasm.	2.19081e-15
NZ_AP019735.1\|WP_141413362.1\|3037078_3037465_+\|VOC-family-protein	gnl\|CDD\|319905	cd07241, VOC_BsYyaH, vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	2.6547e-54
NZ_AP019735.1\|WP_141413355.1\|3025547_3026540_-\|4Fe-4S-binding-protein	gnl\|CDD\|224516	COG1600, COG1600, Uncharacterized Fe-S protein [Energy production and conversion].	7.95582e-17
NZ_AP019735.1\|WP_141413361.1\|3033495_3034332_+\|metal-ABC-transporter-permease	gnl\|CDD\|224033	COG1108, ZnuB, ABC-type Mn2+/Zn2+ transport systems, permease components [Inorganic ion transport and metabolism].	1.10842e-57
NZ_AP019735.1\|WP_141413365.1\|3040439_3042719_+\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	4.34127e-44
NZ_AP019735.1\|WP_019129438.1\|3035847_3037074_+\|bifunctional-3,4-dihydroxy-2-butanone-4-phosphate-synthase/GTP-cyclohydrolase-II	gnl\|CDD\|181774	PRK09311, PRK09311, bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II.	0
NZ_AP019735.1\|WP_141413659.1\|3037469_3038453_+\|methionyl-tRNA-formyltransferase	gnl\|CDD\|234567	PRK00005, fmt, methionyl-tRNA formyltransferase; Reviewed.	2.83137e-139
NZ_AP019735.1\|WP_141413356.1\|3026568_3027540_-\|flotillin-like-protein-FloA	gnl\|CDD\|378816	pfam12127, YdfA_immunity, SigmaW regulon antibacterial. This protein is found in bacteria. Proteins in this family are about 330 amino acids in length. The operon from which this protein is derived confers immunity for the host species to a broad range of antibacterial compounds, unlike the specific immunity proteins that are linked to and co-regulated with their antibiotic-synthesis proteins.	0
NZ_AP019735.1\|WP_141413658.1\|3029623_3031030_-\|TrkH-family-potassium-uptake-protein	gnl\|CDD\|182698	PRK10750, PRK10750, Trk system potassium transporter TrkH.	5.66324e-77
NZ_AP019735.1\|WP_141413357.1\|3027566_3028043_-\|serine-protease	gnl\|CDD\|223961	COG1030, NfeD, Membrane-bound serine protease (ClpP class) [Posttranslational modification, protein turnover, chaperones].	2.31334e-09
NZ_AP019735.1\|WP_141413358.1\|3028088_3029636_-\|SPOR-domain-containing-protein	gnl\|CDD\|236462	PRK09303, PRK09303, histidine kinase.	0.00548045
NZ_AP019735.1\|WP_019129434.1\|3039862_3040027_-\|rubredoxin	gnl\|CDD\|238372	cd00730, rubredoxin, Rubredoxin; nonheme iron binding domains containing a [Fe(SCys)4] center. Rubredoxins are small nonheme iron proteins. The iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc. They are believed to be involved in electron transfer.	2.55267e-23
NZ_AP019735.1\|WP_141413353.1\|3022916_3024377_-\|hypothetical-protein	gnl\|CDD\|370579	pfam09603, Fib_succ_major, Fibrobacter succinogenes major domain (Fib_succ_major). This domain of about 175 to 200 amino acids is found, in from one to five copies, in over 50 proteins in Fibrobacter succinogenes S85, an obligate anaerobe of the rumen. Many members of this family have an apparent lipoprotein signal sequence. Conserved cysteine residues, suggestive of disulfide bond formation, are also consistent with an extracytoplasmic location for this domain. This domain can also be found in small numbers of proteins in Chlorobium tepidum and Bacteroides thetaiotaomicron.	0.00016144
NZ_AP019735.1\|WP_019129439.1\|3034328_3035831_+\|YjgP/YjgQ-family-permease	gnl\|CDD\|367632	pfam03739, YjgP_YjgQ, Predicted permease YjgP/YjgQ family. Members of this family are predicted integral membrane proteins of unknown function. They are about 350 amino acids long and contain about 6 transmembrane regions. They are predicted to be permeases although there is no verification of this.	7.26053e-48
NZ_AP019735.1\|WP_141413363.1\|3038419_3038965_-\|FUSC-family-protein	gnl\|CDD\|226614	COG4129, COG4129, Predicted membrane protein [Function unknown].	1.54772e-09
NZ_AP019735.1\|WP_141413352.1\|3020905_3022168_+\|amidohydrolase-family-protein	gnl\|CDD\|238624	cd01299, Met_dep_hydrolase_A, Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.	2.02231e-109

>NZ_AP019735.1|WP_141413359.1|3031065_3031908_-|hypothetical-protein
MKGIRKRVLVSFLSVVVLLFFAGLVSLFELRRVSSDTEEILRASERNLGLAKDMLDAAARQNKAVVHSIVFRQRDYDTVLMGSIAEMARTLEVVRREAVEQAYLDTLSVSAMNVQRLTQEFLRLQAQRMTSEVSGRLELRGGKDSLSMKSVEMDFDGARWYAEAYSKAYDKLTGSIKNYMISTQSSLAPRTEQLKRNAYRAVTPVLISLLVMIAIVLMLYYFVSAYLVRPVLAMNKSLGDYLRFGLPFRIKAEVKDEVAELKDRIDDVIQLARKTKPEQR
>NZ_AP019735.1|WP_141413658.1|3029623_3031030_-|TrkH-family-potassium-uptake-protein
MLVVALFMLLSAGVSLVSHTDSGYYPLLLSALLTALLGAFPLIFVDRTEQLSSKEGYCIVVGSWIVASVVGMFPYLMWGGEFSLVNAWFESVSGYTTTGASILKDVEALPRGLLFWRSCSTWLGGVGVVMFALLILPSLGTNKALLTNVELSSMAKHNYHYKASMIAQILLFIYLGLTFCSTLALKLAGMNWFDALTQAMSAVATSGFSTKNASIGYFDSVAVESILIVTMLLASIHFGVLFATLTGRRNNIFHSEVTRWYLSIVAVVTVVVAGSLYFGGVYDTVAGALRYAAFQVVSLISTAGFATADTTVWPATAIVLLISVSIVCGCAGSTTGGIKTDRFLLAIKTLRLRFSLQQHPNAVVRVRIDGNVLDDKIASTAVVFIVAYFLALLAGTVVGTMCGVDMETSFSSSVACMGNVGPGFGMVGSLGNYSDLPAVMKFSNTMLMLLGRLEIFGLVQLFFLKWWR
>NZ_AP019735.1|WP_141413358.1|3028088_3029636_-|SPOR-domain-containing-protein
MVEMMRKGFFLLAVLVAVGAAEASAQEVTARIAGLEGNAEYMEMLREEASLQAREDSVTMVVNRVRRQLRDDPAQRAVYSAEILRCEEQLFSIRTERGRLTDRINTVEQDWVLANLDLSSPSTTTAGRAAGTPLPDSLQTADLVHNAYFREQLPQADYRALLSAQRRERTAFDLAAACAANYEAIEELKISYDTITAETPAAVLYERYRTLQSLNRSLCDSLQRVWGAVYDNKNYAYAYVLDRLGRDDLLAKTEEQLAGVRQQMASERGRYYADELTDYLLQKRALVDVETELAGALGLTAARDSLARAAAGLRIVDYRLPKLFIEERMFLEYEPIGFVTPAKYNASHHIPEVKVYERGTIYRILLGTYTNRTNGGYLFKGAYPLGYEKVEGKYAYYAGGYRTLDEARAAQEQMKKKGFRRPEIVVWNDGERTNLADAAEQGNAPMFRVEIGGLDGFPEELRAAVQAVAGESEISRAGRHFIVGPLADKAVADKVAEAVMQQNASLEVKIAEIVE
>NZ_AP019735.1|WP_141413357.1|3027566_3028043_-|serine-protease
MWLIILLILLGVLFLVAELVLLPGVSLGALFALVCYGSAIYTAFADYGPFTGGIVVLIILALSFVATVLSLRSKTWQRFSLKQKIESSSMPLPDNEVKAGDRGVAVSRLAPMGKVEIGGRIYEAKSTDVYIDQRSTVEVVGFENFNVVVRKVADEPSV
>NZ_AP019735.1|WP_141413356.1|3026568_3027540_-|flotillin-like-protein-FloA
MDQTGIIAITVFAGLVALWLIFYFIPVGLWFSALVSGVRISLLQLILMRWRKVPPSVIVSSMIESTKAGLSLDPNELEAHFLAGGNVPNVVHALVSAQKANIQLDFKMATAIDLAGRDVFEAVQMSVNPKVINTPPVAAVAKDGIQLIAKARVTVRANIKQLVGGAGEETVLARVGEGIVSSIGSAVSHKVVLENPDSISRVVLDKGLDAGTAFEILSIDIADIDVGKNIGAQLQMDQAQADKNIAQAKAEERRAMAVALEQENRAKAQDARAKVILAEAEVPLAMAEAFRNGNLGIMDYYKMKNVMADTAMREAISKPVDKK
>NZ_AP019735.1|WP_141413355.1|3025547_3026540_-|4Fe-4S-binding-protein
MSVEELTSALETYIRESPRNYVDEAMALVPSDVGQRLYDTPLVRVGSADDPEWEEMKRPEAVGHLFRTPKEWLPEAVSVVSYFAPFSDFVVEGNKRDAVDVGNGWLYARVEGQAFLTEVNRFLERWFRERGYRAVAPYASAGFRYVFEAGTNAEIADKSLSFTSNWSERHVAYVCGLGTFSLSKGLITERGVSGRFGSVVTDAPLPVTKRRYTGLYDYCSMCGACVRNCPAQAISLEHGKSHHLCCSYFDTLREKYALRFGCGKCQVNVPCERENPQKRISSVFELHFVRKEASPYPDVKTECSFGSCALREPPKVNRQRRSGGLQHGTA
>NZ_AP019735.1|WP_141413354.1|3024693_3025461_+|CDGSH-iron-sulfur-domain-containing-protein
MKKIDIEKGSKRADARFRITVEETGPYLIYGQPPLAQQFIMPDAEGESWYFQQGAHFPTDDEPTALCRCGASKNKPYCDGAHVHAAWDPRLTADDAPLLDNVELTEGETLSMTDNPKYCVFARFCDAKGQAWNLVGQPENDEARELAIREASMCPSGRLMAWDNETGTPYEFRFEPSLGLIEDVAIGASSGLWVRGGIPVSRESGETYEIRNRVVLCRCGASHNKPYCDGTHASIRFNDRLEGTPEGETLPEKVY
>NZ_AP019735.1|WP_141413353.1|3022916_3024377_-|hypothetical-protein
MKNLTVKIFVGLFVVATVLLQSCKKDSETYSFLLNERGAFVEEPGGTTSLGFTAINISSVTPTTVPQGWSVTVDMNERRISVTAPTTFPDDPKTLADGEEEEEENTNVRFGTVYLTGRSSGGSSVSTSLYVSLAETVDLTGQPSNCYIINKSNARYCIDVTRKGEDTEATMSPASVAILWETPYKVIEFPKLVDGKAYFYHAIGTDDDEKEFFNHGNALLGAFDAAGNLLWSWHLWCAEFDPADEQVELGGEVMMKRNLGAGVVSGTSEEDILASYGVYYQWGRKDPFVGPRYYNMADSADAQVYDSQNLRVYPEYAATDAERGSAGYASAHAMTFITGTKESGYNWLQTADVSLWGTEKNNNDPCPRGWKVPSKEVFAALHIKDVISPELEKNYGFTLSDGTNEAFFPGAGRRSFYTGALTNMNDNEVRPTPWTGYYWSSTGEGKEAYAMDFSFDINGTRAGSSFQGAALQYAAGGMQVRCVKMR
>NZ_AP019735.1|WP_026074706.1|3022319_3022814_-|3'-5'-exonuclease
MRDFAAIDFETANGQRTSVCSVGVVVVRGGRPSESIYRLIRPYPNYYSAFTTAIHGLTRSDTENAPSFPDVWGEIAPRIEGLPLVAHNSPFDEGCLRAVHAHYGLPYPDYRFLCTLSASRRRIKGLPNYQLHTVSAACGYLLERHHHALADAEACAEIALRLFG
>NZ_AP019735.1|WP_141413352.1|3020905_3022168_+|amidohydrolase-family-protein
MDSQLLLNNVEIFNGKDARTFSGNLLIRNNRIETISAAPIETPSERPVTVIDGKGRFLMPGLIDAHWHAYLCCNTMTDLLAGDPSYTHLMAGREAAETLQRGFTAIRDAGGPVFGLKRAIDSGTLRGPRIYPSGAMISQTSGHGDFRMIYEHAHGGCGCEMAHVEQIGASKIADGADAVTAAVRENLRQGASQIKLMAGGGAASLYDPLDVTEFFEEELRAAVRAAEDWGTYVMVHVYNPRGIARALKAGVRSIEHGHLIDEPTMALLAESGAWLSMQAFAVEDNTYPSPVQQAKHLQICNGTDRTYRLAKKHGVKLAWGTDLLFDPANTKNQNHGIVKLQKWFTNFEILRMVTCDNARLLALSGARNPYPGNLGVIEEGALADLLVIEGNPLERIEVLENPHDNLRVIVKDGVVCKNTL
>NZ_AP019735.1|WP_141413361.1|3033495_3034332_+|metal-ABC-transporter-permease
MDFFYDIARYAYLHNALAACILSGIACGIMGTYVVCRRTVFLAGGITHASFGGLGIAFYLGLNPIAGALVFAVLSALGIEWAGNRGRIREDSAIGIIWSVGMALGVLFMSLRPGYTSGDLAGYLFGSIVTVSGADVAALAALTALVVAGAALWLRPVMYVAFDREFAHSQGIATQTVSYLMAALTAVTIVLAIRVMGIVLLISLMTVPAVTMNTLSKSFRTIAFGSAVLGALGGVAGLAVSYQWELPSGVAIIFVLTASLIVAKLLSLRHESAKTRRG
>NZ_AP019735.1|WP_019129439.1|3034328_3035831_+|YjgP/YjgQ-family-permease
MKTIHKLVLKSYLGPMFLTFFIVMFVLMMNFIWRYIDELVGKGLDAGVIIELMSYAMANMIPMGLPLAMLLAAIMTLGNLGENYELLAMKSAGMSLPKILKPLIIVVGIIAIGSFFVVNNLVPYANKKMLSILYDIRQQKQVIEFQDGLFFNGIEDMSIRVGKQDPKTHLLRDVLIYDNRNINGNMTTTVADSGYIRLSDDKKYLLVTLFNGETYEQTRNYQWYSKSALRHHIFEKQDGVIPMEGFGFERSDANFSNQSTTKNIAQLDRAIDSLELTVNSATTRSYEPLLREQIFANDNQVLPLPDSARIDKSGFRDALIADSIARLGLRDRDKVWGIARANAKNSRGLFSFDESTAKEALNQLYRSKIEWHRKISLPISIMIFFLIGAPLGAIIRKGGLGTPIVISVIFFVIYYIISISGEKAAREGNWEAFYGMWLSSFILAPIAVYLTYKATNDSVLLDVDWYTGRIKYYKEKWGIHTPKWMSALAGRFKRKPEENK
>NZ_AP019735.1|WP_019129438.1|3035847_3037074_+|bifunctional-3,4-dihydroxy-2-butanone-4-phosphate-synthase/GTP-cyclohydrolase-II
MAKNAIFNTVEEAIEDFREGRIVIVVDDEDRENEGDFIVAAEKITPEIVNFMLSNGRGVLCAPLSESRCEELELNMMEENNTSLLGTPFTVTVDLLGQGCTTGVSIHDRAATIRALADPATRPSDLGRPGHVNPLRAREKGVLRRPGHTEAAVDLARLAGLQPCGALIEIMNEDGSMARLPQLLEVAKKFDLKIVSIADLIAYRLREESIIERGVTVDMPTKWGMFRLTPFRQKSNGLEHVALTKGEWTEEEPVLIRMHSSCVTGDIFGSYRCDCGEQLHEAMSMIEREGKGAIVYLNQEGRGIGLCNKIKAYQLQDEGLDTAEANLRLGFRVDERDYGVGASIIRELGIKHMRLMTNNPLKRAGLEGYGLHIDEIVPIVIAPNKYNEHYLETKEVRMGHTLGLFKKK
>NZ_AP019735.1|WP_141413362.1|3037078_3037465_+|VOC-family-protein
MRLHHLALWSRRIELLRDFYTTYFDGHAGEKYENPAKGFESYFVTFADGVSLELMRRTDVTAPDAAQHLGLAHFAFGCESRAEVDRLTERLRADGHPVLSEPRTTGDGYYESAVGDPDGNLVELVYKA
>NZ_AP019735.1|WP_141413659.1|3037469_3038453_+|methionyl-tRNA-formyltransferase
MNPKTLRIVFMGTPEFAVPSLRRLVAEGYNVVGAVTVPDKPAGRGRHLRESDVKIAARELGVPVLQPEKFRDPAFLDALQALQPDLGIVIAFKMLPEVVWAMPRLGTFNLHASLLPEYRGAAPINWAIINGERETGITTFLLNHEIDKGAILAQERVAIAPEDNVGTLYERLMLLGAELVTATVDRIAAGDCTPAEQMHFDESRLHPAPKIFKEDCRINWRQPGERIVNLVRGLSPYPAAWTPIFKKGEPSDTAKIFAVHFEPGGVVQRPGTVETDKRTYLAVACADGRIVVDELQIAGKRRMSARDLLPGMRDLSDYSFGEEAAEA
>NZ_AP019735.1|WP_141413363.1|3038419_3038965_-|FUSC-family-protein
MITPWEILHRVQPLEVIAKAVAVTLAYLLGFAITSHFHEASSLTGAMLACVSAIVVQQQPDIRHAVQQGWLRVLGTFIGAVVAYVYLVNFRFSPAGMVVAVVLEEVICMMFKVPDNGKMATITLIIVLIVSERSPDLSPLANGLLRFSEATVGAVVGIAAVWPVDRYRRWRQASAASSPKE
>NZ_AP019735.1|WP_141413364.1|3039288_3039672_-|hypothetical-protein
MKMTELEKKEIERIQAKIMNTAAIILGCAGIIFVMWIYCIKGPDIDRSLREHAKYTTAYISGIAGRPGRVSVFLIYKHDGKIYKRGVGYYPRIETFSMKPPREGDSCIVAYDSLNPRYCTIYKDFRR
>NZ_AP019735.1|WP_019129434.1|3039862_3040027_-|rubredoxin
MKKYRCTVCEWIYDPAVGDPDGGIAAGTAFEDIPEDWVCPLCGVGKDQFEPVEE
>NZ_AP019735.1|WP_141413365.1|3040439_3042719_+|TonB-dependent-receptor
MHRFRLILLPLCLFATATAIGQTVTGRIVDERQQPVAGVAVVMQTPDSVYVDAVASDLEGRFAIASGVRPYRLLFQHLSYDPLTVERSGDDAGTVTLTEATNLVDEVVVRGERPLVKVEQGRLSYDLQVAAQGKIAANAYEALTKLPGVSERDGALTLAGAAGVTVILNGKPSTMTAEQLAALLKSTPVEQVEKVEVLYAAPPQYHIRGAAINVVLRRRFGRSFSGQVNGTYEGGYYHSWGTGASAVYSTPTLSVDALYRVGEARSMRKLPLTSQHTVGSDTFDIRQEQRLADDNLTHNLRTGLSWKTSEKSHIDLAYTASFTPSGKGDISATGNYVASDSHIRDDAAMHNLALSASTGFGMQIGADYTHYNTTSRQEMSLLPADGAPSSFRTDAGQCIDRLSLSLDQSHDLGRQWTLDYGARFVYVRDNDYQYYTSEEAMSDRDTDLRLDEYTYDLYAGTSRNFASGVSFSASLTGEYYRRNGYDRWAFFPQASLSWMASADHILQAEFSSDKSYPSFWDMSGAVTYLDGYAEVHGTPGLRPSSNYGLTLTYVLKQKYIFQLFGNHRVDAFTQSAYLSPDRPALIYQTLNWDYMSSFGALAVVPLRIGERFTSRITLSGFDYLLRNRDFYGMDYKRSKWVGYAALDNTLRLSRKPDLAFEFGGYYQSEAIQCTYDIGASWRLDAGVKWTFAAGKAELSVKGNDLFDSMTPVSEVDFGEQRLRMGNDFHTRNVTVNFVYRFGGYKDRERKKVDTSRFGH
>NZ_AP019735.1|WP_141413366.1|3043097_3043493_+|hypothetical-protein
MKQFITLICAGLLMSSCATIFCGSKTKVTFDGEISEKATLTIDGMKHTNVTFPYTTKIRRSFDETVVKIESPNYTAEPIIINKSFNAVSVINLLNILGWGIDAATGAITKPEFKFYQIDFQPKETTAPNQK

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Crispr_ID: NZ_AP019735_17

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP019735_17

3100440-3100557

Orphan

Consensus_repeat	Method
CGGCAGAATCGAACATGCGTTTGCTTCTGCGCTCGACTTTTCGTA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP019735_17

>merge|NZ_AP019735|17|3100440-3100557|CRISPRCasFinder
CGGCAGAATCGAACATGCGTTTGCTTCTGCGCTCGACTTTTCGTACTTTGGCTGCGCCTTAGATACTCCGTCTCGGCAGAATCAAACATGCGTTTGCTTCTGCGCTCGACTTTTCGTA

>NZ_AP019735|17|17|3100440-3100557|CRISPRCasFinder
CGGCAGAATCGAACATGCGTTTGCTTCTGCGCTCGACTTTTCGTA	CTTTGGCTGCGCCTTAGATACTCCGTCT
CGGCAGAATCAAACATGCGTTTGCTTCTGCGCTCGACTTTTCGTA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP019735.1\|WP_141413403.1\|3104046_3105189_-\|galactose-1-epimerase	unknown	unknown	gnl\|CDD\|185696
NZ_AP019735.1\|WP_141413394.1\|3092753_3093212_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378971
NZ_AP019735.1\|WP_019129386.1\|3093897_3094788_+\|zinc-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|238500
NZ_AP019735.1\|WP_019129373.1\|3107257_3108172_-\|mechanosensitive-ion-channel-family-protein	unknown	unknown	gnl\|CDD\|223740
NZ_AP019735.1\|WP_141413405.1\|3109486_3110263_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_019129372.1\|3108258_3109482_+\|phosphoserine-phosphatase-SerB	unknown	unknown	gnl\|CDD\|319803
NZ_AP019735.1\|WP_141413392.1\|3090017_3090464_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_026074695.1\|3105525_3105996_-\|methylglyoxal-synthase	unknown	unknown	gnl\|CDD\|179969
NZ_AP019735.1\|WP_141413400.1\|3100673_3101960_+\|DUF21-domain-containing-protein	unknown	unknown	gnl\|CDD\|224173
NZ_AP019735.1\|WP_026074694.1\|3106266_3106674_-\|DUF5606-domain-containg-protein	unknown	unknown	gnl\|CDD\|375774
NZ_AP019735.1\|WP_019129383.1\|3097081_3097372_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413401.1\|3101946_3102972_+\|tRNA-dihydrouridine-synthase-DusB	unknown	unknown	gnl\|CDD\|129820
NZ_AP019735.1\|WP_141413398.1\|3098507_3100286_-\|arginine--tRNA-ligase	unknown	unknown	gnl\|CDD\|223097
NZ_AP019735.1\|WP_141413404.1\|3106758_3107241_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP019735.1\|WP_141413402.1\|3102977_3104036_-\|winged-helix-DNA-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|377630
NZ_AP019735.1\|WP_141413397.1\|3097556_3098360_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|143586
NZ_AP019735.1\|WP_019129388.1\|3090477_3090864_+\|HIT-family-protein	unknown	unknown	gnl\|CDD\|223611
NZ_AP019735.1\|WP_141413395.1\|3094780_3095530_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213202
NZ_AP019735.1\|WP_141413396.1\|3095526_3096900_-\|aldehyde-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|143454
NZ_AP019735.1\|WP_141413391.1\|3087797_3090005_+\|RelA/SpoT-family-protein	unknown	unknown	gnl\|CDD\|223394

Protein	Function_ID	Function_description	E-value
NZ_AP019735.1\|WP_019129388.1\|3090477_3090864_+\|HIT-family-protein	gnl\|CDD\|223611	COG0537, Hit, Diadenosine tetraphosphate (Ap4A) hydrolase and other HIT family hydrolases [Nucleotide transport and metabolism / Carbohydrate transport and metabolism / General function prediction only].	4.71302e-35
NZ_AP019735.1\|WP_141413394.1\|3092753_3093212_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378971	pfam12844, HTH_19, Helix-turn-helix domain. Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.	4.99424e-10
NZ_AP019735.1\|WP_019129386.1\|3093897_3094788_+\|zinc-ABC-transporter-substrate-binding-protein	gnl\|CDD\|238500	cd01018, ZntC, Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and bind their specific ligands in the cleft between these domains. In addition, many of these proteins possess a metal-binding histidine-rich motif (repetitive HDH sequence).	2.27618e-80
NZ_AP019735.1\|WP_019129373.1\|3107257_3108172_-\|mechanosensitive-ion-channel-family-protein	gnl\|CDD\|223740	COG0668, MscS, Small-conductance mechanosensitive channel [Cell envelope biogenesis, outer membrane].	5.34409e-51
NZ_AP019735.1\|WP_019129372.1\|3108258_3109482_+\|phosphoserine-phosphatase-SerB	gnl\|CDD\|319803	cd07500, HAD_PSP, phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p. This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	1.43223e-101
NZ_AP019735.1\|WP_141413403.1\|3104046_3105189_-\|galactose-1-epimerase	gnl\|CDD\|185696	cd09019, galactose_mutarotase_like, galactose mutarotase_like. Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.	4.12736e-175
NZ_AP019735.1\|WP_026074695.1\|3105525_3105996_-\|methylglyoxal-synthase	gnl\|CDD\|179969	PRK05234, mgsA, methylglyoxal synthase; Validated.	9.15906e-79
NZ_AP019735.1\|WP_141413400.1\|3100673_3101960_+\|DUF21-domain-containing-protein	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	7.55024e-125
NZ_AP019735.1\|WP_026074694.1\|3106266_3106674_-\|DUF5606-domain-containg-protein	gnl\|CDD\|375774	pfam18347, DUF5606, Domain of unknown function (DUF5606). This is a domain of unknown function found at the N-terminal region of bacterial proteins.	1.28728e-23
NZ_AP019735.1\|WP_141413401.1\|3101946_3102972_+\|tRNA-dihydrouridine-synthase-DusB	gnl\|CDD\|129820	TIGR00737, Probable_tRNA-dihydrouridine_synthase, putative TIM-barrel protein, nifR3 family. This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General].	3.73198e-119
NZ_AP019735.1\|WP_141413398.1\|3098507_3100286_-\|arginine--tRNA-ligase	gnl\|CDD\|223097	COG0018, ArgS, Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis].	4.53486e-157
NZ_AP019735.1\|WP_141413397.1\|3097556_3098360_-\|hypothetical-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	0.00971963
NZ_AP019735.1\|WP_141413402.1\|3102977_3104036_-\|winged-helix-DNA-binding-domain-containing-protein	gnl\|CDD\|377630	pfam06224, HTH_42, Winged helix DNA-binding domain. This family contains two copies of a winged helix domain.	7.26288e-63
NZ_AP019735.1\|WP_141413395.1\|3094780_3095530_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213202	cd03235, ABC_Metallic_Cations, ATP-binding cassette domain of the metal-type transporters. This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.	1.94544e-82
NZ_AP019735.1\|WP_141413396.1\|3095526_3096900_-\|aldehyde-dehydrogenase-family-protein	gnl\|CDD\|143454	cd07136, ALDH_YwdH-P39616, Bacillus subtilis aldehyde dehydrogenase ywdH-like. Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.	0
NZ_AP019735.1\|WP_141413391.1\|3087797_3090005_+\|RelA/SpoT-family-protein	gnl\|CDD\|223394	COG0317, SpoT, Guanosine polyphosphate pyrophosphohydrolases/synthetases [Signal transduction mechanisms / Transcription].	0

>NZ_AP019735.1|WP_141413398.1|3098507_3100286_-|arginine--tRNA-ligase
MNIDHFISEAVSRSVEALYGPLGEEQLQIQKTRKEFDGDYTLVVFPLLRRSRKSPEATAAEIGEHLTAHMPEVKSFNVIKGFLNLALSDGFWADRFAEIAADGAFGQAPATGRNVMIEYSSPNTNKPLHLGHIRNNLLGYSVAQILRAVGHNVIKVNLVNDRGIHICKSMLAWKRYGGGETPASSGMKGDHLVGKYYVEFDKHYKAQVKELTASGMSEEEAKKRAPLMLEAQEMLRRWEARDPEVYGLWEMMNGWVYGGFDVTYKALGVDFDKVYYESQTYLLGKDIVQKGLDMGIFYRREDGSVWIDLTADGLDQKLLLRGDGTSVYMTQDLGTAYRRFEENDLDDMIYVVGNEQNYHFQVLKLVLKKLGYDWSDHITHLSYGMVELPNGKMKSREGTVVDADDLIDDMVRTAREMSDELGKLDDCTEDEAAAISRMVGLGALKYFILKVDPKKTMLFDPRESIDFNGNTGPFIQYTHARIRSVLRKAQEAGIACGEASAAAYLPEEVALVKQLADYPNVVKAAAENFAPSIVAAYAYELAKQYNAYYHDHSILREEDAAVRAMRLRLSEQVARVIRLAMRLLGIDVPERM
>NZ_AP019735.1|WP_141413397.1|3097556_3098360_-|hypothetical-protein
MKRIFTTFVCAFAVCAAADAQQRSGAPASCPQADTVLLSADVDGTYLVRKYLVKQHADRNSDYAVRYQVDVAQLSSTLAGNARQLDDLQAFIDKVSQDKSLRVTGVTITGYASPDGPYAPNERLARKRATDFRNYVDSRYRLSASYPVTVSAVVDEWRAAVPAVEASSIPSKQEVLQILNGSDKATVKEMRLKRLPAAWNYMRQHILPPMRHVEMAFTYDKSSVVTERTPIPLPEVEPVIHATYILVDDQPDGLIIDMDEFDCTCTM
>NZ_AP019735.1|WP_019129383.1|3097081_3097372_-|hypothetical-protein
MANLRELKKEIDYRLEEVVFDCDMAIAFQPSKEQEIFELMQKAVALRNELIAKVSNPTEPHNKSLVRKYYAALRADIVRSFEALFEELSKINEAKK
>NZ_AP019735.1|WP_141413396.1|3095526_3096900_-|aldehyde-dehydrogenase-family-protein
MDIPKLIAAQRAYFETGATHDIAVRRRALQALQASVRRHEEVLCSALRADLGKSAVESYMTEIGIVAGEIRFALRNLKRWMRPRRVPTPLFAWPARSRVRYEPLGVVLVVAPWNYPLQLTLLPLVGALAAGNCVVLKPSPGAPATAAVLSEIVGECFPEELVALVPHAPQAVEELLTQRFDHIFYTGGGTFGREIMVRAAERLTPVTLELGGKSPCVVGAEADLKLAARRIVWGKTLNAGQTCVAPDFLLVHESVCDRLLVELQRAVERQWGSDPRFAVDYPRMVDGAHARRVAELLSTAGGETVCGGEVLEEERYVAPTIVLNPDPQSRLMREEIFAPVLPVLTFAELSEAADALLAADRPLALYYFGDEREGRRLCERVPSGGVAFNDVVMQVSSRRLPFGGVGASGMGRYHGEASFECFSNCRSYFLGSKRFDLPLRYAPYPKRLLGWLRRLMD
>NZ_AP019735.1|WP_141413395.1|3094780_3095530_+|ATP-binding-cassette-domain-containing-protein
MSNVLISVRDLSVAYEGTTALDEVSLDIFEDDFLGVIGPNGGGKTSLVRAILGNIPYRGTVNYAAELFRGKERLIGYLPQQNVFDRAFPISVTETVLSGLQGHKRFRSRYTAEDRRRALELLERTGIAEVAGRAIGEISGGQMQRALLCRAIISEPRLLILDEPANFVDNQFENELYRILQELNRRMAIVMVSHDVGTISSVVKSIVCVNRHVHRHDSNVIDEEQLRNYGCPIQLISHGDVPHTVLSRH
>NZ_AP019735.1|WP_019129386.1|3093897_3094788_+|zinc-ABC-transporter-substrate-binding-protein
MRTAYLYLLFLSLFATGCTSSTRQTDKERLYVSILPLRSLVEQIVGDDFKVDVLVPAGASPESFEPTPRQYVALNRSKLVFNVGLIDFEQNLLRDFPDREKLVNLSRGIRLLEGSCAHGHTHEPTEKARASEGHAHGIDPHIWTSPRALKQMAANAYDALRTSFPDSVRYTENYEKLLVRLDSLDTACAEALRQADVHTIVIYHPALTYYAADYGLEQLAVEHDGKEPSARHLARLIEEARRKKVRRVFYQAQYPASTVKVIAEDIGARSVKIDPLREDVIENIGEITRQLTSGNE
>NZ_AP019735.1|WP_141413394.1|3092753_3093212_+|helix-turn-helix-domain-containing-protein
MGEKLLRLMKSEGLTSSRLAEILGTGASNISHIISGRSKPGYDLLRKILLSFPQINPDWLLLDDETMYRSDETPIREQPVSPDLFTAESATSEHPSGSPYETDIAGNTDTVDAVDPHRIASGGFRNMTSSTVQRIIIVYSDRTFESFTPKQE
>NZ_AP019735.1|WP_019129388.1|3090477_3090864_+|HIT-family-protein
MASIFSRIIAGEIPSYKVAEDANYYAFLDINPLTEGHTLVVPKKEVDYIFDLDDQTLAGMMLFAKKIARRIERQIDCKRVAVVVLGLEVPHAHIHLIPIKSESDVDFRREKLSLTPEEFQAIAAKLNR
>NZ_AP019735.1|WP_141413392.1|3090017_3090464_+|hypothetical-protein
MDITVLIWVAIIILWSVKTASDQKKRTQRQERQADDTAERVAPPVEMEPRPARHARRPAEQEARRDARVEEAASEPLVVEAVSLETFDDEASAADTIPAPIATHDVRQETPEEKRPTCPAATDGPLGEPFDLRRAVIYSEILKPKFEE
>NZ_AP019735.1|WP_141413391.1|3087797_3090005_+|RelA/SpoT-family-protein
MDYTAEDEKIIEERWEDLLRSCTKICRKDEDWDFIKRAFFLAKEAHAGVRRRSGEPYLLHPIAVAKIVIEEIGLGVKSVVASLLHDVVEDTEYTVEDMERIFGPKIASMVDGLTKMSGVFNADTSEQAEYFRKVLLTLSDDVRVILIKIADRLHNMRTLGAMPLNKQIKITSETIYLFAPLAYRLGLFAIKTELEDLCMKYRFPEQYEEISRKLDETEASRQEFIARFNAPIVEALRHDGINFEISARVKSIYSIWMKMQRKQIPFEEVYDLFAIRIVFKPLPFPSEKTQCYQIYATITDIYTPKPDRLRDWINTPKANGYEALHSTVTSPDGVWVEVQIRTQRMDDIAERGVAAHWKYKQETISQNEDELDKWLKKIRDALNSPTENAVDFLDNFKLSLYTSEIVVFTPKGEPRRLPFGATALDFAYDIHTNVGNKAIGAKINHKLEPVTTQISSGDQIEIITADNARPKAEWLDLVTTSKAKQSIKNFLKREQQNNIERGMATLTERLAKLNINLSGRVLRKLVPAYECATKEEFYSKIGAGIIRLDDIEKHLKVNSASKILKFWTLFIPKKARPESEDDETPAIDEAADDTSPEFVVAECCKPIPGDKVVGFRDPQSGKIIVHKATCEELNRLASQFGRNIIKDEIKWSQHKAVSYLSTIELRGIDRTGILLDLANVISRDFSINIREIGIQSHDGIFEGTLSLYVKNAESLSVVLENLRKIKGMESVKRNL
>NZ_AP019735.1|WP_141413400.1|3100673_3101960_+|DUF21-domain-containing-protein
MEIVIIILLILLNGIFAMSEIALISARRSNLELRARQGNAGARRALRIIEDPDKFLSTIQIGITLIGILTGIYSGDALAAKFGRELALLGIPLRTATIAAQVTIVVIVTYLTLIFGELVPKRIGMNTAEKIACAVARPMRALSVAASPFVWLLSRSTAAITRLLGLKESDNKVTEEEIRSIIQESVDDGEVRVVEQQIVGRVFSLGDRAVDSVMTPRSEIVWIDIAMTTDQIRERVNRNPHSLYPVADGELDKLVGVVYLKDLFQHLAEPDFNLCKTLRPVKFFHESCEVYNAMDQLRSEQLGYGIVCDEFGVTRGIVTLKDIFEALVGEIPEDLDEPDIVRREDGSCLVDGQCSFYDFLAYFNMEEVIPHTAYKTISGLILDELDHIPQTGEKLHWNRFTLEIVDMDGARIDKILVTPDTIPADENS
>NZ_AP019735.1|WP_141413401.1|3101946_3102972_+|tRNA-dihydrouridine-synthase-DusB
MKIADLELGDKPLFLAPMEDVTDPSFRSMCKEFGADVVYTEFISSDGLIRDAAKSLKKLEITEAERPVGIQIYGHLIEPMVEAARMAEAAGPDIIDINFGCPMKKIAGRGAGSGMMRDVPLMVEMTRRIVQAVDHTPVTVKTRLGWDDENKNIEEIALRLQDVGIAALTIHGRTRAQIYRGEADWTLIGRVKNNPAIRIPIIGNGDVDSGPRAAAMFDRYGVDGVMIGRATYGRPWIFREVRHYLTTGEVLPQPTVVERVEIAKRHLRKSVEIKGEYVGILEMRRHLSNYFKGLPDFKQTRLQLVTLTDIPALMATLDSIAERWGDFDTSQVVPAPLSHEL
>NZ_AP019735.1|WP_141413402.1|3102977_3104036_-|winged-helix-DNA-binding-domain-containing-protein
MNRLTDIRLHAQQLVAPQFDDPVELIRWMGMVQAQEYGSAKWAVALRLRTLAAAPVEEALREGRILRMHIMRPTWHFIAAEDVRWMLHLSARRIRAANASFAKGNGCGLDEGDYLRCSRLLERILGGGNHLTRQQIAGELERAGMAVDAPRLNRLMMHAETDGVVCSGADRAGKPTYALLAERVPQAVDLPEEEALALLALRYFRSHSPATFDDFVWWSGLPVGQARRGVGALDGELLRESFGGREYLLHESWATCRKAPAHAHLLPAFDEYLIAYKDRSDVLAPEHRARAFNDFGVFRPVLLHGGRIVGQWGRKGTQVGVELFASEKQPSARLLRSAEGRWKLFREGQAFS
>NZ_AP019735.1|WP_141413403.1|3104046_3105189_-|galactose-1-epimerase
MKKTLLCWLAALGAAAVIPACGGAAGDKSLSGLDRERFRSEVNGRPTDLYTLTNAAGMEVCITNFGGRIVSVMVPDRTGTLRDVVLGFDNIADYVRIPSDFGASIGRYANRIGHGRFVLDGDTVRLPVNNYGHCLHGGPDGWQYRVYEAHQPDPQSLALTLHSPDGDAGFPGAVTAKVVYRLTEDNAIDITYEATADRPTVVNLTNHSYFNLSGDPTHPILDNLLTIAADGYTPVDSTFLTLGRIDSVGGTPFDFRRPKAIGAEIDSDDEQLRNGHGYDHNWVLATAGDLSRPAARLVSPVSGIALEVFTDEPGIQVYVGNFLDGTVRGKHGIPYAHRTAVCLETQHYPDSPNKPQWPSVVLRPGETYHSRCIYRFSVDK
>NZ_AP019735.1|WP_026074695.1|3105525_3105996_-|methylglyoxal-synthase
MKEKKKVALVAHDNMKRDLAEWVDWNWEILLRHHLVCTGTTGKMVTRTLTERGGAEEISHFDITLLKSGPLGGDQQLGSMIADGEISALIFFWDPMSAQPHDVDVKALLRIATLYNVPTAINRSSADFLISSPLFEHDDYRPVVKDYTSYIERVLK
>NZ_AP019735.1|WP_026074694.1|3106266_3106674_-|DUF5606-domain-containg-protein
MELKEILAISGQPGLYKYVAQSTNGVIVESLLDGKRMNASASSKVSALTEISIFTEGDDLPLADVFTNIYNHTGGKEAISHKEAPEKLKAAFAEVLPDYDRDRVHVSDMKKVFMWYNILLGAGFTEFKLPETEEE
>NZ_AP019735.1|WP_141413404.1|3106758_3107241_-|hypothetical-protein
MKKLIVWAVLSAAVAVLPSCGDDEGEGCSTPVISEVNYSPKNPSKSEEVTVTARIRNEHCPFQACVTYQVDSITGTWGNTTESYRSTDPVYSTVAGETYDFMAKIPATKLTGRKVRFMIEVTTQHRLYVSSDFEEYVVPGPIEPDPDQPGDSGESDGSEK
>NZ_AP019735.1|WP_019129373.1|3107257_3108172_-|mechanosensitive-ion-channel-family-protein
MLGFFLEAETLILPDSVQKAQWKQIVERFTSLDAETFLRDFTGQVIWVALKIAVAFAIYAAGRWIINRLVHLMDASFDRRQVDKSLRSFLRSLVKGAAYTILLLIIVQLLGFNTTSLVALLAASGFGIGMALSGTLQNFAGGIMVMFMHPYRIGDYIEAQGQAGTVKEIRLFSTVVTTTDNKRIYIPNSSISNAIVNNYSSETMRRVEWKVSLAYGDDVAVAKRTMLAMLESDKRVLHTPDAPADPFVALSELADSAIVVVARTWTLNGDYWDLFFDMNERFYNELPQQGLHFPFPQLDVHLDK
>NZ_AP019735.1|WP_019129372.1|3108258_3109482_+|phosphoserine-phosphatase-SerB
MESQVEIIQINIAGKDQPGLTSSLTDILARYDAFILDIGQANIHQSLTLGILIKTTSDKSGAIMKELLFKSSELGINIRFTPISEERYTAWVGMQGKNRYIITLLGRQLTARHIADVAGVISRQGLNIDAIKRMTGRVPLHEDERAPKSCIEFSVRGSLTEEATTAIQEQFMSFSNNGVDISFQRDDIFRRSRRLICFDMDSTLIETEVIDELAERAGVGAQVRAITERAMRGEIDFRESFTERVALLKGLDVSVMEEIAQQLPITEGLERMMTILKRVGYKTAILSGGFTYFGNYLRQRFGFDYVYANELEIVDGRLTGRYAGEIVDGRRKAELLRLLCQFENINIAQSIAVGDGANDLPMLSLAGLGIAFHAKPKVKATAGQSISTIGLDGILYFLGLKDSWIER
>NZ_AP019735.1|WP_141413405.1|3109486_3110263_+|hypothetical-protein
MKRPVVIALLALCGLSCGCRDRFDVPDTPADAPAANITIASLHAFLHAETVVVREELTVGGTVVSSDEAGNFYRTLVLDDGTGGAELRIAEYNLYTICPPGCRLTVSLRGCALGERNGVLQIGLPPDAYSPYPTGYISSRVLLERLLHPTGERQEPLATPCEIARLGTASCGRLVRIDALRFRPDAEQAVPQTWEGYRLFEDAAGRTIAVYTSAYARFADREIPAGECSLTGVLEYGTAGSYGKQFILQMRDENDCTH

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_AP019735_5	5.1\|901008\|52\|NZ_AP019735\|CRISPRCasFinder	901008-901059	52	NZ_AP019735.1	706173-706224	0	1.0
NZ_AP019735_5	5.1\|901008\|52\|NZ_AP019735\|CRISPRCasFinder	901008-901059	52	NZ_AP019735.1	805878-805929	0	1.0
NZ_AP019735_5	5.1\|901008\|52\|NZ_AP019735\|CRISPRCasFinder	901008-901059	52	NZ_AP019735.1	900931-900982	0	1.0
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	2019354-2019381	0	1.0
NZ_AP019735_2	2.1\|351178\|46\|NZ_AP019735\|CRISPRCasFinder	351178-351223	46	NZ_AP019735.1	700334-700379	1	0.978
NZ_AP019735_5	5.1\|901008\|52\|NZ_AP019735\|CRISPRCasFinder	901008-901059	52	NZ_AP019735.1	2434913-2434964	1	0.981
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	1700302-1700329	1	0.964
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	2463041-2463068	1	0.964
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	2669414-2669441	1	0.964
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	879217-879244	1	0.964
NZ_AP019735_5	5.1\|901008\|52\|NZ_AP019735\|CRISPRCasFinder	901008-901059	52	NZ_AP019735.1	902925-902976	2	0.962
NZ_AP019735_5	5.1\|901008\|52\|NZ_AP019735\|CRISPRCasFinder	901008-901059	52	NZ_AP019735.1	1718936-1718987	2	0.962
NZ_AP019735_13	13.1\|2400482\|49\|NZ_AP019735\|CRISPRCasFinder	2400482-2400530	49	NZ_AP019735.1	2019361-2019409	2	0.959
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	1559811-1559838	2	0.929
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	2960785-2960812	2	0.929
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	768535-768562	2	0.929
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	1474194-1474221	2	0.929
NZ_AP019735_17	17.1\|3100485\|28\|NZ_AP019735\|CRISPRCasFinder	3100485-3100512	28	NZ_AP019735.1	1544998-1545025	2	0.929

1. spacer 5.1|901008|52|NZ_AP019735|CRISPRCasFinder matches to position: 706173-706224, mismatch: 0, identity: 1.0

tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	CRISPR spacer
tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	Protospacer
****************************************************

2. spacer 5.1|901008|52|NZ_AP019735|CRISPRCasFinder matches to position: 805878-805929, mismatch: 0, identity: 1.0

tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	CRISPR spacer
tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	Protospacer
****************************************************

3. spacer 5.1|901008|52|NZ_AP019735|CRISPRCasFinder matches to position: 900931-900982, mismatch: 0, identity: 1.0

tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	CRISPR spacer
tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	Protospacer
****************************************************

4. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 2019354-2019381, mismatch: 0, identity: 1.0

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttggctgcgccttagatactccgtct	Protospacer
****************************

5. spacer 2.1|351178|46|NZ_AP019735|CRISPRCasFinder matches to position: 700334-700379, mismatch: 1, identity: 0.978

tttattcgtatctttgacttcgtcttagatacttcgcctcggccat	CRISPR spacer
tttattcgtatctttgacttcgtcttagatacttcgcctcagccat	Protospacer
****************************************.*****

6. spacer 5.1|901008|52|NZ_AP019735|CRISPRCasFinder matches to position: 2434913-2434964, mismatch: 1, identity: 0.981

tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	CRISPR spacer
tcttcgttttctcgcctcggcatagcccgaacaagttcggctctgcgctcgg	Protospacer
***************************.************************

7. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 1700302-1700329, mismatch: 1, identity: 0.964

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttggcttcgccttagatactccgtct	Protospacer
******** *******************

8. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 2463041-2463068, mismatch: 1, identity: 0.964

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttggctgcgccgtagatactccgtct	Protospacer
************* **************

9. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 2669414-2669441, mismatch: 1, identity: 0.964

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttggctgcgccgtagatactccgtct	Protospacer
************* **************

10. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 879217-879244, mismatch: 1, identity: 0.964

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttggctgcgccgtagatactccgtct	Protospacer
************* **************

11. spacer 5.1|901008|52|NZ_AP019735|CRISPRCasFinder matches to position: 902925-902976, mismatch: 2, identity: 0.962

tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	CRISPR spacer
tcttcgttttctcgcttcggcacagcctgaacaagttcggctctgcgctcgg	Protospacer
***************.******.*****************************

12. spacer 5.1|901008|52|NZ_AP019735|CRISPRCasFinder matches to position: 1718936-1718987, mismatch: 2, identity: 0.962

tcttcgttttctcgcctcggcatagcctgaacaagttcggctctgcgctcgg	CRISPR spacer
tcttcgttttctcgcctcggcatagtccgaacaagttcggctctgcgctcgg	Protospacer
*************************.*.************************

13. spacer 13.1|2400482|49|NZ_AP019735|CRISPRCasFinder matches to position: 2019361-2019409, mismatch: 2, identity: 0.959

agaagcaagcgtcagcttgattctaccgagacggagtatctaaggcgca	CRISPR spacer
agaagcaagcgtcagcttgattatgccgagacggagtatctaaggcgca	Protospacer
********************** *.************************

14. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 1559811-1559838, mismatch: 2, identity: 0.929

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttgactgcgtcttagatactccgtct	Protospacer
*****.*****.****************

15. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 2960785-2960812, mismatch: 2, identity: 0.929

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttggctgcgccgaagatactccgtct	Protospacer
*************  *************

16. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 768535-768562, mismatch: 2, identity: 0.929

ctttggctgcgccttagatactccgtct	CRISPR spacer
cttcggctgcgtcttagatactccgtct	Protospacer
***.*******.****************

17. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 1474194-1474221, mismatch: 2, identity: 0.929

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttgactgcgtcttagatactccgtct	Protospacer
*****.*****.****************

18. spacer 17.1|3100485|28|NZ_AP019735|CRISPRCasFinder matches to position: 1544998-1545025, mismatch: 2, identity: 0.929

ctttggctgcgccttagatactccgtct	CRISPR spacer
ctttggcttcgccttaggtactccgtct	Protospacer
******** ********.**********

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_AP019735_11	11.1\|1762178\|32\|NZ_AP019735\|CRISPRCasFinder	1762178-1762209	32	NZ_CP028919	Gemmobacter sp. HYN0069 plasmid unnamed1, complete sequence	194188-194219	6	0.812
NZ_AP019735_14	14.1\|2498695\|30\|NZ_AP019735\|CRISPRCasFinder	2498695-2498724	30	NZ_CP022371	Bosea sp. AS-1 plasmid unnamed2, complete sequence	5763-5792	6	0.8
NZ_AP019735_11	11.1\|1762178\|32\|NZ_AP019735\|CRISPRCasFinder	1762178-1762209	32	NZ_HG938354	Neorhizobium galegae bv. orientalis str. HAMBI 540 plasmid pHAMBI540a, complete sequence	1596581-1596612	9	0.719
NZ_AP019735_11	11.1\|1762178\|32\|NZ_AP019735\|CRISPRCasFinder	1762178-1762209	32	NC_010514	Methylobacterium radiotolerans JCM 2831 plasmid pMRAD03, complete sequence	23074-23105	11	0.656

1. spacer 11.1|1762178|32|NZ_AP019735|CRISPRCasFinder matches to NZ_CP028919 (Gemmobacter sp. HYN0069 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.812

gttgcgctcggcttgacgaaatggttgaattt	CRISPR spacer
gttgcgcgcggcttgacggaatggttgcgctg	Protospacer
******* **********.******** ..*

2. spacer 14.1|2498695|30|NZ_AP019735|CRISPRCasFinder matches to NZ_CP022371 (Bosea sp. AS-1 plasmid unnamed2, complete sequence) position: , mismatch: 6, identity: 0.8

ggacattgccgagcgggagtatctacggcg-	CRISPR spacer
tgacattgccgagcgggaggacct-ctccgt	Protospacer
 ****************** *.** *  **

3. spacer 11.1|1762178|32|NZ_AP019735|CRISPRCasFinder matches to NZ_HG938354 (Neorhizobium galegae bv. orientalis str. HAMBI 540 plasmid pHAMBI540a, complete sequence) position: , mismatch: 9, identity: 0.719

gttgcg----ctcggcttgacgaaatggttgaattt	CRISPR spacer
----cggctcctcggcttgccgaaaaggttgaagcg	Protospacer
    **    ********* ***** ******* .

4. spacer 11.1|1762178|32|NZ_AP019735|CRISPRCasFinder matches to NC_010514 (Methylobacterium radiotolerans JCM 2831 plasmid pMRAD03, complete sequence) position: , mismatch: 11, identity: 0.656

gttgcgctcggcttgacgaaatggttgaattt	CRISPR spacer
agcccgctcgccttgacgaaatggctgtcgga	Protospacer
. . ****** *************.**

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

377562 : 426513

Flavobacterium_phage(13.33%)

integrase,portal,terminase,head,capsid,protease,tRNA

attL 417551:417563|attR 427356:427368

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_141411988.1\|377562_378840_-\|capsid	phage major capsid protein	R9ZZJ5	Cellulophaga_phage	2.7e-32	29.7
WP_141411989.1\|378845_379541_-\|head,protease	HK97 family phage prohead protease	A0A0R6PIB4	Moraxella_phage	2.8e-15	34.2
WP_162502255.1\|379540_380752_-\|portal	phage portal protein	NA	NA	NA	NA
WP_162502256.1\|380858_382091_-	hypothetical protein	A0A1B0WLL2	Flavobacterium_phage	1.2e-29	29.5
WP_141411992.1\|382074_382665_-\|terminase	terminase small subunit	A0A1V0E5Q4	Salmonella_phage	1.5e-06	40.3
WP_141411993.1\|382718_382946_-	hypothetical protein	NA	NA	NA	NA
WP_141411994.1\|382967_383321_-	hypothetical protein	NA	NA	NA	NA
WP_141411995.1\|383325_383688_-	hypothetical protein	NA	NA	NA	NA
WP_141411996.1\|383723_384194_-	hypothetical protein	NA	NA	NA	NA
WP_141411997.1\|384195_384813_-	hypothetical protein	A0A219YFC7	Ochrobactrum_phage	1.9e-07	33.7
WP_141411998.1\|384809_385688_-	radical SAM protein	H7BVD6	unidentified_phage	1.8e-51	39.5
WP_141411999.1\|385678_386176_-	adenine methyltransferase	A0A223W0E9	Agrobacterium_phage	5.9e-52	60.2
WP_141412000.1\|386259_387024_-	phage antirepressor KilAC domain-containing protein	B5TRA6	Bacteroides_phage	6.5e-66	54.8
WP_141412001.1\|387026_387542_-	hypothetical protein	NA	NA	NA	NA
WP_141412002.1\|387627_388341_-	pentapeptide repeat-containing protein	NA	NA	NA	NA
WP_141412003.1\|388318_388714_-	VRR-NUC domain-containing protein	NA	NA	NA	NA
WP_141412004.1\|388710_389298_-	hypothetical protein	NA	NA	NA	NA
WP_141412005.1\|389300_390152_-	hypothetical protein	NA	NA	NA	NA
WP_141412006.1\|390148_390517_-	hypothetical protein	NA	NA	NA	NA
WP_141412007.1\|390670_390967_-	hypothetical protein	A0A218ML91	uncultured_virus	4.9e-06	34.3
WP_141412008.1\|390969_391428_-	hypothetical protein	NA	NA	NA	NA
WP_141412009.1\|391424_392117_-	hypothetical protein	NA	NA	NA	NA
WP_162502257.1\|392120_392291_-	hypothetical protein	NA	NA	NA	NA
WP_141412010.1\|392292_392691_-	hypothetical protein	NA	NA	NA	NA
WP_019129613.1\|394431_394797_-	DUF2335 domain-containing protein	S5WJ01	Leptospira_phage	2.3e-05	30.9
WP_141412011.1\|395381_395990_-	hypothetical protein	NA	NA	NA	NA
WP_141412012.1\|396180_396453_-	hypothetical protein	NA	NA	NA	NA
WP_141412013.1\|397040_397274_-	hypothetical protein	NA	NA	NA	NA
WP_141412014.1\|397399_398047_+	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_141412015.1\|398087_398477_+	hypothetical protein	NA	NA	NA	NA
WP_141412016.1\|398607_399306_+	hypothetical protein	F5A3G5	Riemerella_phage	9.3e-11	26.7
WP_141412017.1\|399331_399847_+	hypothetical protein	NA	NA	NA	NA
WP_162502241.1\|400001_400316_+	hypothetical protein	NA	NA	NA	NA
WP_141412019.1\|400377_400968_+	ORF6N domain-containing protein	NA	NA	NA	NA
WP_141413532.1\|401433_402786_+	FAD-dependent oxidoreductase	NA	NA	NA	NA
WP_141412020.1\|402942_405732_-	family 78 glycoside hydrolase catalytic domain	NA	NA	NA	NA
WP_141412021.1\|406075_407896_-	beta-galactosidase	NA	NA	NA	NA
WP_141412022.1\|408158_410432_+	bifunctional alpha,alpha-trehalose-phosphate synthase (UDP-forming)/trehalose-phosphatase	NA	NA	NA	NA
WP_019131167.1\|410421_412215_+	glycoside hydrolase family 15 protein	NA	NA	NA	NA
WP_141412023.1\|412269_414807_-	hypothetical protein	NA	NA	NA	NA
WP_026075041.1\|414864_416271_-	peptidylprolyl isomerase	NA	NA	NA	NA
WP_141412024.1\|416290_417163_-	hypothetical protein	NA	NA	NA	NA
WP_141412025.1\|417217_418195_-\|protease	CPBP family intramembrane metalloprotease	NA	NA	NA	NA
417551:417563	attL	NA	NA	NA	NA
WP_019131172.1\|418312_419083_+	ParA family protein	A0A240F4U1	Ochrobactrum_phage	1.4e-15	30.4
WP_026075042.1\|419241_420102_+	ParB/RepB/Spo0J family partition protein	I3NLC2	Bifidobacterium_phage	2.0e-15	37.7
WP_141412026.1\|420105_421404_+	hypothetical protein	NA	NA	NA	NA
WP_141412027.1\|421420_422800_+	transglycosylase SLT domain-containing protein	A0A0S2SXN2	Bacillus_phage	2.5e-15	43.4
WP_141412028.1\|422796_424140_+\|tRNA	tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE	NA	NA	NA	NA
WP_117513472.1\|424401_425280_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_117513473.1\|425397_426513_+\|integrase	site-specific integrase	A0A1B0WMK0	Flavobacterium_phage	5.3e-08	29.7
427356:427368	attR	NA	NA	NA	NA

DBSCAN-SWA_2

1849008 : 1856658

Synechococcus_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_019130343.1\|1849008_1849725_+	phosphoribosylaminoimidazolesuccinocarboxamide synthase	G8EYA2	Synechococcus_phage	2.5e-43	42.5
WP_019130342.1\|1849800_1851213_+	amidophosphoribosyltransferase	A0A0M3SGR2	Mollivirus	5.0e-48	32.1
WP_019130341.1\|1851263_1852289_+	phosphoribosylformylglycinamidine cyclo-ligase	Q58MH8	Prochlorococcus_phage	2.9e-61	40.2
WP_141412704.1\|1852296_1852860_+	phosphoribosylglycinamide formyltransferase	M4QRX9	Synechococcus_phage	7.4e-19	37.2
WP_141412705.1\|1852870_1854400_+	bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase	Q58MG4	Prochlorococcus_phage	4.7e-76	48.3
WP_141412706.1\|1854545_1855796_+	phosphoribosylamine--glycine ligase	NA	NA	NA	NA
WP_141412707.1\|1855800_1856658_+	bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD	A0A249XZQ2	Enterococcus_phage	4.4e-31	40.6

DBSCAN-SWA_3

2895678 : 2903164

Enterobacteria_phage(28.57%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_141413282.1\|2895678_2896146_-	thioredoxin	A0A1J0GW78	Streptomyces_phage	3.6e-11	39.5
WP_141413283.1\|2896893_2897952_-	dTDP-glucose 4,6-dehydratase	I7HTA3	Enterobacteria_phage	1.2e-83	49.4
WP_141413651.1\|2898031_2898820_-	glycerophosphodiester phosphodiesterase	A0A173GBD0	Staphylococcus_phage	1.8e-07	26.2
WP_141413284.1\|2898832_2899699_-	dTDP-4-dehydrorhamnose reductase	A0A291LA50	Escherichia_phage	1.5e-39	40.5
WP_141413285.1\|2899691_2900264_-	dTDP-4-dehydrorhamnose 3,5-epimerase	A0A1D8EQH2	Escherichia_phage	2.3e-44	55.1
WP_141413286.1\|2900308_2901190_-	glucose-1-phosphate thymidylyltransferase RfbA	I7I009	Enterobacteria_phage	2.4e-104	63.1
WP_141413287.1\|2901214_2903164_-	polysaccharide biosynthesis protein	A0A1V0SAI8	Catovirus	6.3e-25	29.2

Anti-CRISPR protein detection

Acr_ID: NZ_AP019735.1|WP_141411797.1|60682_61102_+|PcfK-like-protein

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Acr_ID: NZ_AP019735.1|WP_004291533.1|1161269_1161686_+|hypothetical-protein

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Acr ID

Acr position

Acr size

Homology with known anti

Neighbor HTH/AcRanker

Neighbor Aca

In prophage

Protospacer in prophage

NZ_AP019735.1|WP_141411797.1|60682_61102_+|PcfK-like-protein

60682_61102_+

139 aa aa

hit_Aca_id	identity	query_coverage	hit_coverage
gnl\|BL_ORD_ID\|40	0.5833333333333334	0.9568345323741008	0.9290780141843972

NZ_AP019735.1|WP_004291533.1|1161269_1161686_+|hypothetical-protein

1161269_1161686_+

138 aa aa

hit_Aca_id	identity	query_coverage	hit_coverage
gnl\|BL_ORD_ID\|40	0.5571428571428572	0.9855072463768116	0.9929078014184397

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_AP019735

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

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