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_CP016795	Streptomyces olivaceus strain KLBMP 5084 chromosome, complete genome	8 crisprs	DEDDh,WYL,cas4,csa3,Cas9_archaeal,RT,cas3,c2c9_V-U4,cas8e,cse2gr11,cas7,cas5,cas6e,DinG	1	4	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP016795_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016795_1

755504-755656

Orphan

Consensus_repeat	Method
CCGGTCCGGTGGGTCCTCGTCGGC	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP016795_1

>merge|NZ_CP016795|1|755504-755656|CRISPRCasFinder
CCGGTCCGGTGGGTCCTCGTCGGCGCGGGAGCGGAACCCGCCCAGTGGTTCTCGTCGGCGCGGGAGCGGTCCCGGTCCGGTGGGTTCTCGTCGGCACGACGGCGGGGCCCGTCAGCCGAGCCAGCCCGGCCGGACCAGTCCGGACTCGTAGGC

>NZ_CP016795|1|1|755504-755656|CRISPRCasFinder
CCGGTCCGGTGGGTCCTCGTCGGC	GCGGGAGCGGAACCCGCCCAGTGGTTCTCGTCGGCGCGGGAGCGGTC
CCGGTCCGGTGGGTTCTCGTCGGC	ACGACGGCGGGGCCCGTCAGCCGAGCCAGCCCGG
CCGGACCAGTCCGGACTCGTAGGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016795.1\|WP_031029491.1\|761769_761964_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031029450.1\|743177_743774_+\|DNA-starvation/stationary-phase-protection-protein	unknown	unknown	gnl\|CDD\|153102
NZ_CP016795.1\|WP_037762050.1\|748756_750043_+\|sugar-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270303
NZ_CP016795.1\|WP_070387474.1\|744940_746143_+\|cysteine-desulfurase-like-protein	unknown	unknown	gnl\|CDD\|273906
NZ_CP016795.1\|WP_070387476.1\|753421_754612_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340951
NZ_CP016795.1\|WP_031029504.1\|768019_768808_-\|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein	unknown	unknown	gnl\|CDD\|238847
NZ_CP016795.1\|WP_070387473.1\|743784_744852_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274414
NZ_CP016795.1\|WP_070387477.1\|764673_765543_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_070387478.1\|765523_766822_-\|aldolase	unknown	unknown	gnl\|CDD\|367449
NZ_CP016795.1\|WP_031029482.1\|757685_758984_-\|geranylgeranyl-reductase-family-protein	unknown	unknown	gnl\|CDD\|273936
NZ_CP016795.1\|WP_037762047.1\|751893_753273_+\|beta-glucosidase	unknown	unknown	gnl\|CDD\|274539
NZ_CP016795.1\|WP_031029485.1\|759133_760489_+\|dipeptidase	unknown	unknown	gnl\|CDD\|236127
NZ_CP016795.1\|WP_079154857.1\|763419_764496_+\|LacI-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224525
NZ_CP016795.1\|WP_037762024.1\|760567_761611_-\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|239217
NZ_CP016795.1\|WP_070387475.1\|746199_748470_-\|alpha-xylosidase	unknown	unknown	gnl\|CDD\|236731
NZ_CP016795.1\|WP_031029464.1\|750066_751020_+\|sugar-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224096
NZ_CP016795.1\|WP_031029467.1\|751025_751853_+\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_CP016795.1\|WP_031029494.1\|762076_763030_-\|ROK-family-protein	unknown	unknown	gnl\|CDD\|224851
NZ_CP016795.1\|WP_031029502.1\|767001_767964_-\|electron-transfer-flavoprotein-subunit-alpha/FixB-family-protein	unknown	unknown	gnl\|CDD\|224936
NZ_CP016795.1\|WP_037762041.1\|754719_755460_+\|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme	unknown	unknown	gnl\|CDD\|274422

Protein	Function_ID	Function_description	E-value
NZ_CP016795.1\|WP_031029450.1\|743177_743774_+\|DNA-starvation/stationary-phase-protection-protein	gnl\|CDD\|153102	cd01043, DPS, DPS protein, ferritin-like diiron-binding domain. DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.	3.32934e-46
NZ_CP016795.1\|WP_037762050.1\|748756_750043_+\|sugar-ABC-transporter-substrate-binding-protein	gnl\|CDD\|270303	cd13585, PBP2_TMBP_like, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold. This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	6.83073e-73
NZ_CP016795.1\|WP_070387474.1\|744940_746143_+\|cysteine-desulfurase-like-protein	gnl\|CDD\|273906	TIGR01976, am_tr_V_VC1184, cysteine desulfurase family protein, VC1184 subfamily. This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity].	1.87297e-169
NZ_CP016795.1\|WP_070387476.1\|753421_754612_+\|MFS-transporter	gnl\|CDD\|340951	cd17393, MFS_MosC_like, Membrane protein MosC and similar proteins of the Major Facilitator Superfamily of transporters. The gene encoding Sinorhizobium meliloti membrane protein MosC is part of the mos locus, which encodes the biosynthesis of the rhizopine 3-O-methyl-scyllo-inosamine. MosC belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	4.51483e-93
NZ_CP016795.1\|WP_031029504.1\|768019_768808_-\|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein	gnl\|CDD\|238847	cd01714, ETF_beta, The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is an heterodimer that consists of an alpha and a beta subunit which binds one molecule of FAD per dimer . A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The beta subunit protein is distantly related to and forms a heterodimer with the alpha subunit.	2.79927e-78
NZ_CP016795.1\|WP_070387473.1\|743784_744852_+\|hypothetical-protein	gnl\|CDD\|274414	TIGR03062, hypothetical_protein_lp_1332, YhgE/Pip C-terminal domain. This family contains the C-terminal domain of a family of multiple membrane-spanning proteins of Gram-positive bacteria. One member was shown to be a host protein essential for phage infection, so many members of this family are called "phage infection protein". A separate model, TIGR03061, represents the conserved N-terminal domain. The domains are separated by regions highly variable in both length and sequence, often containing extended heptad repeats as described in model TIGR03057.	0.000221798
NZ_CP016795.1\|WP_070387478.1\|765523_766822_-\|aldolase	gnl\|CDD\|367449	pfam03328, HpcH_HpaI, HpcH/HpaI aldolase/citrate lyase family. This family includes 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase and 4-hydroxy-2-oxovalerate aldolase.	1.44856e-05
NZ_CP016795.1\|WP_031029482.1\|757685_758984_-\|geranylgeranyl-reductase-family-protein	gnl\|CDD\|273936	TIGR02032, Uncharacterized_protein_MJ1520, geranylgeranyl reductase family. This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll].	6.83105e-99
NZ_CP016795.1\|WP_037762047.1\|751893_753273_+\|beta-glucosidase	gnl\|CDD\|274539	TIGR03356, BGL, beta-galactosidase.	0
NZ_CP016795.1\|WP_031029485.1\|759133_760489_+\|dipeptidase	gnl\|CDD\|236127	PRK07907, PRK07907, hypothetical protein; Provisional.	0
NZ_CP016795.1\|WP_079154857.1\|763419_764496_+\|LacI-family-transcriptional-regulator	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	1.26735e-102
NZ_CP016795.1\|WP_037762024.1\|760567_761611_-\|NUDIX-domain-containing-protein	gnl\|CDD\|239217	cd02883, Nudix_Hydrolase, Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes 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. Members of this family are recognized by a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of nudix hydrolase 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 and "house-cleaning" enzymes. Substrate specificity is used to define child 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. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.	6.57924e-19
NZ_CP016795.1\|WP_070387475.1\|746199_748470_-\|alpha-xylosidase	gnl\|CDD\|236731	PRK10658, PRK10658, putative alpha-glucosidase; Provisional.	0
NZ_CP016795.1\|WP_031029464.1\|750066_751020_+\|sugar-ABC-transporter-permease	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	2.13227e-91
NZ_CP016795.1\|WP_031029467.1\|751025_751853_+\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	3.23566e-72
NZ_CP016795.1\|WP_031029494.1\|762076_763030_-\|ROK-family-protein	gnl\|CDD\|224851	COG1940, NagC, Transcriptional regulator/sugar kinase [Transcription / Carbohydrate transport and metabolism].	7.55546e-64
NZ_CP016795.1\|WP_031029502.1\|767001_767964_-\|electron-transfer-flavoprotein-subunit-alpha/FixB-family-protein	gnl\|CDD\|224936	COG2025, FixB, Electron transfer flavoprotein, alpha subunit [Energy production and conversion].	4.34175e-105
NZ_CP016795.1\|WP_037762041.1\|754719_755460_+\|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme	gnl\|CDD\|274422	TIGR03083, TIGR03083, uncharacterized Actinobacterial protein TIGR03083. This protein family pulls together several groups of proteins, each very different from the others. They share in common three conserved regions. The first is a region of about 38 amino acids, nearly always at the N-terminus of a protein. This region has a bulky hydrophobic residue, usually Trp, at position 29, and a His residue at position 37 that is invariant, so far, in over 150 instances. The second conserved region has a motif [DE]xxxHxxD. The third conserved region contains a hydrophobic patch and a well-conserved Arg residue. Most examples are found in the Actinobacteria, including the genera Mycobacterium, Corynebacterium, Streptomyces, Nocardia, Frankia, etc. The pattern of near-invariant residues against a backdrop of extreme sequence divergence suggests enzymatic activity and conservation of active site residues.	2.42418e-17

>NZ_CP016795.1|WP_037762041.1|754719_755460_+|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme
MQTTAYVETLDREGALLAAAAEAAGGDAEVPTCPAWRVRDLLRHTGMVHRWATAFVAEGYTGPRPGGPLPDLDGAPLLAWFREGHGRLVDTLAGASPDVRCWHFLPAPSPLAFWARRQAHETTVHRLDAEAAAGGVPTGIGSDFAVDGIDELLCAFHTRPKSAVRTDGPRTLRVRATDVPDAVWTVRLSAQPPVTERDGTGGADCEVTGPAAVLYPALWNRRAFPTVHGDASLAALWRERSGVTWR
>NZ_CP016795.1|WP_070387476.1|753421_754612_+|MFS-transporter
MPGRRDDLTRLRAALTAFFALDGLVFAGWVVRIPAVKEQTGASASALGLALLGVSAGAVVTMTLTGRLVRRYDSHRVTVACAVLLCLSIALPPLTHSALALGAVLLVFGSAYGGINVAFNSAAVDLVAELRRPIMPSFHAAFSLGGMVGAGLGGLVAGSLSPTRHLLALTVTGLLVTLVAGRVLLRIEPLAPAERAAEEEGAAEKEGAGRRPDRRTRRLVVTFGLIALCTAYGEGAMADWGALHLEQDLDASPGLAAAGYSCFALAMTVGRLTGTTLLERLGRTATVVAGGTTAVAGMLTGALAPSVWAALFGFAITGLGLANIFPVAIERAGALGGPSGVATASTLGYGGMLLGPPAIGFMADWFSLPAALTSVAVLAAVAVLVAVATRRATVPA
>NZ_CP016795.1|WP_037762047.1|751893_753273_+|beta-glucosidase
MSDYPGFPPGFVLGAATASYQIEGAAQEDGRGPSIWDTYSHTPGLVANGDTGDVACDHYHRYPEDVALLRDLGVHSYRFSIAWPRIVPDGSGPVNRKGLDFYSRLVDELLTAGIEPAATLYHWDLPQALEDRGGWRVRETAERFAEYTAVVAEHLGDRVPRWITLNEPWCSSFLGYSVGRHAPGAKEGRGALAAAHHLLVGHGLAVKALRAAGVREVGITLNLDRNLPATDSAADLAAVVRADTQHNLVWTEPILAGRYPAAEEETWGELITGADFRQDGDLELISQPLDFLGVNYYRPIVVADAPHRESDPARRVATDNRYQEVRLPGVRETAMGWPVVPDSFTDLLVALKQQYGDALPPVHITENGSAEDDAPAADGAVHDTDRVAYLHDHLTALKSAIDAGVDVRGYYVWSLLDNFEWAYGYDKRFGIVRVDYDTQERTPKDSYRWYREMIAANRG
>NZ_CP016795.1|WP_031029467.1|751025_751853_+|carbohydrate-ABC-transporter-permease
MASHTPTASRRRWGSTVAGVLILCVMLFPLYWMLNTALQPDSGLLQVDPVPGGLDLSGFSKAVTDQGGHLLTSLAVSLGAVAICLAVSAPAAYGLARFGLRGSRTIVFGTLITQMVPGIVIANALYNSYVDLGLVNSYFGLMLADASLGIPFSIVLMRSFMVSIPGEVIEAAQIDGAGPVRTFVRVVLPMSRNSLITSGLFAFLFAWSDFMFALTLNTTDDVKPITLGIYQYIGAHVGDWGSVMAASVLSAVPAAILLVLAQKYIAAGITGGSVK
>NZ_CP016795.1|WP_031029464.1|750066_751020_+|sugar-ABC-transporter-permease
MPTSAVTARTPAEAPEPAAAPDPGRIARRRRLAQWGFVAPAVVFMLLFFGYPLVRNVVMSFQDYTPKTFFTGEAPFNGADNWSNVFQDALFGKALWHTLVFTAGSLLGQFCIGLALAVFFSRRFPLNGVLRSLILLPWLVPMVVSGIVWRRILDQDTGVLNSFLDTLGIAGHTPWLTSPEMALVSVILVNIWIGIPFNMVILYGGLQEIPKELHEAAALDGASAWRTFRSVTLPMLKPVVTVVLVLGFMSTVKILDLILALTDGGPADATQTLGTLTYQNSFVQLDFGAGAVVGNVLILISAVFAVFYLRANRTEGK
>NZ_CP016795.1|WP_037762050.1|748756_750043_+|sugar-ABC-transporter-substrate-binding-protein
MSKRFTSLALTAHPPAATHRGRERARRVVAPFAAVSVLVAGAALTGCGQQRDADVYTVMNSSTDESYHRWDAEAMARCGKQLGITIEQQSVPAAQVMTKALRMASSKSLPDIVQFDASEMPTFADAGGLVDLRTLGLSTDGIPDGIVDFGSYKGTYYGAARSVNTLALFYNKDVLDRAGVEVPTTWAGLRETAKRLTQGKQYGLALSAGGAEDGVFQFTPFMWSNGGDETDLDGPQVVEALDYWKGLLQDGSLSKSTVNWTQADVNDQFMAGNAAMMINGPWQVETLNSDKSLHWGIAPIPVPEAGDDSVGPLGGAVLTVPNTGDEAREKTAARIVACLASEKEQLTYALNSWMVPANARAAAVWREKVPELDSLADQVAVARSRTGKLGAGWSSVSLALQSAFQSALTGQSSETALKRAQQRATSGN
>NZ_CP016795.1|WP_070387475.1|746199_748470_-|alpha-xylosidase
MKFTDGFWLVREGVHLSYATEVRDVRHESKRFTAHAAVQKVTRRGDTLNAPLLTVECFSPVEGVIGVRVTHHAGKRRTGPEFALADPADGAGEVRREGTVTELTSGPLTLRLDREGPWGLTFRDADGRELTRANAKGTAFATTDDGAHHMLGRLALGVGEQVYGLGERFTPFVKNGQAVDMWQADGGTSSEQAYKNVPFYLSSRGYGVFVNHPGAVSFEVGSESVGQVQFSVEDQTLEYYVVAGPTPKDVLTRYTALTGRPALPPAWSFGLWLTTSFTTSYDETTVTSFVDGMAERDIPLSVFHFDCFWMREYQWCDFRWDPDVFPDPDGMLARLKARGLRISVWINPYIGQKSPLFEEAAALGHLVRRANGDIWQWDLWQAGMGLVDFTSPAARDWFAAKLKPLLDQGVDCFKTDFGERIPTDVVWHDGSDPERMHNYYTHLFNRTVFELLEKERGRGEAVLFARSATAGGQQYPVHWGGDCFSSFEAMAESLRGGLSLSLSGFGFWSHDIGGFEGTPDAAVFKRWLAFGLLSSHSRLHGSSSYRVPWEFGEEAVEVARDFTRLKHRLMPYLYGVAAEAHRTGVPMMRPMVLEYPHDPGCRPLDRQYMLGPDLLVAPVFTEDGEVEVYLPEGTWTHLLTGERVTGPVWRTERHGYDSLPLYVREGAVLPLARDDRRPDGDWLDAPTLLVHPPARADWAAEVTVPDLLGTAAAAFRVRREGDVLRVTASGTDRPFTVRVAGGASADGTGEVTVPLG
>NZ_CP016795.1|WP_070387474.1|744940_746143_+|cysteine-desulfurase-like-protein
MALDVEAIRAQIPALKSGSARFDAPGGTQTPQPVIDAIGEALANPLANRGRTTEGERNADGIVSEARAALGDLLATDPRGIVLGRSATQLAYDLSRTLAKSWGPGDEVVVTRLDHDSNIRPWVQAAEAAGASVRTADFDPATGELRPEHVEAVLSPRTRLVAVTAASNLVGAMPDLPAVARLAHGVGALVHVDAVHYASHAVVDPAVLGADTLVCSPYKFLGPHLGVLAARPEFLESLRPDKLLPSSDAVPERFELGTLPYELLAGTRAAVDFLAGLDPEARGSRRDRLVASFAALEAHEDALRGRIEQGLAALDGITVYSRAVRRTPTLLFTVAGLRPAEVYRHLADHGVDAPAGTFYALEASRRLGLGDEGGVRVGLAPYTDTDDVDRLLTALGTLNG
>NZ_CP016795.1|WP_070387473.1|743784_744852_+|hypothetical-protein
MAHLSEDDAGAGPPHRGHRWAAFRQTPFWPATVLMLILAAAAGLFAGSYTYSMANPTPRLIPTAVVGQYEQDRGRAFLAGLEKALDTSVRVHPYRTRTAAHEAIEQQEVFAVFELRDDGRNAVLDVSGASGASVAELLTKTAPAVGEKLGVHVTVHDVNPLQEGDPRGLAIFYVSLAAVIIGFVGAIQLSVHARSLTPVERILFTAAYALLGGFAIAATVDWLLGALDLPFAESWSILALTMFVSGMVFTMFNTLFGRWAMLPTWGLMVIIGNPSSGGAVSWPLLPSPLGLIGRWLPPGGSVNAQHTAVYFQGHQHVFPFLVLGGWALLSCTVFWVWRHRHPGGREKSAVTAEEP
>NZ_CP016795.1|WP_031029450.1|743177_743774_+|DNA-starvation/stationary-phase-protection-protein
MSSPKSSSSAQHSSDGSQPWLHQQGRIIQEFGTVKQFPVALSMETRLYSGQRLNKVLADTRILHDLYKKYHWLMRGATFYQLHLLLDKHAGEQLELIDTIAERVQTLGGVAVGDPRHVAEITTVPRPPDGVEEVPSMLSRLLEAHELILTECHDAAARTQELGDDGTNDLLVSEVVRTNELQAWFVAEHLVDTPLVHA
>NZ_CP016795.1|WP_031029482.1|757685_758984_-|geranylgeranyl-reductase-family-protein
MSSENSSAGDARQVWDVVVVGAGPAGASAAYAAAVAGRRVLLLEKAELPRYKTCGGGIIGPSRDTLPPGFELPFRDRVHAVTFSNNGRFTRTRRSRQMLFGLINRPEFDQQLVEHAQKAGAELRTGATVTRVEQHGSAVPDRRTVAVVLQGGETVLARAVVGADGSASRIGAHVGVKLDQVDLGLEAEIPVPETVADDWKGRVLIDWGPLPGSYGWVFPKGDTLTVGVISARGEGAATKRYLEDFVGRLGLAGFEPSISSGHLTRCRADDSPLSRGRVLVCGDAAGLLEPWTREGISFALRSGRLAGEWAVRIAESHDAVDARKQALNYAFAIKAGLGVEMSVGKRMLAVFERRPGLFHAALTGFRPAWKAFKDITQGSTTLGELVRGHPLAQRALAAMDRRPAGGEDTAPSAPADTVPATAPARADDEAGA
>NZ_CP016795.1|WP_031029485.1|759133_760489_+|dipeptidase
MSSNPVAETVASLMPRAKEELAALVAFRSVADFEQFPRSESVGAAEWTAAALRAEGFQDVALLDTPDGTQSVYGYLPGPEGAKTVLLYAHYDVQPPLDEAAWVSPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGTGGLERYAEAHPELLAADTVVIGDTGNFRVGLPTVTATLRGMTMLRVRVDTLEGNLHSGQFGGAAPDALAALIRVLDSLRAEDGSTTVDGLAADSVWEGLAYDDEQFRRDARVLDGVELIGSGTVADRVWARPAVTVLGIDCPPVVGATPSVQASARALVSLRLPPGVDATAATKLLRAHLEARTPWGARVDVEQIGQGQAFRADTTSPAYRAMADAMAVAYPGEEMQYAGQGGSIPLCNTLAALYPQAEILLIGLSEPDAQIHAVNESVSPEELERLSVAEAHFLLNYAAS
>NZ_CP016795.1|WP_037762024.1|760567_761611_-|NUDIX-domain-containing-protein
MTVVWINGAFGAGKTTTARELIDLIPNSTLFDPEVVGGALAQLLPPKRLAEVGDFQDLPIWRRLVIDTAAAMLADLGGTLVVPMTLLRQEYRDEIFGGLAARRIDVRHVLLAPAETILRKRMARREIPDGLPDDGIRFRQWSHDHLEPYRSALASWLTADAHPVDTGALTPREAAARVAEAVGTGAVPACGIVQTPEPTGETVAAGVLLFDEQDRVLLVDPTYKPGWEFPGGVVEPGEAPARAGVREVAEETGIRLDDVPALLVVDWEPPAPPAYGGLRMLFDGGRLGSAGAGRVLLPGAELRAWRFVTEDEAADLLPPVRYERLRWALRARERGAALYLEAGTPVG
>NZ_CP016795.1|WP_031029491.1|761769_761964_-|hypothetical-protein
MKKRSMLALASLATGFVVAAVTPSHAAPSELPLGLDLQDTVSTVQDTVATDSLTLDEGSLGQLG
>NZ_CP016795.1|WP_031029494.1|762076_763030_-|ROK-family-protein
MHTDLVAALDIGGTKIAGALVDGDGRIQARAQRATPAREDGDTVMGAVEAVLAELTASPLWGRATAVGIGSAGPVDASAGTVSPVNVPGWRDYPLVRRVRAAAGDLPVELIGDGVAIAAAEHWHGAARGHDNALCMVVSTGVGGGLVLGGRLHPGPTGNAGHIGHISVDLDGDPCPCGARGCVERIASGPNIARRALEAGWLPGPDGDASAAAVAASARLGDPVAVASFERAAQALAAGIAATATLVEIDIAVVGGGVGKAGDVLFAPLRKALTDYATLSFVRRLAVVPAQTGTDAGLVGAAAAALTRTPGARTAHV
>NZ_CP016795.1|WP_079154857.1|763419_764496_+|LacI-family-transcriptional-regulator
MDDMTGHRIVPDTTRRAARTPGNRYGNRPTMKDVAARAGVGLKTVSRVVNGEPGVTPETERRVQEAIDALGFRRNDSARVLRKGRTASIGLVLEDLADPFYGPLSRAVEEVARAHGALLINGSSAEDPEREQELVLALCARRVDGLVVIPAGDDHRYLEPEVKAGVATVFVDRPAGQIDADVVVSDNFGGARDGVAHLIAHGHRRIGFIGDMPRIHTAAERLRGYRAAMEDAGITVQGSWMSLGVTDPERVRRAAEEMLAGPRPVTAIFTGNNRVTVTVVRVLAEHPPGAALVGFDDIELADLLRPGVTVVAQDAAALGRTAAERLFRQLDGTLLAPERIELPTRLVTRGSGELPPAL
>NZ_CP016795.1|WP_070387477.1|764673_765543_+|hypothetical-protein
MSRPSERDRGPERPPGEDRTLEALGLAGVPREEPLLYPGAWPRESGLLDGDRLLPLAGAVHDDGGGRVPVLAIGSNASPGQLRHKMAEFGIGSPVPMVRSRVTGLGIGVSAHVSRMGYVSASPVAAPGAVRELFVLWLDAEQLAVVDASEGVPVAGGNFDRAWLPAPDVRVEPGDGSVLRGAYAYVNRHGVLHDGTGTGAPRRHPGEQRPLIAGLLHGSARLRALFGTTPDEFCARARADRRLCDRGTRLFLEEERVTGSGLERYVGGGPDDPFAGARPPSAGPTGPTP
>NZ_CP016795.1|WP_070387478.1|765523_766822_-|aldolase
MGQQEKVATSLAGAVGEEISASLAPVDAELERRYPGDPGTRQPVHTVYVPGDAYAADTVRSWGDRALAALDEHAPDAASLAAVLGLADDLAEPVYARVRAKLEREPIEDLRIDFEDGYGGRTDAEEDEAAARAARLTAEAYELGTAAPYTGIRMKCMEAPVRARGIRTLDVFLSGLVEAGGLPDGLVLTLPKVTYPEQVTAMVRLLEAFEKARGLEAGRIGFEIQIETSQSILAADGTATVARLIQAAEGRATGLHYGTFDYSACLGVSAAHQASDHPAADHAKAVMQVAAAGTGVRVSDGSTNVLPVGPTPKVHDAWRLHYGLTRRALARAYYQGWDMHPGHLPTRYAAVFAFYREGFEQAAARLARYANRTGGDVMDEPATAKALSGYLLRGLDCGALDIGEVARLTGLTRADLESFSAPRRGDLTASAQ
>NZ_CP016795.1|WP_031029502.1|767001_767964_-|electron-transfer-flavoprotein-subunit-alpha/FixB-family-protein
MAEVLVYVDHVDGAVRKPTLELLTLARRVGEPVAVALGNGAGDTAAALAEHGAVKVLTSEAAEYADYLVVPKVDALQAAVGQVSPAAVLVPSSAEGKEIAARLALRLGSGIITDAVDLEAGDEGPVATQSVFAAAFSTKSRVSKGTPVITVKPNSAAVEPAPAAGAVEALAVTFSDAATGTKVTGRTPRESTGRPELTEAAIVVSGGRGVNGAENFAIIEALADSLGAAVGASRAAVDAGWYPHTNQVGQTGKSVSPQLYIASGISGAIQHRAGMQTSKTIVAINKDAEAPIFELVDYGVVGDLFDVVPQLTEEVKTRKG
>NZ_CP016795.1|WP_031029504.1|768019_768808_-|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein
MSLRIVVTVKYVPDATGDRHFADDLTVDRDDVDGLLSELDEYAVEQALQISENSDDDVEITVLTVGPEDAKDALRKALSMGADKAIHVEDDDLHGTDAIGTSLVLAKAVEKAGYDLVVSGMASTDGTMGIVPALLAERLGVPQVTLLSEVSVEGGTVKGRRDGDSATEQLEASLPAVVSVTDQSGEARYPSFKGIMAAKKKPVESWDLSDLEIDEDEVGLENAYTVVESAAERPARSAGTIVKDEGEGGKQLAEFLAGQKFV

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Crispr_ID: NZ_CP016795_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016795_2

1537010-1537140

Orphan

Consensus_repeat	Method
GGGCACCACGCGCGCGCGTGCGG	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP016795_2

>merge|NZ_CP016795|2|1537010-1537140|CRISPRCasFinder
GGGCACCACGCGCGCGCGTGCGGGCGCGCCGGGCACCACGCGCGCGCGTGCGAGCGCGCCGGGCACCCCGCGCGCGCGTGCGGAAGTAACGGAAGCAGCGGAAGAAACCTCCCGCACGCGCGCGCGTGCGG

>NZ_CP016795|2|2|1537010-1537140|CRISPRCasFinder
GGGCACCACGCGCGCGCGTGCGG	GCGCGCCGGGCACCACGCGCGCGCGTGCGAGCGCGCC
GGGCACCCCGCGCGCGCGTGCGG	AAGTAACGGAAGCAGCGGAAGAAAC
CTCCCGCACGCGCGCGCGTGCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016795.1\|WP_031047643.1\|1546977_1547745_-\|enoyl-ACP-reductase-FabI	unknown	unknown	gnl\|CDD\|236124
NZ_CP016795.1\|WP_037770590.1\|1544174_1544399_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031047577.1\|1528580_1529120_+\|YbhB/YbcL-family-Raf-kinase-inhibitor-like-protein	unknown	unknown	gnl\|CDD\|176643
NZ_CP016795.1\|WP_031047640.1\|1546201_1546879_+\|FadR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225097
NZ_CP016795.1\|WP_031047596.1\|1533967_1534609_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225107
NZ_CP016795.1\|WP_078536047.1\|1548631_1549132_-\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|340413
NZ_CP016795.1\|WP_070387734.1\|1539098_1541675_-\|FHA-domain-containing-protein	unknown	unknown	gnl\|CDD\|224054
NZ_CP016795.1\|WP_031047574.1\|1527747_1528530_+\|sporulation-protein	unknown	unknown	gnl\|CDD\|369195
NZ_CP016795.1\|WP_070387733.1\|1538276_1538975_+\|transglycosylase-SLT-domain-containing-protein	unknown	unknown	gnl\|CDD\|381605
NZ_CP016795.1\|WP_070387731.1\|1536012_1536708_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP016795.1\|WP_037770604.1\|1534601_1535780_-\|GAF-domain-containing-sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226951
NZ_CP016795.1\|WP_070387730.1\|1531159_1531591_-\|NfeD-family-protein	unknown	unknown	gnl\|CDD\|224501
NZ_CP016795.1\|WP_031047585.1\|1529978_1530920_-\|SPFH/Band-7/PHB-domain-protein	unknown	unknown	gnl\|CDD\|223407
NZ_CP016795.1\|WP_031047582.1\|1529320_1529827_+\|HNH-endonuclease	unknown	unknown	gnl\|CDD\|224321
NZ_CP016795.1\|WP_031047628.1\|1543562_1544081_-\|histidine-phosphatase-family-protein	unknown	unknown	gnl\|CDD\|224973
NZ_CP016795.1\|WP_031047646.1\|1547750_1548455_-\|3-oxoacyl-[acyl-carrier-protein]-reductase	unknown	unknown	gnl\|CDD\|273824
NZ_CP016795.1\|WP_031047593.1\|1533532_1533781_-\|chaplin	unknown	unknown	gnl\|CDD\|367652
NZ_CP016795.1\|WP_037770593.1\|1542233_1543478_+\|phosphoserine-phosphatase-SerB	unknown	unknown	gnl\|CDD\|319803
NZ_CP016795.1\|WP_037770609.1\|1531645_1532443_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224044
NZ_CP016795.1\|WP_070387735.1\|1544779_1545991_-\|CynX/NimT-family-MFS-transporter	unknown	unknown	gnl\|CDD\|129974

Protein	Function_ID	Function_description	E-value
NZ_CP016795.1\|WP_031047643.1\|1546977_1547745_-\|enoyl-ACP-reductase-FabI	gnl\|CDD\|236124	PRK07889, PRK07889, enoyl-[acyl-carrier-protein] reductase FabI.	1.18818e-172
NZ_CP016795.1\|WP_031047577.1\|1528580_1529120_+\|YbhB/YbcL-family-Raf-kinase-inhibitor-like-protein	gnl\|CDD\|176643	cd00865, PEBP_bact_arch, PhosphatidylEthanolamine-Binding Protein (PEBP) domain present in bacteria and archaea. PhosphatidylEthanolamine-Binding Proteins (PEBPs) are represented in all three major phylogenetic divisions (eukaryotes, bacteria, archaea). The members in this subgroup are present in bacterial and archaea. Members here include Escherichia coli YBHB and YBCL which are thought to regulate protein phosphorylation as well as Sulfolobus solfataricus SsCEI which inhibits serine proteases alpha-chymotrypsin and elastase. Although their overall structures are similar, the members of the PEBP family have very different substrates and oligomerization states (monomer/dimer/tetramer). In a few of the bacterial members present here the dimerization interface is proposed to form the ligand binding site, unlike in other PEBP members.	3.63889e-61
NZ_CP016795.1\|WP_031047640.1\|1546201_1546879_+\|FadR-family-transcriptional-regulator	gnl\|CDD\|225097	COG2186, FadR, Transcriptional regulators [Transcription].	1.72786e-50
NZ_CP016795.1\|WP_031047596.1\|1533967_1534609_-\|response-regulator-transcription-factor	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	1.04675e-81
NZ_CP016795.1\|WP_078536047.1\|1548631_1549132_-\|ATP-binding-protein	gnl\|CDD\|340413	cd16936, HATPase_RsbW-like, Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains. This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.	3.25819e-20
NZ_CP016795.1\|WP_070387734.1\|1539098_1541675_-\|FHA-domain-containing-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	2.93908e-75
NZ_CP016795.1\|WP_031047574.1\|1527747_1528530_+\|sporulation-protein	gnl\|CDD\|369195	pfam07070, Spo0M, SpoOM protein. This family consists of several bacterial SpoOM proteins which are thought to control sporulation in Bacillus subtilis.Spo0M exerts certain negative effects on sporulation and its gene expression is controlled by sigmaH.	2.62969e-110
NZ_CP016795.1\|WP_070387733.1\|1538276_1538975_+\|transglycosylase-SLT-domain-containing-protein	gnl\|CDD\|381605	cd13402, LT_TF-like, lytic transglycosylase-like domain of tail fiber-like proteins and similar domains. These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). LTs catalyze 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 to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.	5.61782e-32
NZ_CP016795.1\|WP_070387731.1\|1536012_1536708_+\|SDR-family-oxidoreductase	gnl\|CDD\|212491	cd05233, SDR_c, classical (c) SDRs. 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, 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.	1.46192e-40
NZ_CP016795.1\|WP_037770604.1\|1534601_1535780_-\|GAF-domain-containing-sensor-histidine-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.94364e-54
NZ_CP016795.1\|WP_070387730.1\|1531159_1531591_-\|NfeD-family-protein	gnl\|CDD\|224501	COG1585, COG1585, Membrane protein implicated in regulation of membrane protease activity [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion].	6.94238e-17
NZ_CP016795.1\|WP_031047585.1\|1529978_1530920_-\|SPFH/Band-7/PHB-domain-protein	gnl\|CDD\|223407	COG0330, HflC, Membrane protease subunits, stomatin/prohibitin homologs [Posttranslational modification, protein turnover, chaperones].	1.0241e-66
NZ_CP016795.1\|WP_031047582.1\|1529320_1529827_+\|HNH-endonuclease	gnl\|CDD\|224321	COG1403, McrA, Restriction endonuclease [Defense mechanisms].	8.79144e-18
NZ_CP016795.1\|WP_031047628.1\|1543562_1544081_-\|histidine-phosphatase-family-protein	gnl\|CDD\|224973	COG2062, SixA, Phosphohistidine phosphatase SixA [Signal transduction mechanisms].	1.72059e-46
NZ_CP016795.1\|WP_031047646.1\|1547750_1548455_-\|3-oxoacyl-[acyl-carrier-protein]-reductase	gnl\|CDD\|273824	TIGR01830, 3-oxoacyl-_reductase_FabG, 3-oxoacyl-(acyl-carrier-protein) reductase. This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis].	8.17042e-119
NZ_CP016795.1\|WP_031047593.1\|1533532_1533781_-\|chaplin	gnl\|CDD\|367652	pfam03777, DUF320, Small secreted domain (DUF320). Small domain found in a family of secreted streptomyces proteins. It occurs singly or as a pair. Many of the domains have two cysteines that may form a disulphide bridge.	5.26234e-17
NZ_CP016795.1\|WP_037770593.1\|1542233_1543478_+\|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.	3.24218e-92
NZ_CP016795.1\|WP_037770609.1\|1531645_1532443_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224044	COG1119, ModF, ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion transport and metabolism].	2.50626e-92
NZ_CP016795.1\|WP_070387735.1\|1544779_1545991_-\|CynX/NimT-family-MFS-transporter	gnl\|CDD\|129974	TIGR00896, Inner_membrane_transport_protein_YeaN, cyanate transporter. This family of proteins is involved in active transport of cyanate. The cyanate transporter in E.Coli is used to transport cyanate into the cell so it can be metabolized into ammonia and bicarbonate. This process is used to overcome the toxicity of environmental cyanate. [Transport and binding proteins, Other].	5.40328e-138

>NZ_CP016795.1|WP_070387731.1|1536012_1536708_+|SDR-family-oxidoreductase
MPVAIITGASKGLGRAFAEALAARGWDLVLDARDAEVLQGTATALEAYGARVTALPGDVTDAGHRAALVAGARLLGGVDLLVSNASALGAEPLVRLAELPLDGLRRALEVNVVAALGLVREALPSLRAAPAGAVLTVSSDAAAEAYETWGGYGASKAALDQLAAVLGAEEPGLRVWAVDPGDMATDLYAAAVPDDDDPRPDPVSVVPALLRLLDERPASGRYGAPALLEER
>NZ_CP016795.1|WP_037770604.1|1534601_1535780_-|GAF-domain-containing-sensor-histidine-kinase
MSHGPRSGLAAVSSALLAMSRHLEVRDVLKTIVASARELLDAQYAALGVPDDHGGFAQFVVDGVSDEQWKAIGPLPRQHGILAAMLHEATPERLADVRKDPRFGGWPSAHPDLVDFLGLPIRDGDEVIGALFLANKLRPEGQDPAHSPCPEPSGTCGFTPDDEELLGILAQHAAIALTNARLYERSRELTIAEERSRLAHELHDAVSQKLFSLRLTAQAATALVDRDPARAKGELHQVATLAAEAADELRAAVVELRPAALEEDGLVATLRTQIQVLDRAHAARVTFAGHGVKALPAAQEEALLRVAQEALHNALRHSGAAHVEVTLKRRDSGAVLRVTDDGGGFDPRAVRRAGRHLGLVSMRDRAGGTGGRLTVHSAPGEGTTIEMEVPGG
>NZ_CP016795.1|WP_031047596.1|1533967_1534609_-|response-regulator-transcription-factor
MADPIKVLLVDDHQVVRRGLRTFLEVQDDIEVVGEAADGAEGVDRAQELRPDVILMDVKMPGMDGVDALRRLRELDNDARVLVVTSFTEQRTVVPALRAGAAGYVYKDVDPDALAGAIRSVHAGHILLQPEVAGALLSQEESNSGPGRAGSLTEREREVLGLIADGRSNREIARALVLSEKTVKTHVSNILMKLDLADRTQAALWAVRHGVAG
>NZ_CP016795.1|WP_031047593.1|1533532_1533781_-|chaplin
MKNLKKAAAVSMVAGGLMVAGAGMASATDGGAHAHGEAIGSPGVASGNLVQAPIHIPVNAVGNSVNVIGVLNPAFGNLGLNH
>NZ_CP016795.1|WP_037770609.1|1531645_1532443_-|ABC-transporter-ATP-binding-protein
MSDVLELQDVSVVREGRALVDQVSWSVKEGERWVILGPNGAGKTTLLNVASSYLYPSNGTATILGETLGKPGTDVFELRPRIGVAGIAMADKLPKRQTVLQTVLTAAYGMTAGWQEEYEDIDERRARAFLDRLGMTEYLDRRFGTLSEGERKRTLIARALMTDPELLLLDEPAAGLDLGGREDLVRRLGRLARDPIAPSMIMVTHHVEEIAPGFTHVLMIRQGKVMAAGPLELELTSRNLSHCFGLPLVVEQAGDRWTAKGLPLS
>NZ_CP016795.1|WP_070387730.1|1531159_1531591_-|NfeD-family-protein
MNDIDAWVWWLVAAAALGIPLVVTAMPEFGMFGVGAIAAAVTAGLGAGVVAQVLVFVIVSVALIAVVRPIAARHRAQQPHMASGVDALKGRQAVVLERVDGSGGRIKLAGEVWSARALDTGRAFEAGEEVDVVEIDGATAVVM
>NZ_CP016795.1|WP_031047585.1|1529978_1530920_-|SPFH/Band-7/PHB-domain-protein
MEPVIIVLIILVVLVFIALIKTIQVIPQASAAIVERFGRYTRTLNAGLNIVVPFIDTIRNRIDLREQVVPFPPQPVITQDNLVVNIDTVIYYQVTDARAATYEVASYIQAIEQLTVTTLRNIIGGMDLERTLTSREEINAALRGVLDEATGKWGIRVNRVELKAIEPPTSIQDSMEKQMRADRDKRAAILQAEGVRQSEILRAEGEKQSQILRAEGEAKAAALRAEGEAQAVRTVFEAIHAGDPDQKLLSYQYLQMLPKIAEGDANKLWIVPSEIGDALKGLSGAMGNIPGLGGGNGGASVPAQERREKPSID
>NZ_CP016795.1|WP_031047582.1|1529320_1529827_+|HNH-endonuclease
MRDTLVLNASFEPLSTVTLNRAVVLVLQDKAVVEQAHPSLRMRGAALDIPAPRVIRLCQYVRVPFRRRAPWSRRGVLVRDRHRCAYCGRRATTVDHVVPRSHGGQDTWLNTVASCAQDNHRKANRTPEQAGMPLLRQPFEPTPADAMLLALARDDFAALPEWLALEAA
>NZ_CP016795.1|WP_031047577.1|1528580_1529120_+|YbhB/YbcL-family-Raf-kinase-inhibitor-like-protein
MTELKRRPLPHDFHPPVPSFTVTSEDVREGGTLKDAQVHAAGNTSPQLRWEGFPAETKSFAVTCYDPDAPTGSGFWHWVVFDIPASVTELPVGAGSGTFEGLPEGAVQARNDYGGKEFGGAAPPAGDGPHRYVFTVYAVDQEKLGPDADGTPAFVGFNLRFHTIARAQLIGEYEVPAEG
>NZ_CP016795.1|WP_031047574.1|1527747_1528530_+|sporulation-protein
MAFKKLLASLGAGGASVETVLSEVNVVPGGVVQGEVRIQGGEVDQEIQGLSVGLQAKVEVESGDQEYKQDIEFTKVQLGGAFQLQAGAVHAVPFGLEIPWETPITVIDGQSLRGMHIGVSTELAIARAVDSSDLDPVGVHPLPAQKAILDAFIQLGFRFKNADMERGHIRGTRQQLPFYQEIEFFPPQQYRGLNQVELSFVADAQAMDVVLEMDKKSGLFSEGSDTFRSFQVGLNDYQGTDWAAYLNQWLSEVGSKRNWF
>NZ_CP016795.1|WP_070387733.1|1538276_1538975_+|transglycosylase-SLT-domain-containing-protein
MLKNILPRGRSRSLNRTQKAAIAGVGTLGAAAVALTAVPASGQSTTSEAAPTAKVEYSTKQIKDVDAGVTGRLAGASQKVASIDAKKEAASNKATTAKKAVEKHETRKSTSRSAERTEVKKAAKSYPDNLDGWIREARAILSKHDIPGTYDGIHRNIIRESSGNPKAINDWDINAINGIPSKGLLQVIPPTFKAYHVPGTSWDIYDPVANIAAACNYAADKYGTMDNVDSAY
>NZ_CP016795.1|WP_070387734.1|1539098_1541675_-|FHA-domain-containing-protein
MPELVLESNGQTWTLDPSRSYALGRDPQGELVFDDARVSWRHATISFNGRSWVVEDHGSTNGTFVHGQRVQQMELGAGTVLNLGNATDGPRVSLTGAQAAVGTPQAQPQQQPYAAQGANAGWAQQAPVQEPPQQAAQHGHPHQAPQPGWQQQPQQQAAPQPQQAAAHFPQQQGPGGAAGAPPAHGDRSPTTFHQFSLGRVMRIGRALENELVVSDLQVSRNHAEFHATPDGRMEIRDLGSHNGTYVNGLPIAKGGSQLLGPTDIVGVGHSTFRIVGDRLEEFVDTGEVSFSARHLTVTVDGGKQILKDVSFGVPEKSLIAVIGPSGSGKSTLLKALTGYRPADQGEVLYDNRNLYKQFAELRQRIGLVPQDDILHKELTVKKALKYAAKLRFPADTTAAERDSRIDEVLRELKLDIHKDKKVTSLSGGQRKRVSVALELLTKPSLIFLDEPTSGLDPGMDRDVMQLLRGLADDGRTVLVVTHSVAELATCDKLLVMAPGGSVAYFGPPEEALNFFGYDTWADVFSAFENYRDYDWAGRWKGSQHYQMYAADIDAVAPQSVQVPAMQAMKPPKPQGWMSQFVTLVRRYVSVIVSDKGFLALTVILPAVLGAVSLLIDPDKGLLPNPANPQTGRIIPNGTATTVLLILAVGACFAGAANSVRELIKERVIYERERATGLSRSAYLMSKVFVLGTVTVLQGLLVGVIGFATREIPEEGLVLSGLPLVELSLPIMALGFTSMMFGLIISSLVKTAEKTMPLLVMFAIIQVVFTGCLFALNDAVGVNQFSYLMPSRWAVAAAGATLDFNKISPPEQGSEADPLWEHTVGAWGLDMAALIVLGVICGFFVARFLRRHEPEVMRK
>NZ_CP016795.1|WP_037770593.1|1542233_1543478_+|phosphoserine-phosphatase-SerB
MSATQTSDVPTLLVKIFGKDRPGITAALFDTLAAYSVDVVDIEQVVTRGRIVLCALVSEPPRGLEGDLRATVHSWAESLKLQAEIISGIGDNRPRGLGRSLVTVLGHPLTAEATAAIAARIAESGSNIDRIFRLAKYPVTAVEFAVSGAETEPLRTALATEAAALGVDIAVVAAGLHRRAQRLVVMDVDSTLIQDEVIELFAAHAGCEDKVAEVTAAAMRGELDFEQSLHARVALLAGLDASVVEKVRAEVRLTPGARTLIRTLKRLGYQVGVVSGGFTQVTDDLKERLGLDFAQANTLEIADGRLTGRVTGEIVDRAGKARLLRRFAAEAGVPLSQTVAIGDGANDLDMLNAAGLGVAFNAKPVVREAAHTAVNVPFLDTVLYLLGITREEVEAADTLDEDLGAGLGLPLDRV
>NZ_CP016795.1|WP_031047628.1|1543562_1544081_-|histidine-phosphatase-family-protein
MSVAEPRRIVLFRHAKADWPQVTDHERPLADRGRKDAAEAGRRLADTGVPFDQALCSTSARTRETWKLAVQEFPHRPKTVYEERIYEASPGELIAVLNETPDDLRNVLVIGHNPGMEGLAEILAGSAEDEARERMTGRGFPTAAFAVLTFTGDWKDVEPGRASLVDYWAPTD
>NZ_CP016795.1|WP_037770590.1|1544174_1544399_-|hypothetical-protein
MAVTTHTPPPRAPGADRTTGSGTETRLPWWALALPVLAFMTLLLLILNPADAQAAASPPGIVHLLEWLRQLILR
>NZ_CP016795.1|WP_070387735.1|1544779_1545991_-|CynX/NimT-family-MFS-transporter
MLMLGIVLAAFNLRPAITSLGALLEEVRDGLGMSGSVAGLLTSVPPLCFAVFGVTAPRLARRFGPGAVVWAGMVAITAGLLIRPYAGGTAGFLAATALALMGIAVSNVLMPVIVKRYFPDRVGSMTGLYSMALAFGTSIAAAATVPVTNALGGGWQPGLAVWATLGVAAVLAWIPFVRHREAPQSAPAPERTADTPGGRGAGPAPEQSPLRITRSRTAWALAVFFGLQATAAYITMGWMAQIFRDSGVSAGTAGLLLAVIMVMGVPLAFVIPRVATRLPHQGPIVLVLGLCGLAGYAGLYFAPVGGAWAWALLLGISNCAFPLALTMVGMRARTGAGVAQLSAFAQSTGYLISIPGPLLVGVLYQHSGGWGLPITLMCALMVPQIVVGVLAGRDRTVEDEAGR
>NZ_CP016795.1|WP_031047640.1|1546201_1546879_+|FadR-family-transcriptional-regulator
MPLSHPRRSALSEQVIAALRQQVASGEWPVGTRIPTEPELVEQLGVARNTVREAVRALAHNGLLDIRQGSGTYVVATSELAGVMQRRFADTDPRHIAELRSTLESAAARLAAERRTEKDLKQLDALLVRREEAFETGDTEAFVTADANFHLAVVAASHNDAMTAMYADLDEVMRDWLRGDVGSELTPDAHMDHTRLVDAIRAGDAETARREAADYPFLCRPGPVG
>NZ_CP016795.1|WP_031047643.1|1546977_1547745_-|enoyl-ACP-reductase-FabI
MSGILEGKRVLITGVLMESSIAFHAAKLAQEQGAEIILTAFPRPTLTERIAKKLPKPTKVIELDVTNDEHLGRLADVVGEELGGLDGVVHSIGFAPQDALGGNFLNTPFESVATAMHVSAYSLKSLTMACLPLMQNGGSVVGLTFDAQYAWPQYDWMGPAKAALEATSRYMARDLGKQKIRCNLVSAGPIGSMAAKSIPGFADLASVWDSRSPLEWDLKDPDPAGRGIVALLSDWFPKTTGEIIHVDGGLHAIGA
>NZ_CP016795.1|WP_031047646.1|1547750_1548455_-|3-oxoacyl-[acyl-carrier-protein]-reductase
MSRSVLVTGGNRGIGLAIARAFADAGDNVAITYRSGEPPEGFLAVKCDITDTEQVEQAYKEVEEAHGPVEVLIANAGINKDQLLMRMSEEDFTSVVETNLTGTFRVVKRANRGMLRAKKGRVVLISSVVGLLGSAGQANYAASKAAMVGFARSLARELGSRNLTFNVVAPGFVDTDMTRELSEEQQAKILAQVPLGRLARSEEIAATVRFLASDDASYITGAVIPVDGGLGMGH
>NZ_CP016795.1|WP_078536047.1|1548631_1549132_-|ATP-binding-protein
MFAQRFSATRRGARLARRLATHQLDLWHLPYDSPASDTITLVVSELAANAALHGCVPGRDFELRLVYDRSAGLVRVEVSDTHPELPAPTARPAADDEGGRGLLLVAAVADRWGVERRTGPGKTVWAECTVVKPVTVADRPGMPHCQVVEGVDPPALLLAEREDDRR

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Crispr_ID: NZ_CP016795_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016795_3

1880022-1880127

Orphan

Consensus_repeat	Method
GGGCTCGGCCGGGCGGTGGTCCGGCGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016795_3

>merge|NZ_CP016795|3|1880022-1880127|CRISPRCasFinder
AGGGCGGGCCGGGGGTGGGTCGTGCGGGCTCGGCCGGGCGGTGGTCCGGCGGGAGGGCGGGCCGGAGGTGGGTCGCATGGGCTCGGCCGCGCGGTGGTCCGGCGGG

>NZ_CP016795|3|3|1880022-1880127|CRISPRCasFinder
AGGGCGGGCCGGGGGTGGGTCGTGCGGG	CTCGGCCGGGCGGTGGTCCGGCGGGAGGGCGGGCCGGAGGTGGGTCGCAT
GGGCTCGGCCGCGCGGTGGTCCGGCGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016795.1\|WP_031030848.1\|1877069_1878023_-\|ROK-family-glucokinase	unknown	unknown	gnl\|CDD\|273246
NZ_CP016795.1\|WP_164711366.1\|1885803_1886148_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_070387857.1\|1890362_1891706_-\|RNA-binding-protein	unknown	unknown	gnl\|CDD\|377585
NZ_CP016795.1\|WP_079154888.1\|1871617_1872370_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225107
NZ_CP016795.1\|WP_031030820.1\|1891768_1892008_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_070387849.1\|1872362_1873613_-\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226951
NZ_CP016795.1\|WP_031030840.1\|1880272_1880707_-\|SRPBCC-family-protein	unknown	unknown	gnl\|CDD\|176861
NZ_CP016795.1\|WP_070387851.1\|1875380_1876067_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_037764447.1\|1881948_1883745_+\|long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|341233
NZ_CP016795.1\|WP_070387856.1\|1886459_1887659_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_037764426.1\|1869352_1870348_-\|2-hydroxyacid-dehydrogenase	unknown	unknown	gnl\|CDD\|240659
NZ_CP016795.1\|WP_107060424.1\|1892258_1892936_+\|rhomboid-family-intramembrane-serine-protease	unknown	unknown	gnl\|CDD\|366759
NZ_CP016795.1\|WP_070387854.1\|1880817_1881573_-\|metallophosphoesterase	unknown	unknown	gnl\|CDD\|277338
NZ_CP016795.1\|WP_070387848.1\|1870537_1871566_-\|6-phosphofructokinase	unknown	unknown	gnl\|CDD\|274155
NZ_CP016795.1\|WP_070387852.1\|1876208_1876973_-\|endonuclease	unknown	unknown	gnl\|CDD\|197318
NZ_CP016795.1\|WP_070390226.1\|1867526_1869401_+\|phenazine-specific-anthranilate-synthase	unknown	unknown	gnl\|CDD\|223225
NZ_CP016795.1\|WP_031030823.1\|1889061_1890105_-\|C40-family-peptidase	unknown	unknown	gnl\|CDD\|366353
NZ_CP016795.1\|WP_070387855.1\|1883791_1884934_-\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340831
NZ_CP016795.1\|WP_070387853.1\|1878715_1879936_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223082
NZ_CP016795.1\|WP_070387850.1\|1874584_1875388_+\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|224561

Protein	Function_ID	Function_description	E-value
NZ_CP016795.1\|WP_031030848.1\|1877069_1878023_-\|ROK-family-glucokinase	gnl\|CDD\|273246	TIGR00744, Glucokinase_Glucose_kinase., ROK family protein (putative glucokinase). This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General].	5.22534e-163
NZ_CP016795.1\|WP_070387857.1\|1890362_1891706_-\|RNA-binding-protein	gnl\|CDD\|377585	pfam05991, NYN_YacP, YacP-like NYN domain. This family consists of bacterial proteins related to YacP. This family is uncharacterized functionally, but it has been suggested that these proteins are nucleases due to them containing a NYN domain. NYN (for N4BP1, YacP-like Nuclease) domains were discovered by Anantharaman and Aravind. Based on gene neighborhoods it was suggested that the bacterial YacP proteins interact with the Ribonuclease III and TrmH methylase in a processome complex that catalyzes the maturation of rRNA and tRNA.	5.22033e-14
NZ_CP016795.1\|WP_079154888.1\|1871617_1872370_-\|response-regulator-transcription-factor	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	1.50375e-65
NZ_CP016795.1\|WP_070387849.1\|1872362_1873613_-\|sensor-histidine-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	3.6793e-23
NZ_CP016795.1\|WP_031030840.1\|1880272_1880707_-\|SRPBCC-family-protein	gnl\|CDD\|176861	cd07819, SRPBCC_2, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.	3.45551e-55
NZ_CP016795.1\|WP_037764447.1\|1881948_1883745_+\|long-chain-fatty-acid--CoA-ligase	gnl\|CDD\|341233	cd05907, VL_LC_FACS_like, Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases. This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.	0
NZ_CP016795.1\|WP_037764426.1\|1869352_1870348_-\|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.	5.08212e-172
NZ_CP016795.1\|WP_107060424.1\|1892258_1892936_+\|rhomboid-family-intramembrane-serine-protease	gnl\|CDD\|366759	pfam01694, Rhomboid, Rhomboid family. This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.	1.74424e-25
NZ_CP016795.1\|WP_070387854.1\|1880817_1881573_-\|metallophosphoesterase	gnl\|CDD\|277338	cd07392, MPP_PAE1087, Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain. PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	3.32216e-16
NZ_CP016795.1\|WP_070387848.1\|1870537_1871566_-\|6-phosphofructokinase	gnl\|CDD\|274155	TIGR02483, ATP-dependent_6-phosphofructokinase_1, phosphofructokinase. Members of this family that are characterized, save one, are phosphofructokinases dependent on pyrophosphate (EC 2.7.1.90) rather than ATP (EC 2.7.1.11). The exception is one of three phosphofructokinases from Streptomyces coelicolor. Family members are both bacterial and archaeal. [Energy metabolism, Glycolysis/gluconeogenesis].	0
NZ_CP016795.1\|WP_070387852.1\|1876208_1876973_-\|endonuclease	gnl\|CDD\|197318	cd09084, EEP-2, Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins.	6.06468e-20
NZ_CP016795.1\|WP_070390226.1\|1867526_1869401_+\|phenazine-specific-anthranilate-synthase	gnl\|CDD\|223225	COG0147, TrpE, Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism / Coenzyme metabolism].	7.19124e-57
NZ_CP016795.1\|WP_031030823.1\|1889061_1890105_-\|C40-family-peptidase	gnl\|CDD\|366353	pfam00877, NLPC_P60, NlpC/P60 family. The function of this domain is unknown. It is found in several lipoproteins.	1.35283e-32
NZ_CP016795.1\|WP_070387855.1\|1883791_1884934_-\|glycosyltransferase-family-4-protein	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	2.27824e-69
NZ_CP016795.1\|WP_070387853.1\|1878715_1879936_-\|hypothetical-protein	gnl\|CDD\|223082	COG0003, ArsA, Predicted ATPase involved in chromosome partitioning [Cell division and chromosome partitioning].	1.1487e-37
NZ_CP016795.1\|WP_070387850.1\|1874584_1875388_+\|alpha/beta-fold-hydrolase	gnl\|CDD\|224561	COG1647, COG1647, Esterase/lipase [General function prediction only].	2.68744e-40

>NZ_CP016795.1|WP_070387853.1|1878715_1879936_-|hypothetical-protein
MRTLLLTGPGGTGRTTLAAATALAAARQGTRTLLLGTDRDDTLGAALGMRTGPAPALVEPRLTVWRPDPAQGFRDGLAALQDRAASALDLLGAARLDPEELTPLPGADDLALLRALREAALAEAHDLLVVDLPAAPRALALLAAPEELRRCLRRLLPPERQAARALRPVLGRLAGVPLPTGALYETAARWELELAATEAVLADRNTVVRLVAEPGPAGADAVRTAALGLALRGLRTDLLVANRVLPEDVPADSWLGGPLAQQRKALAEWQGTYDVRTVPHLGRDPRGTDDLAALGAPGAVPDAAPGDRPGAVPGADAHAAPVEWTVTDRLAEDGVLVWSIPLPGAVREELDLVRRGDELAVAAGPFRRTVPLPSALRRCTVDGAALRGDTLTVRFTPDPGLWPRGR
>NZ_CP016795.1|WP_031030848.1|1877069_1878023_-|ROK-family-glucokinase
MGLTIGVDIGGTKIAAGVVDEEGNILSTHKVPTPTTPEAIVDAIASAVEGARVGHEIVAVGIGAAGYVNRQRSTVYFAPNIDWRQEPLKEKVEARVGLPVVVENDANAAAWGEYRFGGGKGHRNVICITLGTGLGGGIIIGNKLRRGHFGVAAEFGHIRMVPDGLLCGCGSQGCWEQYASGRALVRYAKQRANATPERAEVLLALGDGTPEGIEGKHISVAARQGCPVAVDSYRELARWAGAGLADLASLFDPSAFIVGGGLSDEGDLVLDPIRKSYKRWLVGGNWRPVADVIAAQLGNKAGLVGAADLAREPDPIM
>NZ_CP016795.1|WP_070387852.1|1876208_1876973_-|endonuclease
MATSSLSPLPNSRTEPDGSAVVRVLSYNVRSMRDDTDALARIVTACAPDLVLLQEAPRLFRWRKKITRLAAASGLVLLSGGGTAAGPALLCSLRATVERTGDVLLPLTPGRHRRGLAAAVVRIGGARLGVLSTHLSLSADERHEQAGLLLDHLAALGVTHAVAGGDLNEPPGGRTFRRLGEGLRDCWTAAPWGGEYTFPATAPDRRIDAVFVTEDVEVLGCGVPSGLPGVAEDDLRTATDHLPVLTALRVPATT
>NZ_CP016795.1|WP_070387851.1|1875380_1876067_+|hypothetical-protein
MAEHDSDREDREEREREHGEGGRERAADRGPEDGGTPVDEEAAWAAIVAGYGEEPPDPPGAKPFKSIEDLALLEPETNDMNGTASTTGTTGTTGPDGTDDADDEKPGADRSVPARPLGGSVAFAPGVGPRDHTPAEPSDDDFDADDEGHFVPPEPPPLPEGDTTSRFAWLGVLGGPVLLLLAVVLGWDMTWWLATLSIGGFLGGFATLVVRMRTGDEDDDDPGRGAVV
>NZ_CP016795.1|WP_070387850.1|1874584_1875388_+|alpha/beta-fold-hydrolase
MPVLPGAEPFRHEGGEVGVLLCHGFTGSPQSLRPWARYLAAHGLSVALPLLPGHGTRWQDLQVTGWQDWYAEVDRELRALRERCTRVFVAGLSMGGALALRLAAKHGDAVTGVVVVNPANRMHGVAQHALPVLRHLVPATKGIASDIAKPLGSELGYDRVPLHSAHSLRAFFRLADGDLPQVTQPLLLLRSPQDHVVPPADSARILGRVSSTDVTEILLEQSYHVATLDHDADRIFAESIAFIGRLAPGSVGEPESGLGKEGTAAGG
>NZ_CP016795.1|WP_070387849.1|1872362_1873613_-|sensor-histidine-kinase
MARRERVMRMSVEQPLWRALAGYRVLTMLYAIGFFATAYSGFERPWLAVAYYAVLSVWTLATLPKVANAASCTKRFLAADLTIALAGVLLTPFADAHDRVMDGGPTLPSIWTAGSVLAFAIKGGWRWAAAASTLVAVANLVERGTPARDTVHNVVLVWVASIAIGYVVEVARASERTLARALEIEAATRERERLARDIHDSVLQVLAMVQRRGAVIGGEAAELGRLAGEQEVALRTLVSGGLVPVSRVSEDTAEGAVVRAVEEPEGPEGEFPDGPVDLRALLAPYAGSLVNLAEPGAPVELDPASARELAAAVGAALDNVRRHVGERARAWILVEDEPGEVIVTVRDEGPGIPEGRLAEAEGEGRLGVALSIRGRLRDLGGTAELISVPGQGTEVELRAPKETGGVAARGKAADHG
>NZ_CP016795.1|WP_079154888.1|1871617_1872370_-|response-regulator-transcription-factor
MDEPRAPERQDPEGQNPKERDPARQDAERPDPIRVMVVDDHPMWRDAVARDLAESGFDVVATAGDGDQAVRRARAVTPDVLVLDLNLPGKPGVQVCKEVVGADPKLRVLVLSASGEHADVLEAVKSGATGYLLKSASTEELRDAVRRTAVGDPVFTPGLAGLVLGEYRRLASEPAPAAGGDEPGAPRLTDRETEVLRLVAKGLSYKQIAERLVISHRTVQNHVQNTLGKLQLHNRVELVRYAIERGLDDA
>NZ_CP016795.1|WP_070387848.1|1870537_1871566_-|6-phosphofructokinase
MKVGVLTGGGDCPGLNAVIRAAVRKGVQEYGYDFTGFRDGWRGPLEGDTVLLDIPAVRGILPRGGTVLGSSRTNPLQQEGGIRRIKDNLAELGVEALITIGGEDTLGVAACLAQEYGVPCVGVPKTIDNDLSATDYTFGFDTAVGIATEAIDRLHTTAESHMRVLVVEVMGRHAGWIALHSGLAGGANAILIPEQPFDVEQVCGWVTSRFRASYAPIVVVAEGAVPRDGDMVLKDESLDSYGHVRLSGVGEWLAKQIEKRTGKEARTTVLGHVQRGGTPSVFDRWLATRFGLHAIDCVRDGDFGKMVALRGTDIVRVPIADATARLKTVDPALYDEVGVFFG
>NZ_CP016795.1|WP_037764426.1|1869352_1870348_-|2-hydroxyacid-dehydrogenase
MEILAFGVQADEQPLIEQAFHGREEIRCVDVFLNEDTAPIAAGHEIVSTSVNADLGADVLEILAAGGTRMVAQRSTGFNNIDLATAERLDMTVARVSYYSPYSVAEFAWALAMAVNRRIVRAANRTRDFDFRLQGLMGRDLHGRTAGVLGTGKIGEAFARIAHGFGMRLLGWDVAENPACAELGMRYVPKDELLAQSDLITLHVPLMAETRHLIDAPALKAMRDDAILVNSSRGGLIDTVALVGELRAGRFAGVGLDVYEAEAGLFFLDKSLEPVEDDTLARLVTFPNVLVTSHQAYYTRDAVGQIVDATARNVLDYREGRRSENVLVPRG
>NZ_CP016795.1|WP_070390226.1|1867526_1869401_+|phenazine-specific-anthranilate-synthase
MTGPLAEPRPFALLRRRTPGRDHDTVELLLGPVAEYGSLADLPDDGLALVPFRQIRERGFDVRDDGTPLLALVPEERHEIPLAEALARLPAHEVRVEGGGFDVGDEEYARIVGRVLDEEIGAGEGANFVIRRTYGGRIDGFGRADALALFRRLLVGERGAYWTFVVHTGDRTLVGASPEVHVRMSGGTVVMNPISGTYRYPAEGPTPEDLLDFLADGKEIEELSMVVDEELKMMCTVGDRGGVVVGPRLKEMAHLAHTEYELRGRSSLDVREVLRETMFAATVTGSPVQNACRVIERHEAGGRGYYAGALALLGRDSGGAQTLDSPILIRTADIDAGGRLRVPVGATLVRGSDPAGEVAETHAKAAGVLAALGVRPSRPRAEGGRPGLADDPRVRAALDGRRASLAPFWLRMREPSDALAGRALVVDAEDTFTAMLAHVLRSSGLAVDVRRHDEPGLRAAVLGHEGPVVLGPGPGDPCDTADPRMRFLRRLTADVLREHRHGVLGVCLGHELIAAELGLNLVRREVPYQGAQTEIELFGRRETVGFYNSFTARCDDEAAAELAAHGVEVSRAAGGEVHALRGDGFAGVQFHPESVLTLNGAAIVRELAGQPRGTRTFSERRPSR
>NZ_CP016795.1|WP_031030840.1|1880272_1880707_-|SRPBCC-family-protein
MAEHTSSSITIDAAPADVMEVIADFARYPDWTGEVKEAQVLASDAQGRAEQVRLVMDAGAIKDDQTLAYTWTGEHEVSWTLVKSQMLRSLDGSYLLRAEGKGTEVTYRLTVDVKIPMLGMIKRKAEKVITDRALAGLKKRVETK
>NZ_CP016795.1|WP_070387854.1|1880817_1881573_-|metallophosphoesterase
MVSDVHGNARDLARAGEGADALVCLGDLILFLDYADHSRGIFPDLFGVENADRLVELRTARRFDEARELGSRLWSGVDGDKAQLIEGAVRRQYAELFAAFPTPTYATYGNVDMPPLWPEYAGPGTTVLDGERVEIGGRVFGFVGGGLRTPMRTPYEIGDEEYAAKIEAIGEVDVLCTHIPPQVPELVYDTVARRFERGSGALLDAIRRTRPRYALFGHVHQPLARRMRVGATECVNVGHFASTGRPWVMEW
>NZ_CP016795.1|WP_037764447.1|1881948_1883745_+|long-chain-fatty-acid--CoA-ligase
MREFSLPALYEVPADGNLTDIVRRNAAQHPDVAVIARKVGGAWQDVTARTFLAEVHSAARGLIASGVQPGDRVGLMSRTRYEWTLLDFAIWSAGAITVPVYETSSPEQVQWILGDSGATALVVESAEHAAAVESVRERLPALKNVWQIDAGAVEELGRLGQDVTDRAVEERGSIAKADDPATIVYTSGTTGRPKGCVLTHRSFFAECGNVVERLRPLFRTGECSVLLFLPLAHVFGRLVQVAPMIAPIKLGNVPDIKNLTDELAAFRPTLILGVPRVFEKVYNSARAKAQADGKGKIFDRAADTAIAYSKALDTPTGPSVGLRIKHKVFDKLVYGKLRTVLGGRGEYAISGGAPLGERLGHFFRGIGFTVLEGYGLTESCAATAFNPWDRQKIGTVGQPLPGSVVRIADDGEVLLHGEHLFKEYWNNPGATAEALADGWFHTGDIGTLDEDGYLRITGRKKEIIVTAGGKNVAPAVIEDRIRAHALVAECMVVGDGRPFVGALVTLDEEFLDRWCAEHGKPAGSTAAALREDPDLLAAVQGAIDDGNAAVSKAESVRKFRVLGSQFTEESGYLTPSLKLKRNVVAKDYADEIEAIYAK
>NZ_CP016795.1|WP_070387855.1|1883791_1884934_-|glycosyltransferase-family-4-protein
MRKTLIVTNDFPPRPGGIQAFLHNMALRLDPERLVVYASTWKRSREGVEATAAFDAEQPFTVVRDRKTMLLPTPGATRRAVGLLREHGCTSVWFGAAAPLGLMAPALRKAGAERLVATTHGHEAGWAQLPAARQLLRRIGESTDTITYLGEYTRSRIAGALTPEAAARMVQLPPGVDEKTFHPGSGGDEVRARLGLTERPVVVCVSRLVPRKGQDTLIRAMPRILAAEPDAVLLIVGGGPYEKDLRRLAHDTGVAASVHFTGAVPWPELPAHFGAGDVFAMPCRTRRGGLDVEGLGIVYLEASATGLPVVAGDSGGAPDAVLDGETGWVVRGEDPDETADRVTTLLADPELRRRMGERGRSWVEEKWRWDLLAEQLKTLL
>NZ_CP016795.1|WP_164711366.1|1885803_1886148_-|hypothetical-protein
MNSSTATKAASAAVCAANRERNDGERDDRDSGGRDSGGRDSDDSGGCGCGCGGWGCGCGGWGCGSGDRDLGDRGPGDRAALTRQSSSQPNAAALSPIETVLTVSTCGPRNSIDP
>NZ_CP016795.1|WP_070387856.1|1886459_1887659_-|hypothetical-protein
MAGRRRVSGSSVVALCLLLVALVACGGRPGADPVRADVQRLLDRRAAAVLAHDAAAYARTGTGTGTGFGNLSAIPVADWSYRVSEVDRAGDSATAEVELRYRVEGYDRGAVATARTLRLSRDGTGGQWSVDSERPAEKSGQQPWDQGAVEVVRGARSLVLGVGQSTAALRGYAGLADRAVPAVSDAWDGAWARRVVVVVPRSVEGMAGLLGSPASSYRGIAAVTTGETGGREHAPADRVIVNPDAYGLLGDLGKQVVLTHETTHVATRADTTSATPLWLSEGYADWVGYRDTARGPAQSAPELTRAVLDGGVPGRLPTDDDFGFTADADELARAYESGWLACRMIAAQWGEDRLNAFYRAVGAHDERAGAVEEAMDEVLGTTPEEFTRQWQDYLRTELG
>NZ_CP016795.1|WP_031030823.1|1889061_1890105_-|C40-family-peptidase
MASHRRPKQPSRTRVTVLTTAAAAAVALSSQAANAAPSEKPSKDEVKAKVDKLYEEAEQATEKYNGAKEKQEKLQKEVSTIQDNVARGQEDLNALRDGLGSMASAQYRSGGIDPSLQLFLSADPDDYLDKASTLDQLSGQQVEALKKIQEKQRELSQQRSEASEKLKDLSATRTELGNKKKQVQGKLSEAQKLLNTLTAQERAALKKEETQRATRAGERAGLGGSGTPASGRAAAAFAAAQSKIGTPYVYGATGPSSFDCSGLTSWAYAQAGVGIPRTSEAQTGAGTRISSMGDLQVGDLVFFFNDLHHVGLYAGNGQVLHAPRTGTVVRYESMSTIGGPFMFGVRV
>NZ_CP016795.1|WP_070387857.1|1890362_1891706_-|RNA-binding-protein
MVETQGGEPGDGAAEVLDRPLPDGVRRRVVQIVSDGFGSLTLGELPAQLRQYARFTPSRRVKFAGNAMAAAVETDPLFRGRIGDKLRDAQPELAGALDAGSPPPAADPLDVAAAAYVLRPHGWVKLVTAAGEEAQRADAERADDESRAELERLHEELARAREHTRAETERLRTELDAARRDTEALHRKLRSALSDVKRGEAALRKVQAEMDTVRAEGQTQVSAAESETRRLKARLGEAEAALEATRKAAREGRSVEDMRVRLLLDTLLDATQGLRRELALPPVSARPAETVDAVEPGRMTPKDIANRALSEHDPAVLDQLLALPQAHLVVDGYNVTKTGYPQMPLEKQRLRLLGQLSQLAAQTGAETTCVFDGAELAAPVLLAPPRGVRVLFSKPGVTADELIRQLVRAEPPGRPVIVVSTDREVADGVARAGARPVASVVLLKRVS
>NZ_CP016795.1|WP_031030820.1|1891768_1892008_-|hypothetical-protein
MTVPLPTDTTRWRCTLCGNLTRFDVTRASKVVEYVHLDLAGEPKVEEREVLSETIESVRCRWCNAVDQVELVDRPGAAS
>NZ_CP016795.1|WP_107060424.1|1892258_1892936_+|rhomboid-family-intramembrane-serine-protease
MTYTLITLCCLLFLISPAAGLNPAYGTGEELLAAQRAHFHRWGVIPAELFEDSPGSALTPATALFVHGSWVHLLGNMLFLYVFGAMTEERMGRLQFALFYLGCGYLALVGYAGANAHSQESLVGASGAISAVLGAFLFLFPHARVTSLLPFLFFLPLRFPAWLVLPFWAALQWMAAGRAGDGPGVAYLAHLVGFGLGFVFAWVRFGRTTRVESVPVAAPEGENQP

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Crispr_ID: NZ_CP016795_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016795_4

2234370-2234464

Orphan

Consensus_repeat	Method
TCCCAGGCCGAGGGCGAACGCGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016795_4

>merge|NZ_CP016795|4|2234370-2234464|CRISPRCasFinder
ACCCCGTCCCAGGCCGAGGGCGAACGCGACGAGGACCGGAACGGCAAGGCGGACGTGCCGCACAGCACTCCCTCCCAGGCGGAGGGCGAACGCGA

>NZ_CP016795|4|4|2234370-2234464|CRISPRCasFinder
ACCCCGTCCCAGGCCGAGGGCGA	ACGCGACGAGGACCGGAACGGCAAGGCGGACGTGCCGCACAGCACTCCC
TCCCAGGCGGAGGGCGAACGCGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016795.1\|WP_070387997.1\|2219987_2221445_+\|acyl-CoA-synthetase	unknown	unknown	gnl\|CDD\|236096
NZ_CP016795.1\|WP_079154905.1\|2226567_2231418_+\|protein-kinase	unknown	unknown	gnl\|CDD\|367616
NZ_CP016795.1\|WP_037765621.1\|2218484_2219900_+\|DeoR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|115789
NZ_CP016795.1\|WP_070387998.1\|2232665_2234171_+\|GAF-domain-containing-protein	unknown	unknown	gnl\|CDD\|226951
NZ_CP016795.1\|WP_037765618.1\|2216933_2217548_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_037765627.1\|2225527_2226568_+\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP016795.1\|WP_037765619.1\|2217569_2218277_-\|FadR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225097
NZ_CP016795.1\|WP_037765635.1\|2235847_2236324_+\|peptidoglycan-binding-protein	unknown	unknown	gnl\|CDD\|366659
NZ_CP016795.1\|WP_051159631.1\|2234547_2235621_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|236612
NZ_CP016795.1\|WP_031033810.1\|2231563_2232622_+\|rod-shape-determining-protein	unknown	unknown	gnl\|CDD\|336482
NZ_CP016795.1\|WP_070388003.1\|2275968_2276439_-\|type-VII-secretion-system-associated-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_079154904.1\|2223710_2225489_+\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379142
NZ_CP016795.1\|WP_070388002.1\|2271829_2275903_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372768
NZ_CP016795.1\|WP_031033824.1\|2270816_2271206_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031033838.1\|2276973_2277309_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223285
NZ_CP016795.1\|WP_031033835.1\|2276577_2276886_-\|WXG100-family-type-VII-secretion-target	unknown	unknown	gnl\|CDD\|274862
NZ_CP016795.1\|WP_070388004.1\|2277769_2279407_-\|type-VII-secretion-protein-EccB	unknown	unknown	gnl\|CDD\|368288
NZ_CP016795.1\|WP_070388000.1\|2236481_2237087_-\|SseB-family-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031033826.1\|2271207_2271663_-\|YbaB/EbfC-family-nucleoid-associated-protein	unknown	unknown	gnl\|CDD\|376829
NZ_CP016795.1\|WP_037765624.1\|2221437_2222808_+\|acetyl-CoA-carboxylase	unknown	unknown	gnl\|CDD\|223848

Protein	Function_ID	Function_description	E-value
NZ_CP016795.1\|WP_070387997.1\|2219987_2221445_+\|acyl-CoA-synthetase	gnl\|CDD\|236096	PRK07787, PRK07787, acyl-CoA synthetase; Validated.	0
NZ_CP016795.1\|WP_079154905.1\|2226567_2231418_+\|protein-kinase	gnl\|CDD\|367616	pfam03704, BTAD, Bacterial transcriptional activator domain. Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR, along with the C terminal region, is capable of independently directing actinorhodin production. This family contains TPR repeats.	1.44481e-27
NZ_CP016795.1\|WP_070388002.1\|2271829_2275903_-\|hypothetical-protein	gnl\|CDD\|372768	pfam13868, TPH, Trichohyalin-plectin-homology domain. This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.	2.47716e-28
NZ_CP016795.1\|WP_070387998.1\|2232665_2234171_+\|GAF-domain-containing-protein	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.3144e-15
NZ_CP016795.1\|WP_051159631.1\|2234547_2235621_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|236612	PRK09685, PRK09685, DNA-binding transcriptional activator FeaR; Provisional.	2.44865e-34
NZ_CP016795.1\|WP_037765627.1\|2225527_2226568_+\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	1.2165e-22
NZ_CP016795.1\|WP_037765619.1\|2217569_2218277_-\|FadR-family-transcriptional-regulator	gnl\|CDD\|225097	COG2186, FadR, Transcriptional regulators [Transcription].	2.2314e-52
NZ_CP016795.1\|WP_037765635.1\|2235847_2236324_+\|peptidoglycan-binding-protein	gnl\|CDD\|366659	pfam01471, PG_binding_1, Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.	3.60238e-07
NZ_CP016795.1\|WP_037765621.1\|2218484_2219900_+\|DeoR-family-transcriptional-regulator	gnl\|CDD\|115789	pfam07158, MatC_N, Dicarboxylate carrier protein MatC N-terminus. This family represents the N-terminal region of the bacterial dicarboxylate carrier protein MatC. The MatC protein is an integral membrane protein that could function as a malonate carrier.	3.54154e-60
NZ_CP016795.1\|WP_031033810.1\|2231563_2232622_+\|rod-shape-determining-protein	gnl\|CDD\|336482	pfam06723, MreB_Mbl, MreB/Mbl protein. This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.	4.03085e-148
NZ_CP016795.1\|WP_079154904.1\|2223710_2225489_+\|trypsin-like-peptidase-domain-containing-protein	gnl\|CDD\|379142	pfam13365, Trypsin_2, Trypsin-like peptidase domain. This family includes trypsin-like peptidase domains.	2.05856e-11
NZ_CP016795.1\|WP_031033838.1\|2276973_2277309_-\|hypothetical-protein	gnl\|CDD\|223285	COG0207, ThyA, Thymidylate synthase [Nucleotide transport and metabolism].	0.00204605
NZ_CP016795.1\|WP_031033835.1\|2276577_2276886_-\|WXG100-family-type-VII-secretion-target	gnl\|CDD\|274862	TIGR03930, WXG100_ESAT6, WXG100 family type VII secretion target. Members of this protein family include secretion targets for the two main variants of type VII secretion systems (T7SS), one found in the Actinobacteria, one found in the Firmicutes. This model was derived through iteration from pfam06013. The best characterized member of this family is ESAT-6 from Mycobacterium tuberculosis. Members of this family usually are ~100 amino acids in length but occasionally have a long C-terminal extension.	4.89821e-07
NZ_CP016795.1\|WP_070388004.1\|2277769_2279407_-\|type-VII-secretion-protein-EccB	gnl\|CDD\|368288	pfam05108, T7SS_ESX1_EccB, Type VII secretion system ESX-1, transport TM domain B. EccB is a family of largely Gram-positive bacterial transmembrane componenets of the type VII secretion system characterized in Mycobacterium tuberculosis, systems ESX1-5. Translocation of virulent peptides through the membranes is thought to be mediated via a complex that includes EccB, EccC, EccD, EccE, and MycP. EccB, EccC, EccD, and EccE form a stable complex in the mycobacterial cell envelope.	1.98997e-88
NZ_CP016795.1\|WP_031033826.1\|2271207_2271663_-\|YbaB/EbfC-family-nucleoid-associated-protein	gnl\|CDD\|376829	pfam02575, YbaB_DNA_bd, YbaB/EbfC DNA-binding family. This is a family of DNA-binding proteins. Members of this family form homodimers which bind DNA via a tweezer-like structure. The conformation of the DNA is changed when bound to these proteins. In bacteria, these proteins may play a role in DNA replication-recovery following DNA damage.	1.11967e-05
NZ_CP016795.1\|WP_037765624.1\|2221437_2222808_+\|acetyl-CoA-carboxylase	gnl\|CDD\|223848	COG0777, AccD, Acetyl-CoA carboxylase beta subunit [Lipid metabolism].	3.33642e-47

>NZ_CP016795.1|WP_070387998.1|2232665_2234171_+|GAF-domain-containing-protein
MTAQPAPRLTRLLEAVLAGTGTELDLPGTLRHIAEGAAELTGADRADLVVADPGRDSPTEIRAPAPGPGAPAGPQEGAPGLRVPILVGDEEFGELRLTGRPGAGPFTAEDEQLLRVLATQAGISIGNARLYETARQRERWIEGAAAVTTALLTEESADDALTTVAERARLLADASAGVILHPTAEGGMAIVTASTPDDPDGMLGATIEPGSPVLEQLLGGEPVFLTDSATDPRMTTHVRHRFGPSMMLPLQANGRLIGTLALPRRRGAHRYTDLERLLATQFASQAALALVLADARRGRERLAVYEDRDRIARDLHDLVVQRLFATGMMLESTERRRGAEDVRDILVRAVDELRSTVQEVRTTIFALQQPPAEPPTGLRGRVLRETAAAAARLGFAPSTRFSGAVDTRVPAPVADRLVTALRHALADACARSEVSRVEVAVDTAAPLADGRAGVRLTVFDDGAGGGAEDGAKTDGRDGDEPDGDGGGYRGAGTTVTWWSPL
>NZ_CP016795.1|WP_031033810.1|2231563_2232622_+|rod-shape-determining-protein
MTASTASTASLEALRRCHFAVDLGAARTRVYVKGVGLVVDQPSAAAVNTRTGALIAVGEFAERMTGRTPGYIRVVRPVSGGTVVDIEMAQRMLRHLLGDRVRRALRRKPRLRAAVCTPHDADPLSQRAAIETLVGLGARRVELVDTLIAAAVGCGLPVEQPEATMIMVCGKHATQVAVLSLGSIVTAVRIPVGGEAVDHAIVQLLRHQHELVLPSQSVRPLQLALAGNGLTPQGPSSTEIHGRDVATGLARSVRVDTATVRNAIQTPLTAVLDGIGKVLRDCPPDLVADLADRGIMMVGGSALLPGFDQMLRQSTGMPVHIAERPDVCAVQGLGSMLEGRVEPLVLHPTAAD
>NZ_CP016795.1|WP_079154905.1|2226567_2231418_+|protein-kinase
MPADRPGPPDPLPHLADILGRASSGARPTPLELAELLWLAGQMTPAPDPPDGPAADGTVPEAAAGTFPPPDPVRRPAPDRDLDRDRHHRHGPGREQGQGRDSGQDRPVPGPPPAADAPGTPLRLPSSTMPAPGTSAAEPHSALLAPAPPMLRHTLALQRSLRPLKRRTAAPVGHEVDESATADRIARLGGGPEWWLPVLRPVRERWLRLHLVHDAGPTMPVWQPLVRELHDALAQSGVFRTVVLHRADADGTVGGDGFQAPADGRTVTLLISDCMGPQWREGEAGTRWFGTLRRWARHTPLAVLQPLPERLWRDTALPPVPGRLSAPHRAAPSSSLAFTPYDDTAPPAPRGAVSVPVLEPGPRWLANWAALVASPGGTTHPGAAATLHRPLPADADDRTDLARLSPEDLVLRFRARASREAFRLAGHLALGRPDLPVMRLVQAAVEPDPRPQHLAEVILSGLLTAVAGPPGSYAFRPGVRDLLLRGLPRTARNRTHELLLRTGGLIDERAGRSPGEFRALIPSRGGTERADGGETFAVISEDSARQLGVPARPGAPSPFPRALGDRYRPVRRLAPTGRVWLAEDTGAGRTVAVRLHDRLPGAAGAAARRAFLRDARRLTEFTHPNVVAVLDAGVEDDVPYVVMEHLDGIAVNALARAGEGRLPAPLTVSLAAQLARALTALHRAGLTHGGVEASRLVLLPDGTVRLSLLEPGLSSGRAGRSADLRALCAVLLELCAGTSRLTVPIDSRRLDRLPADLRIDYAHAFDQLMSMDPSAQARGLDLLTDPRLLATAEETYTPRRYRALGPLRVTLPDGSPALPPDERALLTMLLLKHGRTVTHEELRYGLWAPGDEPRDPRRELIRLAARLAEVLGPGVLATPSHGYALHTSADHVDLVHCDELVRRADAARLAGALTEARDLVTEALSLWHGSEPLTGVPGWGAHTARARLLRLRLALHTRRAELDLSLGDYDRASADLAGLLRAHPHREDFRRLYLIALRRQGRGAEALEVYEEYELSGGRSPALTALGRELREEHAGPVDDAPWSEYEDTPDAPDTSPDAGADARHGALSAPDELPEGPFPTEDDFWAWPPEEREEPERHAAEATDGELVGAWGNPRAEDSGPHLPEEEYADADEGPAAERGPGAGPEDEAADAGLDTDYRNCARYSLADGRHGDRDRAAALHVLVSHLLAESGLDGAAYELLDDRDGLLVLLAPRVEAVPLLRATVAGLPGQLARLGGARLRAEFWQVEFQLDGAQEVQSLRADAESVAAVLDASAAQAVVALSDSLYYDEVYDQEGPDGLLLPPGLFRPLADDTGWYRLIDEGTGEESDGGTGGEPEPTTAPEPAREPAPAPDGGPVRGASPLPPGGRPPLPAGSRPRAVAPRSPADLVSGARCVLLGFDDVLARLYRPAAEREVLLDVLRLFADERDPEDALAGLPLPRAATDGYAGTLDFVRALAGHRLDPDVRLRLDRHEARAARTARPVPLADRLIQALDTRGVPVAVVTDRAPGPVTSYLRRRGLLECLRGDVHGRDTDLTRLMPDPDVLHRALERLDADAGDCVLVGSSVAEQAAARAAGLPFVGRYGDEPARRRLTGADGDALLVPDLRPLLTAAENR
>NZ_CP016795.1|WP_037765627.1|2225527_2226568_+|MoxR-family-ATPase
MPLWPVYTGAPAPHDGITRLPPPPPWRAFEGEPVLDPPAEDTDDPGASPDRAQQATAHRATTYQATEDTVQLVNAALYLRRPLLVTGPPGTGKSSLAYAVARELGLGPVLRWNITSRSTLHDGLYTYDPLSRLYAARHATGLPGAPAAATGIEDHLRLGPLGTALLPYARPRALLIDEIDKSDLDLPNDLLHVLEEGQYEIPELVRAARDVPGGRAEVLIDGTDRRVPVERGRVRCREFPFVVLTSNGEREFPPAFLRRCVSLRLRQPEGHHLAEIVRAHLGEPDAYAQQLIQRFLSRVGSGELATDQLLNAIYLARSSGLGADSLDGLAEQLMPYLGRSPQADAF
>NZ_CP016795.1|WP_079154904.1|2223710_2225489_+|trypsin-like-peptidase-domain-containing-protein
MSGAAWHARVACGPEVGAGFLVSGRRLLTCAHVVKWADRAPVTVSFPGRRELGALSAAVAVHGGWQGGAADPGDLAVLELEREVPLTPASFAPPGAERGAPAPDLIAYGFPKGYDEGMLASYRAQPGPLISDEWVQLEAVTAHGQPLAAGFSGAALALADGTVVGMVSAVAGARDVRVGRMLPVEVMARYWPELGELVPTPGHRADVRRRLYALVREAEETGLSCDPKRLYASATDGFDPPPPDGGFAGLREAAAYVQWEVPEPGVVSRFADRLEELLHAPPPRPAAWSPIVVEIDRSGAGADQVTVEVSAYRDGQRHPVDARRLARGAVRAFVQERIDEAFTRLDPGADELLTFVLPREWLNEPVAHWECGEDDSTPLGCAYPLVVTDRHRHRSGRLRHQLRKKWRRLGASGGGTLQRVDCGTGERPAGLRKRLREDAELAGFATAPTVAREHFEVGLTVPVPVLMWPRRGCPGDPHEGPCPGSAFLDELAVSVADVPPSELPRHVMELRETADAADEPDAHWARDLQLLWDDPRCFADPTAALHSPVSPAPPVSPFPPTSPAPSASPTSPVPPGSPISPGSPISPVSPVR
>NZ_CP016795.1|WP_037765624.1|2221437_2222808_+|acetyl-CoA-carboxylase
MGERRSAREFLALVTDDFTELPAPRGEQDPDGPLGWPGYGAARARAADRTGEEESVVCGTGHVEGVRAVLLAFEFGFLGGSLGRRTGDRLEAAYAYARAHRLPVVPLVATGGSRMQEGMLALTQLQRVARQSVLTRRAGLPQVAVVRDPATGGGWATLGSGADVVLALPGAQVGFAGSRVRPPDADPAAYTAEAQVAAGSADAVVPEVELRSTLGRWLRLLTAPSGDPAPVPAPLGARDLPADGWDAVRRARAAGRPRAGAYLDAYFGERVALSGDRCGGADPEGMLCGFGTHAGRTVAYAAQTGTATRPAGYRTATRLIHLADRLGIPVLTLVDTPGAAGDAAAEGQAVGPAIADLFGAVASVRTPVSTLVIGEGGSGGALALAAPGATWATPDSYFSVIAPELAAAILKRPPAQVRLTADQLRLRPQDLAELDVIRTDEQVFPGTGDRRSEGRM
>NZ_CP016795.1|WP_070387997.1|2219987_2221445_+|acyl-CoA-synthetase
MSSLFPALSPAPSGARAGRPALRFGERSLTYAELAAAAGASAGRIGSAGRVSVWATPAMETAVAVVAALLAGVSAVPLNPKSGDKELAHILSDSGPSLVLAPPGAELPPALGTLERVDVDVDARGPVPEERADDGDPALVVYTSGTTGPPKGAVIPRRALSSTLDALADAWQWTGEDVLVQGLPLFHVHGLVLGILGPLRRGGSVRHLGRFSTEGAARELNGGATMLFGVPTMYHRIAETLPGDPELTKALAGARLLVSGSAALPVHDHERIAAATGRRVVERYGMTETLMNTSVRADGEPRAGAVGVPLPGVELRLVEEDGTPIAALDGESVGEIQVRGPNLFTEYLNRPDATAAAFTEDGFFRTGDMAVRDPDGYVRIVGRKATDLIKSGGYKIGAGEIENALLEHPAVREAAVTGEPDPDLGERIVAWIVPADPAAPPALETLADHVAGRLAPHKRPRVVRHVEALPRNDMGKIMKRALTHG
>NZ_CP016795.1|WP_037765621.1|2218484_2219900_+|DeoR-family-transcriptional-regulator
MSPELISILVLVVVFVIATTRSVNMGALAFAAAFGVGTLVADLDADGIFAGFPGDLFVVLVGVTYLFAIARANGTTDWLVHASVRLVRGRVALIPWVMFALTGALTAIGAVSPAAVAIVAPIALSFATRYGISPLLMGTMVVHGAQAGGFSPISIYGSIVNGIVEREKLPGSEVGLFFASLVANLLIAAVLFAVLGGRKLWAQGAVPDGGDADGTGDGGGSSGSGDAKSTGESTGETTGTGTGGVTGTASSPGPTAVAVRPEPGVGGGLGGTVLNPARIATLVALVALVVAVLGFDLDAGLTAVTLAVVLSAAWPDDSRRAVGEIAWSTVLLICGVLTYVGVLEEMGTITWAGEGVGGIGVPLLAAVLLCYIGAIVSAFASSVGIMGALIPLAVPFLAQGEIGAVGMVAALAVSATVVDVSPFSTNGALVLAAAPDVDRDRFFRQLMVYGGIVVAVVPALVWLVLVVPGFG
>NZ_CP016795.1|WP_037765619.1|2217569_2218277_-|FadR-family-transcriptional-regulator
MSDALRPMPRQRLYEQVLERLRQYVTEGGLRAGDRLPPERDLAQRLGVSRASVKQAIVVLEVQGLVEARHGGGTYLVRDSLDSEPVEDMVERRRRLPDVLEAREALETKLAELAAERRTEDDLSAMRAALAVMAEEIGRGAHGVEGDRLFHASVTAAAHSSLLAEFMRSIAHQIAESRTESLRQPGRPDRSLAQHRAILDAIAAREPRQAAAAMRRHVRTVAKVRLLDWDPGDER
>NZ_CP016795.1|WP_037765618.1|2216933_2217548_+|hypothetical-protein
MPTGKRPAGPFTPRDFQLVLLRRMADHNPGPVEDARRELGASVADMREANRRWQAMLHSPGSRSAAARYRSVLGEPESVAPRRVGDLRCEARQWALPLWPDLRFEVLVADRGAVWNEWLVRAPGARGPELRTLDDLAPWSCTVDEAARAFAPARPLQGSAPTRWGLALTAPDRTGVRHEVVAEFTWGLLQRTAVGGREQGPPGG
>NZ_CP016795.1|WP_051159631.1|2234547_2235621_-|helix-turn-helix-domain-containing-protein
MEGTDQRGNASGRGRTAAGAGRGAVLDASVVAPREREDTIRHALWASFSRVDIDHHTSQEDIGARMGLGAVGPMKVCSAQGTPVSLRRTERLAREDHEPSVFLGLQVSGTNMVGQHGRQCLVGPGNLVVFESTAPYTLRFEERFGYLSLRIPREALALPERVLREAAAVTLGPGNPTARLAFTYFSQLAASEELRGGAHAEALVGPSVELLRAVVTSQLGDAGAGRALPEVPLGMRVTQYVRAHLADPDLSAQRIAAAHGVSVRHLYNVLSRSGISLGDWIRTRRLAECRRELAGPGARTRTIAAIGRRWGFVDATHFSKAFKQAYGMSPRAWRELHQPGPARPRRPARRRVDVPAG
>NZ_CP016795.1|WP_037765635.1|2235847_2236324_+|peptidoglycan-binding-protein
MRTALTRTFVGAATVFAIAAGSLAGATVSSAASEPAARPAAGTREVSVLAVTNLGLTVGRAKSWQCFLTRSGYEPWEHAGLLGTDSWKAAQRMFNARGFSGKSKLVVDGVVGPLTIKALQRFLNDFGFGLAVDGIAGKRTSAAFYEFNGVPMPNDPRC
>NZ_CP016795.1|WP_070388000.1|2236481_2237087_-|SseB-family-protein
MSESGAETPAAANPLDPAPPQEYVEAARLAPDHWLYLPDPAWRGEGPPPDWAVVGQWRSDADGTIVEWEDNPEYRPSPEAMGWPEPADAVDRAIQLATTGYGPAEDVTAALAGAEVAVLVTADGEPVRASAPDGTPAVPVYTSARYLHAAGRLASAHLPVSTLLTRVPPDHALYLNSNAPVGMVLPTQGLADLLEEEPRPQ
>NZ_CP016795.1|WP_031033824.1|2270816_2271206_-|hypothetical-protein
MGQRYYVDPARIEALSGQLEEIATLARSMTEEFLDGLAPTVSWPGTSGDFAEKAKPQEQKERQTTKDTMMSIRDALVSITDATLSQVKLMEDTRDRNLEDIERNTSRIETDGFGLDGSGGGDTGGHGRH
>NZ_CP016795.1|WP_031033826.1|2271207_2271663_-|YbaB/EbfC-family-nucleoid-associated-protein
MTEPLEQRLEKAMAELRSAQEAVERTERELRQASFAVLSSDRAVRATVGPQGELTGLDFLEYKYRDMSPQELAASVLEAASAAREKMNRHVMKAMAPFAEPSSEVPELKGFELDWERIFGPGVLEKADQDTDRTDGAAPGWRDALGEDGED
>NZ_CP016795.1|WP_070388002.1|2271829_2275903_-|hypothetical-protein
MVDRYDADSIDNVNKYEGATDASSDVWAGLVTHITGYPVPDRSTVFDTLRSDHGGKLFRMDIRDRGLGSFVQDASGFLRNTGEDYDIWFFDSGKKTQIKQARIVFEGRVKAGDEVIWADPGTDDVANASVREGNEFKDYNKDEMSTVALARYMNGPRTALLELLGGNTADARFSNLGVAEDSSVDLNSFNTTGQTFDFAAQFFRDQGPKIKEWEEALGREDASWKGEAAEVFRSLLTKIRENYDAYIETFDEKPSTGEGDGTGKTVYSRALSQARSALEDAADKLLDAWITWANSDYYDPHRVLRYVLDDLAQWVDSNNVAKTDIKTTYSAYSSSTYHDPQEGFSQNHPEYGDLTDIANWAKVGDKAVQIWSRGVDEHLVKPARTVQSNLNNTFLDLGGDFSENIPEPKSTSTASQEYEERKAEEAQEEIERQNEENRRYQDELREEQEKQREEDRKYQEELREEQRQQREEDKQAQDELREEQNRQREEDKQAQDELREEQNRQREEDRKYQDELRAEQEKQADEAQEQLRTLNDPTTTDLGGLDDLLNRDVPVTESLGDMGGLNGGPGGGDTALTESLGDLGGVNGGPGGGPGTDDLGNFGDANNAANQSLAGLGGTGGGDQPAAVPPPTNLGSLGGLNSGGGTRLPTERTPGLVDGNPVAQFPDGSSTSFDPDTGLLTSTAPDGSTTTTDLGNGLQVTNPDGSVTSLGDDGNLKTTFPDGRTETIDPSTGQAVTTNPDGTTTTTDLGSLGGLNNGAGGGTLDMPTGGSTQLSGGDLTSRFPDGSSTSFDPDTGTLTTTGPDGSTTTTDLGNGLEVTNPDGSVTSLGDDGNLKTTFPDGTTQSIDPSTGQAVTTNPDGTTTTTDLGSLGGLNNGAGGGTLDMPTGGSTQLSGGDLTSRFPDGSSTSFDPDTGTLTTTGPDGSTTTTDLGNGLEVTNPDGSVTSLGDDGNLKTTFPDGTTQSIDPSTGQAVTTNPDGTTTTTDLGSLGGLNGQGNQGGLDSLGDLQTQSNGDLGGLGDLDLGSLDGLNSGGGSGLETPTGGDTSLAGDDLLTRFPDGTRATFDTQTGMLTATNPDGSVTTTDLTHGAQVTNPDGSVTSLDNGMLTTDFPDGSTQVVDPETGIATVTDAQGNTETVNLHDLNTGNGPTSSNGNGLLDELGSLDGLGGSGGTGGGGTSTETLSPSDLGLGNGGSLTSGTGGGLTAGASVGSDGLLTGAAAPLSDSATAAGGTPLAPAAGAGTAGAPGMPGTPGMPMGGMGGMGGGGDKGNGERVRAVLVDAAEESERRNRRRRSPWNRQEDSDTFLSPASRVATTGGDDSSGEEPGQGRGVTTSADYLEEDADVWGTEDGGTPAVIGR
>NZ_CP016795.1|WP_070388003.1|2275968_2276439_-|type-VII-secretion-system-associated-protein
MADNPTDIKHFDLSAMENFRDYEVDRAYKDAKRHREGGGDGDPRTLGDLIDGHTTEDNLDQSQQLLRIGKMASDGRVSGPKLLEGVREAATALDKLLGDQIDLYKELQDALTDTIEGAQKTQAKNLDAIDAQTLLQHFDEVDTLTAGGSGGEDSDS
>NZ_CP016795.1|WP_031033835.1|2276577_2276886_-|WXG100-family-type-VII-secretion-target
MADGIIDVQYPVVRRAVEEMTEQTQQIINALNNLEDELKPLVASWEGSDQEMYRQVQMEWDQATKNMATLLNDNGTLIQSIHDNHSRDERRSADNWGNVRAR
>NZ_CP016795.1|WP_031033838.1|2276973_2277309_-|hypothetical-protein
MADSAARKADYAKGLGGVSSLESARSQVEKIQNNVAEIAARSGVGGDEGQALLKLFRSWNTEAQTVVVQISKMIDALQENVTSANRLAQENQDLTEVLNSKTSQGVFQALL
>NZ_CP016795.1|WP_070388004.1|2277769_2279407_-|type-VII-secretion-protein-EccB
MQSKRDQVQAHSFMMGRLSSGLLTAAPDAPESPLGRTTRGVVFGLLFTVLIGAGTVVYGLLRPGGNDGWRDGGHLVVNRDTGARYLWTDTDGVLHPVRNYTSARLIGGSDLPTEDVGTASLRDVPVGGPVGIPGAPDGLPDAGQLDGGAWNMCVTGPDGADPSTSGAAAAPAVDAAGATTLVVGAPVDSAAVGRDRGVLVSGPDKTQYLVWRGSRLPLDEKSDARTALGYGSVSAAPVSAAFLDALAPGPELRSPDVPGRGGEGPELGGEATRVGQVFEVSVPGGESTYHLLREEGLVPLTRLGAALVLGDPATQKDAYRGESPEARTVGADALREHQAEGAGGDEAAGLPDAPPAPQSVPRGSALCAQVDGGDGGARIGSVLAPLTELAPVAVPEGTADPVREACVPTDATVVRPGHGALVRALHASGAAHAGTTYLVAENGVKYRVPADDSLQALGYTTGDIDSVPAPLLAALPTGADLDPDAASGAAEVRVTAPDCGTDAQQEEAAPGKKAKAASFVTGDPAAAPGTADTALQTRQDGQSEF

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Crispr_ID: NZ_CP016795_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016795_5

2257647-2257742

Orphan

Consensus_repeat	Method
GGCGTCGTCGGTGAACCGGAACCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016795_5

>merge|NZ_CP016795|5|2257647-2257742|CRISPRCasFinder
GGCGTCGTCGGTGAACCGGAACCGGGCGAGCCGCTCGGCGGCGGAGGGGTCGGACGGGTCGGAGGGGTCGGAGGGGTCGTCGGTGAACCGGAACCG

>NZ_CP016795|5|5|2257647-2257742|CRISPRCasFinder
GGCGTCGTCGGTGAACCGGAACCG	GGCGAGCCGCTCGGCGGCGGAGGGGTCGGACGGGTCGGAGGGGTCGGA
GGGGTCGTCGGTGAACCGGAACCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016795.1\|WP_070388006.1\|2285968_2287270_-\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|274856
NZ_CP016795.1\|WP_079154904.1\|2223710_2225489_+\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379142
NZ_CP016795.1\|WP_079154905.1\|2226567_2231418_+\|protein-kinase	unknown	unknown	gnl\|CDD\|367616
NZ_CP016795.1\|WP_070388002.1\|2271829_2275903_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372768
NZ_CP016795.1\|WP_070387998.1\|2232665_2234171_+\|GAF-domain-containing-protein	unknown	unknown	gnl\|CDD\|226951
NZ_CP016795.1\|WP_051159631.1\|2234547_2235621_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|236612
NZ_CP016795.1\|WP_037765627.1\|2225527_2226568_+\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP016795.1\|WP_031033835.1\|2276577_2276886_-\|WXG100-family-type-VII-secretion-target	unknown	unknown	gnl\|CDD\|274862
NZ_CP016795.1\|WP_037765635.1\|2235847_2236324_+\|peptidoglycan-binding-protein	unknown	unknown	gnl\|CDD\|366659
NZ_CP016795.1\|WP_031033810.1\|2231563_2232622_+\|rod-shape-determining-protein	unknown	unknown	gnl\|CDD\|336482
NZ_CP016795.1\|WP_070388003.1\|2275968_2276439_-\|type-VII-secretion-system-associated-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_164711384.1\|2234357_2234504_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031033838.1\|2276973_2277309_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223285
NZ_CP016795.1\|WP_031033824.1\|2270816_2271206_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_070388004.1\|2277769_2279407_-\|type-VII-secretion-protein-EccB	unknown	unknown	gnl\|CDD\|368288
NZ_CP016795.1\|WP_070388005.1\|2281613_2285660_+\|type-VII-secretion-protein-EccCa	unknown	unknown	gnl\|CDD\|274858
NZ_CP016795.1\|WP_070388000.1\|2236481_2237087_-\|SseB-family-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031033826.1\|2271207_2271663_-\|YbaB/EbfC-family-nucleoid-associated-protein	unknown	unknown	gnl\|CDD\|376829
NZ_CP016795.1\|WP_031033845.1\|2279746_2281153_-\|type-VII-secretion-integral-membrane-protein-EccD	unknown	unknown	gnl\|CDD\|274855
NZ_CP016795.1\|WP_037765624.1\|2221437_2222808_+\|acetyl-CoA-carboxylase	unknown	unknown	gnl\|CDD\|223848

Protein	Function_ID	Function_description	E-value
NZ_CP016795.1\|WP_070388005.1\|2281613_2285660_+\|type-VII-secretion-protein-EccCa	gnl\|CDD\|274858	TIGR03924, T7SS_EccC_a, type VII secretion protein EccCa. This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking].	0
NZ_CP016795.1\|WP_079154905.1\|2226567_2231418_+\|protein-kinase	gnl\|CDD\|367616	pfam03704, BTAD, Bacterial transcriptional activator domain. Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR, along with the C terminal region, is capable of independently directing actinorhodin production. This family contains TPR repeats.	1.44481e-27
NZ_CP016795.1\|WP_070388002.1\|2271829_2275903_-\|hypothetical-protein	gnl\|CDD\|372768	pfam13868, TPH, Trichohyalin-plectin-homology domain. This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.	2.47716e-28
NZ_CP016795.1\|WP_031033826.1\|2271207_2271663_-\|YbaB/EbfC-family-nucleoid-associated-protein	gnl\|CDD\|376829	pfam02575, YbaB_DNA_bd, YbaB/EbfC DNA-binding family. This is a family of DNA-binding proteins. Members of this family form homodimers which bind DNA via a tweezer-like structure. The conformation of the DNA is changed when bound to these proteins. In bacteria, these proteins may play a role in DNA replication-recovery following DNA damage.	1.11967e-05
NZ_CP016795.1\|WP_051159631.1\|2234547_2235621_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|236612	PRK09685, PRK09685, DNA-binding transcriptional activator FeaR; Provisional.	2.44865e-34
NZ_CP016795.1\|WP_037765627.1\|2225527_2226568_+\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	1.2165e-22
NZ_CP016795.1\|WP_031033835.1\|2276577_2276886_-\|WXG100-family-type-VII-secretion-target	gnl\|CDD\|274862	TIGR03930, WXG100_ESAT6, WXG100 family type VII secretion target. Members of this protein family include secretion targets for the two main variants of type VII secretion systems (T7SS), one found in the Actinobacteria, one found in the Firmicutes. This model was derived through iteration from pfam06013. The best characterized member of this family is ESAT-6 from Mycobacterium tuberculosis. Members of this family usually are ~100 amino acids in length but occasionally have a long C-terminal extension.	4.89821e-07
NZ_CP016795.1\|WP_037765635.1\|2235847_2236324_+\|peptidoglycan-binding-protein	gnl\|CDD\|366659	pfam01471, PG_binding_1, Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.	3.60238e-07
NZ_CP016795.1\|WP_031033810.1\|2231563_2232622_+\|rod-shape-determining-protein	gnl\|CDD\|336482	pfam06723, MreB_Mbl, MreB/Mbl protein. This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.	4.03085e-148
NZ_CP016795.1\|WP_079154904.1\|2223710_2225489_+\|trypsin-like-peptidase-domain-containing-protein	gnl\|CDD\|379142	pfam13365, Trypsin_2, Trypsin-like peptidase domain. This family includes trypsin-like peptidase domains.	2.05856e-11
NZ_CP016795.1\|WP_031033838.1\|2276973_2277309_-\|hypothetical-protein	gnl\|CDD\|223285	COG0207, ThyA, Thymidylate synthase [Nucleotide transport and metabolism].	0.00204605
NZ_CP016795.1\|WP_070388006.1\|2285968_2287270_-\|S8-family-serine-peptidase	gnl\|CDD\|274856	TIGR03921, T7SS_mycosin, type VII secretion-associated serine protease mycosin. Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair].	2.84341e-42
NZ_CP016795.1\|WP_070388004.1\|2277769_2279407_-\|type-VII-secretion-protein-EccB	gnl\|CDD\|368288	pfam05108, T7SS_ESX1_EccB, Type VII secretion system ESX-1, transport TM domain B. EccB is a family of largely Gram-positive bacterial transmembrane componenets of the type VII secretion system characterized in Mycobacterium tuberculosis, systems ESX1-5. Translocation of virulent peptides through the membranes is thought to be mediated via a complex that includes EccB, EccC, EccD, EccE, and MycP. EccB, EccC, EccD, and EccE form a stable complex in the mycobacterial cell envelope.	1.98997e-88
NZ_CP016795.1\|WP_037765624.1\|2221437_2222808_+\|acetyl-CoA-carboxylase	gnl\|CDD\|223848	COG0777, AccD, Acetyl-CoA carboxylase beta subunit [Lipid metabolism].	3.33642e-47
NZ_CP016795.1\|WP_031033845.1\|2279746_2281153_-\|type-VII-secretion-integral-membrane-protein-EccD	gnl\|CDD\|274855	TIGR03920, T7SS_EccD, type VII secretion integral membrane protein EccD. Members of this family are EccD, a component of actinobacterial type VII secretion systems (T7SS) with ten to eleven predicted transmembrane helix regions. [Protein fate, Protein and peptide secretion and trafficking].	4.39872e-37
NZ_CP016795.1\|WP_070387998.1\|2232665_2234171_+\|GAF-domain-containing-protein	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.3144e-15

>NZ_CP016795.1|WP_070388000.1|2236481_2237087_-|SseB-family-protein
MSESGAETPAAANPLDPAPPQEYVEAARLAPDHWLYLPDPAWRGEGPPPDWAVVGQWRSDADGTIVEWEDNPEYRPSPEAMGWPEPADAVDRAIQLATTGYGPAEDVTAALAGAEVAVLVTADGEPVRASAPDGTPAVPVYTSARYLHAAGRLASAHLPVSTLLTRVPPDHALYLNSNAPVGMVLPTQGLADLLEEEPRPQ
>NZ_CP016795.1|WP_037765635.1|2235847_2236324_+|peptidoglycan-binding-protein
MRTALTRTFVGAATVFAIAAGSLAGATVSSAASEPAARPAAGTREVSVLAVTNLGLTVGRAKSWQCFLTRSGYEPWEHAGLLGTDSWKAAQRMFNARGFSGKSKLVVDGVVGPLTIKALQRFLNDFGFGLAVDGIAGKRTSAAFYEFNGVPMPNDPRC
>NZ_CP016795.1|WP_051159631.1|2234547_2235621_-|helix-turn-helix-domain-containing-protein
MEGTDQRGNASGRGRTAAGAGRGAVLDASVVAPREREDTIRHALWASFSRVDIDHHTSQEDIGARMGLGAVGPMKVCSAQGTPVSLRRTERLAREDHEPSVFLGLQVSGTNMVGQHGRQCLVGPGNLVVFESTAPYTLRFEERFGYLSLRIPREALALPERVLREAAAVTLGPGNPTARLAFTYFSQLAASEELRGGAHAEALVGPSVELLRAVVTSQLGDAGAGRALPEVPLGMRVTQYVRAHLADPDLSAQRIAAAHGVSVRHLYNVLSRSGISLGDWIRTRRLAECRRELAGPGARTRTIAAIGRRWGFVDATHFSKAFKQAYGMSPRAWRELHQPGPARPRRPARRRVDVPAG
>NZ_CP016795.1|WP_164711384.1|2234357_2234504_+|hypothetical-protein
MSEPTPSQAEGERDEDRNGKADVPHSTPSQAEGEREEDETVPGGPEDR
>NZ_CP016795.1|WP_070387998.1|2232665_2234171_+|GAF-domain-containing-protein
MTAQPAPRLTRLLEAVLAGTGTELDLPGTLRHIAEGAAELTGADRADLVVADPGRDSPTEIRAPAPGPGAPAGPQEGAPGLRVPILVGDEEFGELRLTGRPGAGPFTAEDEQLLRVLATQAGISIGNARLYETARQRERWIEGAAAVTTALLTEESADDALTTVAERARLLADASAGVILHPTAEGGMAIVTASTPDDPDGMLGATIEPGSPVLEQLLGGEPVFLTDSATDPRMTTHVRHRFGPSMMLPLQANGRLIGTLALPRRRGAHRYTDLERLLATQFASQAALALVLADARRGRERLAVYEDRDRIARDLHDLVVQRLFATGMMLESTERRRGAEDVRDILVRAVDELRSTVQEVRTTIFALQQPPAEPPTGLRGRVLRETAAAAARLGFAPSTRFSGAVDTRVPAPVADRLVTALRHALADACARSEVSRVEVAVDTAAPLADGRAGVRLTVFDDGAGGGAEDGAKTDGRDGDEPDGDGGGYRGAGTTVTWWSPL
>NZ_CP016795.1|WP_031033810.1|2231563_2232622_+|rod-shape-determining-protein
MTASTASTASLEALRRCHFAVDLGAARTRVYVKGVGLVVDQPSAAAVNTRTGALIAVGEFAERMTGRTPGYIRVVRPVSGGTVVDIEMAQRMLRHLLGDRVRRALRRKPRLRAAVCTPHDADPLSQRAAIETLVGLGARRVELVDTLIAAAVGCGLPVEQPEATMIMVCGKHATQVAVLSLGSIVTAVRIPVGGEAVDHAIVQLLRHQHELVLPSQSVRPLQLALAGNGLTPQGPSSTEIHGRDVATGLARSVRVDTATVRNAIQTPLTAVLDGIGKVLRDCPPDLVADLADRGIMMVGGSALLPGFDQMLRQSTGMPVHIAERPDVCAVQGLGSMLEGRVEPLVLHPTAAD
>NZ_CP016795.1|WP_079154905.1|2226567_2231418_+|protein-kinase
MPADRPGPPDPLPHLADILGRASSGARPTPLELAELLWLAGQMTPAPDPPDGPAADGTVPEAAAGTFPPPDPVRRPAPDRDLDRDRHHRHGPGREQGQGRDSGQDRPVPGPPPAADAPGTPLRLPSSTMPAPGTSAAEPHSALLAPAPPMLRHTLALQRSLRPLKRRTAAPVGHEVDESATADRIARLGGGPEWWLPVLRPVRERWLRLHLVHDAGPTMPVWQPLVRELHDALAQSGVFRTVVLHRADADGTVGGDGFQAPADGRTVTLLISDCMGPQWREGEAGTRWFGTLRRWARHTPLAVLQPLPERLWRDTALPPVPGRLSAPHRAAPSSSLAFTPYDDTAPPAPRGAVSVPVLEPGPRWLANWAALVASPGGTTHPGAAATLHRPLPADADDRTDLARLSPEDLVLRFRARASREAFRLAGHLALGRPDLPVMRLVQAAVEPDPRPQHLAEVILSGLLTAVAGPPGSYAFRPGVRDLLLRGLPRTARNRTHELLLRTGGLIDERAGRSPGEFRALIPSRGGTERADGGETFAVISEDSARQLGVPARPGAPSPFPRALGDRYRPVRRLAPTGRVWLAEDTGAGRTVAVRLHDRLPGAAGAAARRAFLRDARRLTEFTHPNVVAVLDAGVEDDVPYVVMEHLDGIAVNALARAGEGRLPAPLTVSLAAQLARALTALHRAGLTHGGVEASRLVLLPDGTVRLSLLEPGLSSGRAGRSADLRALCAVLLELCAGTSRLTVPIDSRRLDRLPADLRIDYAHAFDQLMSMDPSAQARGLDLLTDPRLLATAEETYTPRRYRALGPLRVTLPDGSPALPPDERALLTMLLLKHGRTVTHEELRYGLWAPGDEPRDPRRELIRLAARLAEVLGPGVLATPSHGYALHTSADHVDLVHCDELVRRADAARLAGALTEARDLVTEALSLWHGSEPLTGVPGWGAHTARARLLRLRLALHTRRAELDLSLGDYDRASADLAGLLRAHPHREDFRRLYLIALRRQGRGAEALEVYEEYELSGGRSPALTALGRELREEHAGPVDDAPWSEYEDTPDAPDTSPDAGADARHGALSAPDELPEGPFPTEDDFWAWPPEEREEPERHAAEATDGELVGAWGNPRAEDSGPHLPEEEYADADEGPAAERGPGAGPEDEAADAGLDTDYRNCARYSLADGRHGDRDRAAALHVLVSHLLAESGLDGAAYELLDDRDGLLVLLAPRVEAVPLLRATVAGLPGQLARLGGARLRAEFWQVEFQLDGAQEVQSLRADAESVAAVLDASAAQAVVALSDSLYYDEVYDQEGPDGLLLPPGLFRPLADDTGWYRLIDEGTGEESDGGTGGEPEPTTAPEPAREPAPAPDGGPVRGASPLPPGGRPPLPAGSRPRAVAPRSPADLVSGARCVLLGFDDVLARLYRPAAEREVLLDVLRLFADERDPEDALAGLPLPRAATDGYAGTLDFVRALAGHRLDPDVRLRLDRHEARAARTARPVPLADRLIQALDTRGVPVAVVTDRAPGPVTSYLRRRGLLECLRGDVHGRDTDLTRLMPDPDVLHRALERLDADAGDCVLVGSSVAEQAAARAAGLPFVGRYGDEPARRRLTGADGDALLVPDLRPLLTAAENR
>NZ_CP016795.1|WP_037765627.1|2225527_2226568_+|MoxR-family-ATPase
MPLWPVYTGAPAPHDGITRLPPPPPWRAFEGEPVLDPPAEDTDDPGASPDRAQQATAHRATTYQATEDTVQLVNAALYLRRPLLVTGPPGTGKSSLAYAVARELGLGPVLRWNITSRSTLHDGLYTYDPLSRLYAARHATGLPGAPAAATGIEDHLRLGPLGTALLPYARPRALLIDEIDKSDLDLPNDLLHVLEEGQYEIPELVRAARDVPGGRAEVLIDGTDRRVPVERGRVRCREFPFVVLTSNGEREFPPAFLRRCVSLRLRQPEGHHLAEIVRAHLGEPDAYAQQLIQRFLSRVGSGELATDQLLNAIYLARSSGLGADSLDGLAEQLMPYLGRSPQADAF
>NZ_CP016795.1|WP_079154904.1|2223710_2225489_+|trypsin-like-peptidase-domain-containing-protein
MSGAAWHARVACGPEVGAGFLVSGRRLLTCAHVVKWADRAPVTVSFPGRRELGALSAAVAVHGGWQGGAADPGDLAVLELEREVPLTPASFAPPGAERGAPAPDLIAYGFPKGYDEGMLASYRAQPGPLISDEWVQLEAVTAHGQPLAAGFSGAALALADGTVVGMVSAVAGARDVRVGRMLPVEVMARYWPELGELVPTPGHRADVRRRLYALVREAEETGLSCDPKRLYASATDGFDPPPPDGGFAGLREAAAYVQWEVPEPGVVSRFADRLEELLHAPPPRPAAWSPIVVEIDRSGAGADQVTVEVSAYRDGQRHPVDARRLARGAVRAFVQERIDEAFTRLDPGADELLTFVLPREWLNEPVAHWECGEDDSTPLGCAYPLVVTDRHRHRSGRLRHQLRKKWRRLGASGGGTLQRVDCGTGERPAGLRKRLREDAELAGFATAPTVAREHFEVGLTVPVPVLMWPRRGCPGDPHEGPCPGSAFLDELAVSVADVPPSELPRHVMELRETADAADEPDAHWARDLQLLWDDPRCFADPTAALHSPVSPAPPVSPFPPTSPAPSASPTSPVPPGSPISPGSPISPVSPVR
>NZ_CP016795.1|WP_037765624.1|2221437_2222808_+|acetyl-CoA-carboxylase
MGERRSAREFLALVTDDFTELPAPRGEQDPDGPLGWPGYGAARARAADRTGEEESVVCGTGHVEGVRAVLLAFEFGFLGGSLGRRTGDRLEAAYAYARAHRLPVVPLVATGGSRMQEGMLALTQLQRVARQSVLTRRAGLPQVAVVRDPATGGGWATLGSGADVVLALPGAQVGFAGSRVRPPDADPAAYTAEAQVAAGSADAVVPEVELRSTLGRWLRLLTAPSGDPAPVPAPLGARDLPADGWDAVRRARAAGRPRAGAYLDAYFGERVALSGDRCGGADPEGMLCGFGTHAGRTVAYAAQTGTATRPAGYRTATRLIHLADRLGIPVLTLVDTPGAAGDAAAEGQAVGPAIADLFGAVASVRTPVSTLVIGEGGSGGALALAAPGATWATPDSYFSVIAPELAAAILKRPPAQVRLTADQLRLRPQDLAELDVIRTDEQVFPGTGDRRSEGRM
>NZ_CP016795.1|WP_031033824.1|2270816_2271206_-|hypothetical-protein
MGQRYYVDPARIEALSGQLEEIATLARSMTEEFLDGLAPTVSWPGTSGDFAEKAKPQEQKERQTTKDTMMSIRDALVSITDATLSQVKLMEDTRDRNLEDIERNTSRIETDGFGLDGSGGGDTGGHGRH
>NZ_CP016795.1|WP_031033826.1|2271207_2271663_-|YbaB/EbfC-family-nucleoid-associated-protein
MTEPLEQRLEKAMAELRSAQEAVERTERELRQASFAVLSSDRAVRATVGPQGELTGLDFLEYKYRDMSPQELAASVLEAASAAREKMNRHVMKAMAPFAEPSSEVPELKGFELDWERIFGPGVLEKADQDTDRTDGAAPGWRDALGEDGED
>NZ_CP016795.1|WP_070388002.1|2271829_2275903_-|hypothetical-protein
MVDRYDADSIDNVNKYEGATDASSDVWAGLVTHITGYPVPDRSTVFDTLRSDHGGKLFRMDIRDRGLGSFVQDASGFLRNTGEDYDIWFFDSGKKTQIKQARIVFEGRVKAGDEVIWADPGTDDVANASVREGNEFKDYNKDEMSTVALARYMNGPRTALLELLGGNTADARFSNLGVAEDSSVDLNSFNTTGQTFDFAAQFFRDQGPKIKEWEEALGREDASWKGEAAEVFRSLLTKIRENYDAYIETFDEKPSTGEGDGTGKTVYSRALSQARSALEDAADKLLDAWITWANSDYYDPHRVLRYVLDDLAQWVDSNNVAKTDIKTTYSAYSSSTYHDPQEGFSQNHPEYGDLTDIANWAKVGDKAVQIWSRGVDEHLVKPARTVQSNLNNTFLDLGGDFSENIPEPKSTSTASQEYEERKAEEAQEEIERQNEENRRYQDELREEQEKQREEDRKYQEELREEQRQQREEDKQAQDELREEQNRQREEDKQAQDELREEQNRQREEDRKYQDELRAEQEKQADEAQEQLRTLNDPTTTDLGGLDDLLNRDVPVTESLGDMGGLNGGPGGGDTALTESLGDLGGVNGGPGGGPGTDDLGNFGDANNAANQSLAGLGGTGGGDQPAAVPPPTNLGSLGGLNSGGGTRLPTERTPGLVDGNPVAQFPDGSSTSFDPDTGLLTSTAPDGSTTTTDLGNGLQVTNPDGSVTSLGDDGNLKTTFPDGRTETIDPSTGQAVTTNPDGTTTTTDLGSLGGLNNGAGGGTLDMPTGGSTQLSGGDLTSRFPDGSSTSFDPDTGTLTTTGPDGSTTTTDLGNGLEVTNPDGSVTSLGDDGNLKTTFPDGTTQSIDPSTGQAVTTNPDGTTTTTDLGSLGGLNNGAGGGTLDMPTGGSTQLSGGDLTSRFPDGSSTSFDPDTGTLTTTGPDGSTTTTDLGNGLEVTNPDGSVTSLGDDGNLKTTFPDGTTQSIDPSTGQAVTTNPDGTTTTTDLGSLGGLNGQGNQGGLDSLGDLQTQSNGDLGGLGDLDLGSLDGLNSGGGSGLETPTGGDTSLAGDDLLTRFPDGTRATFDTQTGMLTATNPDGSVTTTDLTHGAQVTNPDGSVTSLDNGMLTTDFPDGSTQVVDPETGIATVTDAQGNTETVNLHDLNTGNGPTSSNGNGLLDELGSLDGLGGSGGTGGGGTSTETLSPSDLGLGNGGSLTSGTGGGLTAGASVGSDGLLTGAAAPLSDSATAAGGTPLAPAAGAGTAGAPGMPGTPGMPMGGMGGMGGGGDKGNGERVRAVLVDAAEESERRNRRRRSPWNRQEDSDTFLSPASRVATTGGDDSSGEEPGQGRGVTTSADYLEEDADVWGTEDGGTPAVIGR
>NZ_CP016795.1|WP_070388003.1|2275968_2276439_-|type-VII-secretion-system-associated-protein
MADNPTDIKHFDLSAMENFRDYEVDRAYKDAKRHREGGGDGDPRTLGDLIDGHTTEDNLDQSQQLLRIGKMASDGRVSGPKLLEGVREAATALDKLLGDQIDLYKELQDALTDTIEGAQKTQAKNLDAIDAQTLLQHFDEVDTLTAGGSGGEDSDS
>NZ_CP016795.1|WP_031033835.1|2276577_2276886_-|WXG100-family-type-VII-secretion-target
MADGIIDVQYPVVRRAVEEMTEQTQQIINALNNLEDELKPLVASWEGSDQEMYRQVQMEWDQATKNMATLLNDNGTLIQSIHDNHSRDERRSADNWGNVRAR
>NZ_CP016795.1|WP_031033838.1|2276973_2277309_-|hypothetical-protein
MADSAARKADYAKGLGGVSSLESARSQVEKIQNNVAEIAARSGVGGDEGQALLKLFRSWNTEAQTVVVQISKMIDALQENVTSANRLAQENQDLTEVLNSKTSQGVFQALL
>NZ_CP016795.1|WP_070388004.1|2277769_2279407_-|type-VII-secretion-protein-EccB
MQSKRDQVQAHSFMMGRLSSGLLTAAPDAPESPLGRTTRGVVFGLLFTVLIGAGTVVYGLLRPGGNDGWRDGGHLVVNRDTGARYLWTDTDGVLHPVRNYTSARLIGGSDLPTEDVGTASLRDVPVGGPVGIPGAPDGLPDAGQLDGGAWNMCVTGPDGADPSTSGAAAAPAVDAAGATTLVVGAPVDSAAVGRDRGVLVSGPDKTQYLVWRGSRLPLDEKSDARTALGYGSVSAAPVSAAFLDALAPGPELRSPDVPGRGGEGPELGGEATRVGQVFEVSVPGGESTYHLLREEGLVPLTRLGAALVLGDPATQKDAYRGESPEARTVGADALREHQAEGAGGDEAAGLPDAPPAPQSVPRGSALCAQVDGGDGGARIGSVLAPLTELAPVAVPEGTADPVREACVPTDATVVRPGHGALVRALHASGAAHAGTTYLVAENGVKYRVPADDSLQALGYTTGDIDSVPAPLLAALPTGADLDPDAASGAAEVRVTAPDCGTDAQQEEAAPGKKAKAASFVTGDPAAAPGTADTALQTRQDGQSEF
>NZ_CP016795.1|WP_031033845.1|2279746_2281153_-|type-VII-secretion-integral-membrane-protein-EccD
MTDSTVAELCRLTVRAPSVSVDLAVPADVPVTDLLPTLLRYVGEEVEEAGLDHAGWVLQRLGDAPLDEETTLARAGLADGEVLYLRPHTEVLPEARLDDLVDGISDTVGRRMYTWSPKAARGLLGGTAVATVVLALVLVFWPGVDGSGSLRVICAGVAGLLALAGAGSASRAVGDRLTATVLGLLVAPCLALAGWVLPGGDLTGPDTARVVGARLLAAGAAGAGGAVLALAATAVGAPALFATALVAVATAIAGALIGYTGLDAPAAVALVMAVLALGAGAVAPFAFKLAGMRMPALPSSASQLQEGIEPYAGDEVAERTELAGRWVTALFAATGTAAVAALVVLAERPDLPEVLTALVLSLLLLLHSRGLVAVGQRLTLALPGVLGLLLLARAWAVDSDGDMRLVVFAVLLAAASALVIATWTVPGRRMLPYWGRAAELAHTVFAVALLPLTLWVAGLFGWLRGLFG
>NZ_CP016795.1|WP_070388005.1|2281613_2285660_+|type-VII-secretion-protein-EccCa
MPEGQLTLQEPPVLSETAPDTSTIWTYLPMALMSMSMMLMFLRPGGGNGVFMYLALGVMALSAAAMLLGQLMRRSGERKQRLKGERRDYLRYLTQIRKRVRATVVEQQRALAWRHPDPASLRSLARTSRLWERRPADEDFGEVRLAVGEQQLALSLNPVSTRPVEDLEPLCAHALRRFIRAYSTIPEQPIGLYLRSSARILLRPEDAADEDGAAPEVPPQGQALGGTAGTAGAGTGVRATSPADEALAALVRAVLAQLAVFHAPEELWIAVCASDDRRSDWEWAKWLPHVLDPHEEDGAGSVRRITADLTELDDLLGSEFAERPGFDPDARPGRDEPFTVVVLDGVTVPEGHRWAGHGYRNALLLDVSGALRWRPGRNTLRLTVGPDTVSLVRTDRSRKERSVPLGRPDRLGPLGAESLARLLTSRRISLGTDIAQPLETDIELTTLLGIPDLHRHDAPAHFARQTGSARLRVPVAVGVDGRPVELDIKESAQGGMGPHGLLIGATGSGKSELLRTLVLGLALSNSSETLNFVLVDFKGGATFLGLEELPHTSAVITNLADEAALVERMQDALHGELMRRQELLRAAGNHTSALEYERARAGGADLTPLPSLFVVVDEFSELLSSHREFMDLFVMIGRLGRSLGVHLLLASQRLDEGRMHQLESHLSYRIGLRTFSAMESRGVLGVPDAYQLPAAPGNGYLKSGVESLTRFRAAYSSGTYARRTGAVARARVASQVVPWTSGWVVPRAPEPTAEPEPAAEEAGEEETLLAVALDRLRGSGPAAHQVWLPPLDTPVPLDTLLPGIAADPERGLTAAGWHGTGRLRVPVALVDKPFEQRRDPHVVDLSGAGGHVAIAGGSQSGKSTLTRTLITALALTHTPAEVQFYCLDFGGGGLSQLASLPHVGGVAARLNPERVHRAVAEVMTLLARREQFFVDHTVDSMQSYRRRRAAGEFPDEPFGDVFMVVDGWSTVRQDYDDLVPKFNELAARGLNYGIHLLISTTRWVELSAQVRDQSATRLELRMGDPMDSEVDTRKARSVPRTGGRGITPDTKMHFLAGLPRIDGSGSLEDLGEGVAHLVSEISRHWTGPSAPQVRMLPHRLPVAELPAPQPTEGGGMRLALGIDQDALEPVWHDFSRTPHLTVIGDTESGKTNLMRRITEGITARYAPNEAKIIVVDYRRTLVDTIPEEYRIGHVISLDNLKETVEGAARALKTRVPGADIAPSRMRRCDWWTGPRLFVLVDDYDMVSGNSFQSPFEPLFEHLTLGFEMGLHLVVARSAMGAGRAMSDALLRRLDEANNPGVLLSCPPTEGNLFGNTKPRNLPPGRALHVARRKARLIQTALVEDAPES
>NZ_CP016795.1|WP_070388006.1|2285968_2287270_-|S8-family-serine-peptidase
MRPLCGVALAAAVLLPVAAPAAAEPGGAVSAVAGVADGEHAVAGSAGTRAAVAGAPRAVPAADGKSQGLPPMPSAFDPGTQGVPCTAASPEKAEKQDWSRQRLDLARVHQHGAGAGTTVALVDTGVRAGAAGLGDRVTARGDAGDDCVGHGTFLAGLIVGEGWGDTRLPGVAPGAKLLALRGTDERGTADAALVARAVRDATAADADVIAIGVALYKRDKELTSAVADALDAGAVVVAAATPDPPNANATQETPTRTYYPAGEPGVLSVADMLPSGARPGDALPTDGVDLAAPGAGVVSGGPRGNGHYLGAGASVAAAYTAGTAAVLRAARPDDTPGEIVHRLTATAYPADIPQLDAYAAVTTVLGDADAGARSRTEAGPVTVRDTADADGAADRATVFVLLGAAGVLAVLWAVVAVPRARARGWRPADTARD

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Crispr_ID: NZ_CP016795_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016795_6

2272610-2272687

Orphan

Consensus_repeat	Method
GGTGACGGAACCGTCGGGGTTGGT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016795_6

>merge|NZ_CP016795|6|2272610-2272687|CRISPRCasFinder
GGTGACGGAACCGTCGGGGTTGGTCACCTGCGCGCCGTGGGTCAGGTCGGTGGTGGTGACGGAACCGTCCGGGTTGGT

>NZ_CP016795|6|6|2272610-2272687|CRISPRCasFinder
GGTGACGGAACCGTCGGGGTTGGT	CACCTGCGCGCCGTGGGTCAGGTCGGTGGT
GGTGACGGAACCGTCCGGGTTGGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016795.1\|WP_070388006.1\|2285968_2287270_-\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|274856
NZ_CP016795.1\|WP_070388005.1\|2281613_2285660_+\|type-VII-secretion-protein-EccCa	unknown	unknown	gnl\|CDD\|274858
NZ_CP016795.1\|WP_079154905.1\|2226567_2231418_+\|protein-kinase	unknown	unknown	gnl\|CDD\|367616
NZ_CP016795.1\|WP_031033826.1\|2271207_2271663_-\|YbaB/EbfC-family-nucleoid-associated-protein	unknown	unknown	gnl\|CDD\|376829
NZ_CP016795.1\|WP_070388008.1\|2292083_2292740_-\|type-VII-secretion-system-associated-protein	unknown	unknown	gnl\|CDD\|236090
NZ_CP016795.1\|WP_051159631.1\|2234547_2235621_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|236612
NZ_CP016795.1\|WP_037765627.1\|2225527_2226568_+\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP016795.1\|WP_031033835.1\|2276577_2276886_-\|WXG100-family-type-VII-secretion-target	unknown	unknown	gnl\|CDD\|274862
NZ_CP016795.1\|WP_037765635.1\|2235847_2236324_+\|peptidoglycan-binding-protein	unknown	unknown	gnl\|CDD\|366659
NZ_CP016795.1\|WP_070388007.1\|2287350_2290665_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|163057
NZ_CP016795.1\|WP_031033810.1\|2231563_2232622_+\|rod-shape-determining-protein	unknown	unknown	gnl\|CDD\|336482
NZ_CP016795.1\|WP_070388003.1\|2275968_2276439_-\|type-VII-secretion-system-associated-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_164711384.1\|2234357_2234504_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031033838.1\|2276973_2277309_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223285
NZ_CP016795.1\|WP_031033824.1\|2270816_2271206_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_070388004.1\|2277769_2279407_-\|type-VII-secretion-protein-EccB	unknown	unknown	gnl\|CDD\|368288
NZ_CP016795.1\|WP_079154906.1\|2290740_2291991_-\|ricin-type-beta-trefoil-lectin-domain-protein	unknown	unknown	gnl\|CDD\|238092
NZ_CP016795.1\|WP_070388000.1\|2236481_2237087_-\|SseB-family-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031033845.1\|2279746_2281153_-\|type-VII-secretion-integral-membrane-protein-EccD	unknown	unknown	gnl\|CDD\|274855
NZ_CP016795.1\|WP_070387998.1\|2232665_2234171_+\|GAF-domain-containing-protein	unknown	unknown	gnl\|CDD\|226951

Protein	Function_ID	Function_description	E-value
NZ_CP016795.1\|WP_070388008.1\|2292083_2292740_-\|type-VII-secretion-system-associated-protein	gnl\|CDD\|236090	PRK07764, PRK07764, DNA polymerase III subunits gamma and tau; Validated.	0.00177896
NZ_CP016795.1\|WP_070388006.1\|2285968_2287270_-\|S8-family-serine-peptidase	gnl\|CDD\|274856	TIGR03921, T7SS_mycosin, type VII secretion-associated serine protease mycosin. Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair].	2.84341e-42
NZ_CP016795.1\|WP_079154905.1\|2226567_2231418_+\|protein-kinase	gnl\|CDD\|367616	pfam03704, BTAD, Bacterial transcriptional activator domain. Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR, along with the C terminal region, is capable of independently directing actinorhodin production. This family contains TPR repeats.	1.44481e-27
NZ_CP016795.1\|WP_031033826.1\|2271207_2271663_-\|YbaB/EbfC-family-nucleoid-associated-protein	gnl\|CDD\|376829	pfam02575, YbaB_DNA_bd, YbaB/EbfC DNA-binding family. This is a family of DNA-binding proteins. Members of this family form homodimers which bind DNA via a tweezer-like structure. The conformation of the DNA is changed when bound to these proteins. In bacteria, these proteins may play a role in DNA replication-recovery following DNA damage.	1.11967e-05
NZ_CP016795.1\|WP_051159631.1\|2234547_2235621_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|236612	PRK09685, PRK09685, DNA-binding transcriptional activator FeaR; Provisional.	2.44865e-34
NZ_CP016795.1\|WP_037765627.1\|2225527_2226568_+\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	1.2165e-22
NZ_CP016795.1\|WP_031033835.1\|2276577_2276886_-\|WXG100-family-type-VII-secretion-target	gnl\|CDD\|274862	TIGR03930, WXG100_ESAT6, WXG100 family type VII secretion target. Members of this protein family include secretion targets for the two main variants of type VII secretion systems (T7SS), one found in the Actinobacteria, one found in the Firmicutes. This model was derived through iteration from pfam06013. The best characterized member of this family is ESAT-6 from Mycobacterium tuberculosis. Members of this family usually are ~100 amino acids in length but occasionally have a long C-terminal extension.	4.89821e-07
NZ_CP016795.1\|WP_037765635.1\|2235847_2236324_+\|peptidoglycan-binding-protein	gnl\|CDD\|366659	pfam01471, PG_binding_1, Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.	3.60238e-07
NZ_CP016795.1\|WP_070388007.1\|2287350_2290665_-\|AAA-family-ATPase	gnl\|CDD\|163057	TIGR02881, Stage_V_sporulation_protein_K, stage V sporulation protein K. Members of this protein family are the stage V sporulation protein K (SpoVK), a close homolog of the Rubisco expression protein CbbX (TIGR02880) and a members of the ATPase family associated with various cellular activities (pfam00004). Members are strictly limited to bacterial endospore-forming species, but are not universal in this group and are missing from the Clostridium group. [Cellular processes, Sporulation and germination].	5.51413e-86
NZ_CP016795.1\|WP_031033810.1\|2231563_2232622_+\|rod-shape-determining-protein	gnl\|CDD\|336482	pfam06723, MreB_Mbl, MreB/Mbl protein. This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.	4.03085e-148
NZ_CP016795.1\|WP_070388005.1\|2281613_2285660_+\|type-VII-secretion-protein-EccCa	gnl\|CDD\|274858	TIGR03924, T7SS_EccC_a, type VII secretion protein EccCa. This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking].	0
NZ_CP016795.1\|WP_031033838.1\|2276973_2277309_-\|hypothetical-protein	gnl\|CDD\|223285	COG0207, ThyA, Thymidylate synthase [Nucleotide transport and metabolism].	0.00204605
NZ_CP016795.1\|WP_070388004.1\|2277769_2279407_-\|type-VII-secretion-protein-EccB	gnl\|CDD\|368288	pfam05108, T7SS_ESX1_EccB, Type VII secretion system ESX-1, transport TM domain B. EccB is a family of largely Gram-positive bacterial transmembrane componenets of the type VII secretion system characterized in Mycobacterium tuberculosis, systems ESX1-5. Translocation of virulent peptides through the membranes is thought to be mediated via a complex that includes EccB, EccC, EccD, EccE, and MycP. EccB, EccC, EccD, and EccE form a stable complex in the mycobacterial cell envelope.	1.98997e-88
NZ_CP016795.1\|WP_079154906.1\|2290740_2291991_-\|ricin-type-beta-trefoil-lectin-domain-protein	gnl\|CDD\|238092	cd00161, RICIN, Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ligand binding occurs on exposed surfaces of the compact domain sturcture.	2.41029e-29
NZ_CP016795.1\|WP_031033845.1\|2279746_2281153_-\|type-VII-secretion-integral-membrane-protein-EccD	gnl\|CDD\|274855	TIGR03920, T7SS_EccD, type VII secretion integral membrane protein EccD. Members of this family are EccD, a component of actinobacterial type VII secretion systems (T7SS) with ten to eleven predicted transmembrane helix regions. [Protein fate, Protein and peptide secretion and trafficking].	4.39872e-37
NZ_CP016795.1\|WP_070387998.1\|2232665_2234171_+\|GAF-domain-containing-protein	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.3144e-15

>NZ_CP016795.1|WP_031033826.1|2271207_2271663_-|YbaB/EbfC-family-nucleoid-associated-protein
MTEPLEQRLEKAMAELRSAQEAVERTERELRQASFAVLSSDRAVRATVGPQGELTGLDFLEYKYRDMSPQELAASVLEAASAAREKMNRHVMKAMAPFAEPSSEVPELKGFELDWERIFGPGVLEKADQDTDRTDGAAPGWRDALGEDGED
>NZ_CP016795.1|WP_031033824.1|2270816_2271206_-|hypothetical-protein
MGQRYYVDPARIEALSGQLEEIATLARSMTEEFLDGLAPTVSWPGTSGDFAEKAKPQEQKERQTTKDTMMSIRDALVSITDATLSQVKLMEDTRDRNLEDIERNTSRIETDGFGLDGSGGGDTGGHGRH
>NZ_CP016795.1|WP_070388000.1|2236481_2237087_-|SseB-family-protein
MSESGAETPAAANPLDPAPPQEYVEAARLAPDHWLYLPDPAWRGEGPPPDWAVVGQWRSDADGTIVEWEDNPEYRPSPEAMGWPEPADAVDRAIQLATTGYGPAEDVTAALAGAEVAVLVTADGEPVRASAPDGTPAVPVYTSARYLHAAGRLASAHLPVSTLLTRVPPDHALYLNSNAPVGMVLPTQGLADLLEEEPRPQ
>NZ_CP016795.1|WP_037765635.1|2235847_2236324_+|peptidoglycan-binding-protein
MRTALTRTFVGAATVFAIAAGSLAGATVSSAASEPAARPAAGTREVSVLAVTNLGLTVGRAKSWQCFLTRSGYEPWEHAGLLGTDSWKAAQRMFNARGFSGKSKLVVDGVVGPLTIKALQRFLNDFGFGLAVDGIAGKRTSAAFYEFNGVPMPNDPRC
>NZ_CP016795.1|WP_051159631.1|2234547_2235621_-|helix-turn-helix-domain-containing-protein
MEGTDQRGNASGRGRTAAGAGRGAVLDASVVAPREREDTIRHALWASFSRVDIDHHTSQEDIGARMGLGAVGPMKVCSAQGTPVSLRRTERLAREDHEPSVFLGLQVSGTNMVGQHGRQCLVGPGNLVVFESTAPYTLRFEERFGYLSLRIPREALALPERVLREAAAVTLGPGNPTARLAFTYFSQLAASEELRGGAHAEALVGPSVELLRAVVTSQLGDAGAGRALPEVPLGMRVTQYVRAHLADPDLSAQRIAAAHGVSVRHLYNVLSRSGISLGDWIRTRRLAECRRELAGPGARTRTIAAIGRRWGFVDATHFSKAFKQAYGMSPRAWRELHQPGPARPRRPARRRVDVPAG
>NZ_CP016795.1|WP_164711384.1|2234357_2234504_+|hypothetical-protein
MSEPTPSQAEGERDEDRNGKADVPHSTPSQAEGEREEDETVPGGPEDR
>NZ_CP016795.1|WP_070387998.1|2232665_2234171_+|GAF-domain-containing-protein
MTAQPAPRLTRLLEAVLAGTGTELDLPGTLRHIAEGAAELTGADRADLVVADPGRDSPTEIRAPAPGPGAPAGPQEGAPGLRVPILVGDEEFGELRLTGRPGAGPFTAEDEQLLRVLATQAGISIGNARLYETARQRERWIEGAAAVTTALLTEESADDALTTVAERARLLADASAGVILHPTAEGGMAIVTASTPDDPDGMLGATIEPGSPVLEQLLGGEPVFLTDSATDPRMTTHVRHRFGPSMMLPLQANGRLIGTLALPRRRGAHRYTDLERLLATQFASQAALALVLADARRGRERLAVYEDRDRIARDLHDLVVQRLFATGMMLESTERRRGAEDVRDILVRAVDELRSTVQEVRTTIFALQQPPAEPPTGLRGRVLRETAAAAARLGFAPSTRFSGAVDTRVPAPVADRLVTALRHALADACARSEVSRVEVAVDTAAPLADGRAGVRLTVFDDGAGGGAEDGAKTDGRDGDEPDGDGGGYRGAGTTVTWWSPL
>NZ_CP016795.1|WP_031033810.1|2231563_2232622_+|rod-shape-determining-protein
MTASTASTASLEALRRCHFAVDLGAARTRVYVKGVGLVVDQPSAAAVNTRTGALIAVGEFAERMTGRTPGYIRVVRPVSGGTVVDIEMAQRMLRHLLGDRVRRALRRKPRLRAAVCTPHDADPLSQRAAIETLVGLGARRVELVDTLIAAAVGCGLPVEQPEATMIMVCGKHATQVAVLSLGSIVTAVRIPVGGEAVDHAIVQLLRHQHELVLPSQSVRPLQLALAGNGLTPQGPSSTEIHGRDVATGLARSVRVDTATVRNAIQTPLTAVLDGIGKVLRDCPPDLVADLADRGIMMVGGSALLPGFDQMLRQSTGMPVHIAERPDVCAVQGLGSMLEGRVEPLVLHPTAAD
>NZ_CP016795.1|WP_079154905.1|2226567_2231418_+|protein-kinase
MPADRPGPPDPLPHLADILGRASSGARPTPLELAELLWLAGQMTPAPDPPDGPAADGTVPEAAAGTFPPPDPVRRPAPDRDLDRDRHHRHGPGREQGQGRDSGQDRPVPGPPPAADAPGTPLRLPSSTMPAPGTSAAEPHSALLAPAPPMLRHTLALQRSLRPLKRRTAAPVGHEVDESATADRIARLGGGPEWWLPVLRPVRERWLRLHLVHDAGPTMPVWQPLVRELHDALAQSGVFRTVVLHRADADGTVGGDGFQAPADGRTVTLLISDCMGPQWREGEAGTRWFGTLRRWARHTPLAVLQPLPERLWRDTALPPVPGRLSAPHRAAPSSSLAFTPYDDTAPPAPRGAVSVPVLEPGPRWLANWAALVASPGGTTHPGAAATLHRPLPADADDRTDLARLSPEDLVLRFRARASREAFRLAGHLALGRPDLPVMRLVQAAVEPDPRPQHLAEVILSGLLTAVAGPPGSYAFRPGVRDLLLRGLPRTARNRTHELLLRTGGLIDERAGRSPGEFRALIPSRGGTERADGGETFAVISEDSARQLGVPARPGAPSPFPRALGDRYRPVRRLAPTGRVWLAEDTGAGRTVAVRLHDRLPGAAGAAARRAFLRDARRLTEFTHPNVVAVLDAGVEDDVPYVVMEHLDGIAVNALARAGEGRLPAPLTVSLAAQLARALTALHRAGLTHGGVEASRLVLLPDGTVRLSLLEPGLSSGRAGRSADLRALCAVLLELCAGTSRLTVPIDSRRLDRLPADLRIDYAHAFDQLMSMDPSAQARGLDLLTDPRLLATAEETYTPRRYRALGPLRVTLPDGSPALPPDERALLTMLLLKHGRTVTHEELRYGLWAPGDEPRDPRRELIRLAARLAEVLGPGVLATPSHGYALHTSADHVDLVHCDELVRRADAARLAGALTEARDLVTEALSLWHGSEPLTGVPGWGAHTARARLLRLRLALHTRRAELDLSLGDYDRASADLAGLLRAHPHREDFRRLYLIALRRQGRGAEALEVYEEYELSGGRSPALTALGRELREEHAGPVDDAPWSEYEDTPDAPDTSPDAGADARHGALSAPDELPEGPFPTEDDFWAWPPEEREEPERHAAEATDGELVGAWGNPRAEDSGPHLPEEEYADADEGPAAERGPGAGPEDEAADAGLDTDYRNCARYSLADGRHGDRDRAAALHVLVSHLLAESGLDGAAYELLDDRDGLLVLLAPRVEAVPLLRATVAGLPGQLARLGGARLRAEFWQVEFQLDGAQEVQSLRADAESVAAVLDASAAQAVVALSDSLYYDEVYDQEGPDGLLLPPGLFRPLADDTGWYRLIDEGTGEESDGGTGGEPEPTTAPEPAREPAPAPDGGPVRGASPLPPGGRPPLPAGSRPRAVAPRSPADLVSGARCVLLGFDDVLARLYRPAAEREVLLDVLRLFADERDPEDALAGLPLPRAATDGYAGTLDFVRALAGHRLDPDVRLRLDRHEARAARTARPVPLADRLIQALDTRGVPVAVVTDRAPGPVTSYLRRRGLLECLRGDVHGRDTDLTRLMPDPDVLHRALERLDADAGDCVLVGSSVAEQAAARAAGLPFVGRYGDEPARRRLTGADGDALLVPDLRPLLTAAENR
>NZ_CP016795.1|WP_037765627.1|2225527_2226568_+|MoxR-family-ATPase
MPLWPVYTGAPAPHDGITRLPPPPPWRAFEGEPVLDPPAEDTDDPGASPDRAQQATAHRATTYQATEDTVQLVNAALYLRRPLLVTGPPGTGKSSLAYAVARELGLGPVLRWNITSRSTLHDGLYTYDPLSRLYAARHATGLPGAPAAATGIEDHLRLGPLGTALLPYARPRALLIDEIDKSDLDLPNDLLHVLEEGQYEIPELVRAARDVPGGRAEVLIDGTDRRVPVERGRVRCREFPFVVLTSNGEREFPPAFLRRCVSLRLRQPEGHHLAEIVRAHLGEPDAYAQQLIQRFLSRVGSGELATDQLLNAIYLARSSGLGADSLDGLAEQLMPYLGRSPQADAF
>NZ_CP016795.1|WP_070388003.1|2275968_2276439_-|type-VII-secretion-system-associated-protein
MADNPTDIKHFDLSAMENFRDYEVDRAYKDAKRHREGGGDGDPRTLGDLIDGHTTEDNLDQSQQLLRIGKMASDGRVSGPKLLEGVREAATALDKLLGDQIDLYKELQDALTDTIEGAQKTQAKNLDAIDAQTLLQHFDEVDTLTAGGSGGEDSDS
>NZ_CP016795.1|WP_031033835.1|2276577_2276886_-|WXG100-family-type-VII-secretion-target
MADGIIDVQYPVVRRAVEEMTEQTQQIINALNNLEDELKPLVASWEGSDQEMYRQVQMEWDQATKNMATLLNDNGTLIQSIHDNHSRDERRSADNWGNVRAR
>NZ_CP016795.1|WP_031033838.1|2276973_2277309_-|hypothetical-protein
MADSAARKADYAKGLGGVSSLESARSQVEKIQNNVAEIAARSGVGGDEGQALLKLFRSWNTEAQTVVVQISKMIDALQENVTSANRLAQENQDLTEVLNSKTSQGVFQALL
>NZ_CP016795.1|WP_070388004.1|2277769_2279407_-|type-VII-secretion-protein-EccB
MQSKRDQVQAHSFMMGRLSSGLLTAAPDAPESPLGRTTRGVVFGLLFTVLIGAGTVVYGLLRPGGNDGWRDGGHLVVNRDTGARYLWTDTDGVLHPVRNYTSARLIGGSDLPTEDVGTASLRDVPVGGPVGIPGAPDGLPDAGQLDGGAWNMCVTGPDGADPSTSGAAAAPAVDAAGATTLVVGAPVDSAAVGRDRGVLVSGPDKTQYLVWRGSRLPLDEKSDARTALGYGSVSAAPVSAAFLDALAPGPELRSPDVPGRGGEGPELGGEATRVGQVFEVSVPGGESTYHLLREEGLVPLTRLGAALVLGDPATQKDAYRGESPEARTVGADALREHQAEGAGGDEAAGLPDAPPAPQSVPRGSALCAQVDGGDGGARIGSVLAPLTELAPVAVPEGTADPVREACVPTDATVVRPGHGALVRALHASGAAHAGTTYLVAENGVKYRVPADDSLQALGYTTGDIDSVPAPLLAALPTGADLDPDAASGAAEVRVTAPDCGTDAQQEEAAPGKKAKAASFVTGDPAAAPGTADTALQTRQDGQSEF
>NZ_CP016795.1|WP_031033845.1|2279746_2281153_-|type-VII-secretion-integral-membrane-protein-EccD
MTDSTVAELCRLTVRAPSVSVDLAVPADVPVTDLLPTLLRYVGEEVEEAGLDHAGWVLQRLGDAPLDEETTLARAGLADGEVLYLRPHTEVLPEARLDDLVDGISDTVGRRMYTWSPKAARGLLGGTAVATVVLALVLVFWPGVDGSGSLRVICAGVAGLLALAGAGSASRAVGDRLTATVLGLLVAPCLALAGWVLPGGDLTGPDTARVVGARLLAAGAAGAGGAVLALAATAVGAPALFATALVAVATAIAGALIGYTGLDAPAAVALVMAVLALGAGAVAPFAFKLAGMRMPALPSSASQLQEGIEPYAGDEVAERTELAGRWVTALFAATGTAAVAALVVLAERPDLPEVLTALVLSLLLLLHSRGLVAVGQRLTLALPGVLGLLLLARAWAVDSDGDMRLVVFAVLLAAASALVIATWTVPGRRMLPYWGRAAELAHTVFAVALLPLTLWVAGLFGWLRGLFG
>NZ_CP016795.1|WP_070388005.1|2281613_2285660_+|type-VII-secretion-protein-EccCa
MPEGQLTLQEPPVLSETAPDTSTIWTYLPMALMSMSMMLMFLRPGGGNGVFMYLALGVMALSAAAMLLGQLMRRSGERKQRLKGERRDYLRYLTQIRKRVRATVVEQQRALAWRHPDPASLRSLARTSRLWERRPADEDFGEVRLAVGEQQLALSLNPVSTRPVEDLEPLCAHALRRFIRAYSTIPEQPIGLYLRSSARILLRPEDAADEDGAAPEVPPQGQALGGTAGTAGAGTGVRATSPADEALAALVRAVLAQLAVFHAPEELWIAVCASDDRRSDWEWAKWLPHVLDPHEEDGAGSVRRITADLTELDDLLGSEFAERPGFDPDARPGRDEPFTVVVLDGVTVPEGHRWAGHGYRNALLLDVSGALRWRPGRNTLRLTVGPDTVSLVRTDRSRKERSVPLGRPDRLGPLGAESLARLLTSRRISLGTDIAQPLETDIELTTLLGIPDLHRHDAPAHFARQTGSARLRVPVAVGVDGRPVELDIKESAQGGMGPHGLLIGATGSGKSELLRTLVLGLALSNSSETLNFVLVDFKGGATFLGLEELPHTSAVITNLADEAALVERMQDALHGELMRRQELLRAAGNHTSALEYERARAGGADLTPLPSLFVVVDEFSELLSSHREFMDLFVMIGRLGRSLGVHLLLASQRLDEGRMHQLESHLSYRIGLRTFSAMESRGVLGVPDAYQLPAAPGNGYLKSGVESLTRFRAAYSSGTYARRTGAVARARVASQVVPWTSGWVVPRAPEPTAEPEPAAEEAGEEETLLAVALDRLRGSGPAAHQVWLPPLDTPVPLDTLLPGIAADPERGLTAAGWHGTGRLRVPVALVDKPFEQRRDPHVVDLSGAGGHVAIAGGSQSGKSTLTRTLITALALTHTPAEVQFYCLDFGGGGLSQLASLPHVGGVAARLNPERVHRAVAEVMTLLARREQFFVDHTVDSMQSYRRRRAAGEFPDEPFGDVFMVVDGWSTVRQDYDDLVPKFNELAARGLNYGIHLLISTTRWVELSAQVRDQSATRLELRMGDPMDSEVDTRKARSVPRTGGRGITPDTKMHFLAGLPRIDGSGSLEDLGEGVAHLVSEISRHWTGPSAPQVRMLPHRLPVAELPAPQPTEGGGMRLALGIDQDALEPVWHDFSRTPHLTVIGDTESGKTNLMRRITEGITARYAPNEAKIIVVDYRRTLVDTIPEEYRIGHVISLDNLKETVEGAARALKTRVPGADIAPSRMRRCDWWTGPRLFVLVDDYDMVSGNSFQSPFEPLFEHLTLGFEMGLHLVVARSAMGAGRAMSDALLRRLDEANNPGVLLSCPPTEGNLFGNTKPRNLPPGRALHVARRKARLIQTALVEDAPES
>NZ_CP016795.1|WP_070388006.1|2285968_2287270_-|S8-family-serine-peptidase
MRPLCGVALAAAVLLPVAAPAAAEPGGAVSAVAGVADGEHAVAGSAGTRAAVAGAPRAVPAADGKSQGLPPMPSAFDPGTQGVPCTAASPEKAEKQDWSRQRLDLARVHQHGAGAGTTVALVDTGVRAGAAGLGDRVTARGDAGDDCVGHGTFLAGLIVGEGWGDTRLPGVAPGAKLLALRGTDERGTADAALVARAVRDATAADADVIAIGVALYKRDKELTSAVADALDAGAVVVAAATPDPPNANATQETPTRTYYPAGEPGVLSVADMLPSGARPGDALPTDGVDLAAPGAGVVSGGPRGNGHYLGAGASVAAAYTAGTAAVLRAARPDDTPGEIVHRLTATAYPADIPQLDAYAAVTTVLGDADAGARSRTEAGPVTVRDTADADGAADRATVFVLLGAAGVLAVLWAVVAVPRARARGWRPADTARD
>NZ_CP016795.1|WP_070388007.1|2287350_2290665_-|AAA-family-ATPase
MSRQVLSVGPDDRDRFRTIGEALAAARTGALISVRPGTYAENLVIHTRVTLTAAEGRGTVEIRPRSGSVVALRADAVMLSELTLRGADAEAPAVDVRRGQAALDGCEIAGAAWTALLAGGTGSLALRDCRVSNSQGAGIVVTSTTPTTVESCTLEHLGTSGLVVAEQGEVRVRGCTVRDARGNGVLANGDSRGSLEDCDLSSTDKPSLALEGNSTLTVSRTVVHDTSNGVHLSSAGRTTLEDVRITGASGTGITLAAGTDPVLRRCRVSRTRGHGVVVTDRARGTFEDCWIDGAQGVALRVAGAASPALTGLTVRDCAETGLLLEEDAAAELDRLEVIGGAPAIALRAGANPLLRRARLVEPSGDGITATGDARGRVEDCEIVQPGGSGVRAASGSTLYLAGGGVSGAVDSGLVLEDGGSVTVRDFRVENAGAEGVVVDSGGELTANRTSVLTPQGHGVLLREGAIASLSGCEVAGGAQDGFRVETTAPVSLVNCLARENEGGGLVQTTPGERLAVEGLSSTGNGKRDAWGSGSAENTDPAGSGAADGPAQDRPDGPLGALNALIGLDNVKEQVRTLVNLTQLAQRREQLGMSAPPMSRHLVFTGPPGTGKTTVARLYGAILAELGSLRDGHLVEVSRADLVAQVVGGTAIKTTETFERALGGVLFVDEAYTLTSDSGHGGADFGREAVDTLLKLMEDHRDEVVVIVAGYTDEMTGFLASNPGLGSRFSRTVEFENYTVPELVAIMESMCAAHQYELGEGTAAALAAHFDAMPRGAGFGNGRAARGVFEEMVDRQAVRLATLQQVGERDLRLLLPEDVSEAAAEQSAETGVPENDPLTRLGDMVGLAEVKRDVTDLVNLITTARHRAAAGLPVPSLSHHLVFTGPPGTGKTTVARLYGEILSQLGILPRGQLVEAARADLVGRYIGHTAQLTREVFERARGGVLFIDEAYTLTPRGGGNDFGQEAVDTLLKLMEDHRDDVVVIVAGYTGEMERFLSSNPGLASRFPRRIAFADYSSEELVTIVRTQASAMGYECGPGTGPLLREHFDSLPRDQSFGNARLARQVVESMVTRQAGRLSSLAAPTLEDLRVLLPEDVTAATPKAAR
>NZ_CP016795.1|WP_079154906.1|2290740_2291991_-|ricin-type-beta-trefoil-lectin-domain-protein
MPESKSKSTSESPASTTAEGSASGSGAESFPEVKPEAGTAPAGEAQSTAEKAPKAEKAPKAEEAEEAEEAEAAEREPVALALAQAADGPAEDSGTGVGTGVGTGVDTDADAGGASAAKSRLPLLVRTMTATAIDKPDDAVRPVGRPGRAVLAAAAVGGALLVAVPFLLLGPDDEDKEDRASTTAATVLGGDQEEETGDFAVSPPEAGDPADDEKESEKPKAPPAPKTDSGDAEKAAAAEKAEKEKKAAEEKAAKEKAEKEKKAASEQSSKDSGKDVAKNGGNAAAGPALGFPVSFHSHLSGRCIDVPASAFTDGQGLWMWDCNNTDAQKFQFASDGTLRLKGLCMDVAGANFANGTPIQLANCTGVDAQKFALNEAHDLVNTAVGMCVEIEGHDHNAQARVQLWTCTGLDNQKWSV
>NZ_CP016795.1|WP_070388008.1|2292083_2292740_-|type-VII-secretion-system-associated-protein
MEATSGTPASSPGPGAVEAGDTPEIPEAVRAAARQAPGHWIGVVDPEWPEERTPPEWAVLGEWRSGDEGDVGTYRANPAYRPSARALGWPEPTDPVDAAAQRAATGYGSVDEALAALAAAEVTVVAGPDGAPLAAAGQDGEPVVLVFTSPAHAFMSATLRHETLPARELTRSLAGSPTLSLLVNAGAVAPLLVPAARVPVDGGEDPPGPLTHTSGRYP

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Crispr_ID: NZ_CP016795_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016795_7

4754786-4754893

Orphan

Consensus_repeat	Method
CGGAGACCCCGGCCGGCGGTGCGG	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP016795_7

>merge|NZ_CP016795|7|4754786-4754893|CRISPRCasFinder
CGGATGCTCCGGCGTCCGGTGCGGGTGCTCCGGCGTCCGGCACGGAGACCCCGGCCGGCGGTGCGGGGACCCCGGCCGGCGGTGCGGGGACGCCCGCGTCCGGTGCGG

>NZ_CP016795|7|7|4754786-4754893|CRISPRCasFinder
CGGATGCTCCGGCGTCCGGTGCGG	GTGCTCCGGCGTCCGGCA
CGGAGACCCCGGCCGGCGGTGCGG	GGACCCCGGCCGGCGGTG
CGGGGACGCCCGCGTCCGGTGCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016795.1\|WP_031044260.1\|4747008_4748937_-\|2-oxoacid:acceptor-oxidoreductase-subunit-alpha	unknown	unknown	gnl\|CDD\|274738
NZ_CP016795.1\|WP_037761004.1\|4744832_4745687_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187578
NZ_CP016795.1\|WP_037761001.1\|4751622_4752882_-\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226951
NZ_CP016795.1\|WP_037760970.1\|4766382_4767762_-\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|271189
NZ_CP016795.1\|WP_070388922.1\|4760136_4761735_+\|NADH-quinone-oxidoreductase-subunit-M	unknown	unknown	gnl\|CDD\|273903
NZ_CP016795.1\|WP_037760977.1\|4764390_4764807_+\|YccF-domain-containing-protein	unknown	unknown	gnl\|CDD\|236975
NZ_CP016795.1\|WP_078535691.1\|4753040_4753469_+\|NADH-quinone-oxidoreductase-subunit-A	unknown	unknown	gnl\|CDD\|169084
NZ_CP016795.1\|WP_070388923.1\|4761731_4763279_+\|NADH-quinone-oxidoreductase-subunit-N	unknown	unknown	gnl\|CDD\|235603
NZ_CP016795.1\|WP_037760989.1\|4758135_4760130_+\|NADH-quinone-oxidoreductase-subunit-L	unknown	unknown	gnl\|CDD\|235836
NZ_CP016795.1\|WP_031044263.1\|4749208_4749880_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225107
NZ_CP016795.1\|WP_037761010.1\|4743127_4743598_-\|glyoxalase/bleomycin-resistance/dioxygenase-family-protein	unknown	unknown	gnl\|CDD\|380093
NZ_CP016795.1\|WP_070388924.1\|4765013_4765280_+\|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein	unknown	unknown	gnl\|CDD\|182475
NZ_CP016795.1\|WP_070388921.1\|4756344_4756872_+\|4Fe-4S-binding-protein	unknown	unknown	gnl\|CDD\|235637
NZ_CP016795.1\|WP_031044317.1\|4765401_4765890_-\|YajQ-family-cyclic-di-GMP-binding-protein	unknown	unknown	gnl\|CDD\|213038
NZ_CP016795.1\|WP_037761483.1\|4741905_4742865_-\|M28-family-peptidase	unknown	unknown	gnl\|CDD\|349873
NZ_CP016795.1\|WP_037761007.1\|4743606_4744665_-\|EamA-family-transporter-RarD	unknown	unknown	gnl\|CDD\|225510
NZ_CP016795.1\|WP_037760991.1\|4757683_4758139_+\|NADH-quinone-oxidoreductase-subunit-NuoK	unknown	unknown	gnl\|CDD\|180218
NZ_CP016795.1\|WP_070388919.1\|4753459_4754083_+\|NADH-quinone-oxidoreductase-subunit-B	unknown	unknown	gnl\|CDD\|235797
NZ_CP016795.1\|WP_051159442.1\|4745867_4746869_-\|2-oxoacid:ferredoxin-oxidoreductase-subunit-beta	unknown	unknown	gnl\|CDD\|237006
NZ_CP016795.1\|WP_037760995.1\|4755317_4756286_+\|NADH-quinone-oxidoreductase-subunit-H	unknown	unknown	gnl\|CDD\|376297

Protein	Function_ID	Function_description	E-value
NZ_CP016795.1\|WP_031044260.1\|4747008_4748937_-\|2-oxoacid:acceptor-oxidoreductase-subunit-alpha	gnl\|CDD\|274738	TIGR03710, OAFO_sf, 2-oxoacid:acceptor oxidoreductase, alpha subunit. This family of proteins contains a C-terminal thiamine diphosphate (TPP) binding domain typical of flavodoxin/ferredoxin oxidoreductases (pfam01855) as well as an N-terminal domain similar to the gamma subunit of the same group of oxidoreductases (pfam01558). The genes represented by this model are always found in association with a neighboring gene for a beta subunit (TIGR02177) which also occurs in a 4-subunit (alpha/beta/gamma/ferredoxin) version of the system. This alpha/gamma plus beta structure was used to define the set of sequences to include in this model. This pair of genes is not consistantly observed in proximity to any electron acceptor genes, but is found next to putative ferredoxins or ferredoxin-domain proteins in Azoarcus sp. EbN1, Bradyrhizobium japonicum USDA 110, Frankia sp. CcI3, Rhodoferax ferrireducens DSM 15236, Rhodopseudomonas palustris BisB5, Os, Sphingomonas wittichii RW1 and Streptomyces clavuligerus. Other potential acceptors are also sporadically observed in close proximity including ferritin-like proteins, reberythrin, peroxiredoxin and a variety of other flavin and iron-sulfur cluster-containing proteins. The phylogenetic distribution of this family encompasses archaea, a number of deeply-branching bacterial clades and only a small number of firmicutes and proteobacteria. The enzyme from Sulfolobus has been characterized with respect to its substrate specificity, which is described as wide, encompassing various 2-oxoacids such as 2-oxoglutarate, 2-oxobutyrate and pyruvate. The enzyme from Hydrogenobacter thermophilus has been shown to have a high specificity towards 2-oxoglutarate and is one of the key enzymes in the reverse TCA cycle in this organism. Furthermore, considering its binding of coenzyme A, it can be reasonably inferred that the product of the reaction is succinyl-CoA. The genes for this enzyme in Prevotella intermedia 17, Persephonella marina EX-H1 and Picrophilus torridus DSM 9790 are in close proximity to a variety of TCA cycle genes. Persephonella marina and P. torridus are believed to encode complete TCA cycles, and none of these contains the lipoate-based 2-oxoglutarate dehydrogenase (E1/E2/E3) system. That system is presumed to be replaced by this one. In fact, the lipoate system is absent in most organisms possessing a member of this family, providing additional circumstantial evidence that many of these enzymes are capable of acting as 2-oxoglutarate dehydrogenases and.	0
NZ_CP016795.1\|WP_037761004.1\|4744832_4745687_-\|SDR-family-oxidoreductase	gnl\|CDD\|187578	cd05269, TMR_SDR_a, triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.	6.15399e-83
NZ_CP016795.1\|WP_037761001.1\|4751622_4752882_-\|sensor-histidine-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.01166e-30
NZ_CP016795.1\|WP_037760970.1\|4766382_4767762_-\|tyrosine-type-recombinase/integrase	gnl\|CDD\|271189	cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The 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.	1.05423e-14
NZ_CP016795.1\|WP_070388922.1\|4760136_4761735_+\|NADH-quinone-oxidoreductase-subunit-M	gnl\|CDD\|273903	TIGR01972, NADH-quinone_oxidoreductase_subunit_M, proton-translocating NADH-quinone oxidoreductase, chain M. This model describes the 13th (based on E. coli) structural gene, M, of bacterial NADH dehydrogenase I, as well as chain 4 of the corresponding mitochondrial complex I and of the chloroplast NAD(P)H dehydrogenase complex. [Energy metabolism, Electron transport].	1.07679e-171
NZ_CP016795.1\|WP_037760977.1\|4764390_4764807_+\|YccF-domain-containing-protein	gnl\|CDD\|236975	PRK11770, PRK11770, YccF domain-containing protein.	2.11929e-54
NZ_CP016795.1\|WP_078535691.1\|4753040_4753469_+\|NADH-quinone-oxidoreductase-subunit-A	gnl\|CDD\|169084	PRK07756, PRK07756, NADH-quinone oxidoreductase subunit A.	5.23662e-35
NZ_CP016795.1\|WP_070388923.1\|4761731_4763279_+\|NADH-quinone-oxidoreductase-subunit-N	gnl\|CDD\|235603	PRK05777, PRK05777, NADH-quinone oxidoreductase subunit NuoN.	5.3732e-99
NZ_CP016795.1\|WP_037760989.1\|4758135_4760130_+\|NADH-quinone-oxidoreductase-subunit-L	gnl\|CDD\|235836	PRK06590, PRK06590, NADH:ubiquinone oxidoreductase subunit L; Reviewed.	4.11281e-145
NZ_CP016795.1\|WP_031044263.1\|4749208_4749880_-\|response-regulator-transcription-factor	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	6.42678e-38
NZ_CP016795.1\|WP_037761010.1\|4743127_4743598_-\|glyoxalase/bleomycin-resistance/dioxygenase-family-protein	gnl\|CDD\|380093	pfam18029, Glyoxalase_6, Glyoxalase-like domain. This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.	1.6708e-25
NZ_CP016795.1\|WP_070388924.1\|4765013_4765280_+\|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein	gnl\|CDD\|182475	PRK10457, PRK10457, hypothetical protein; Provisional.	1.86619e-11
NZ_CP016795.1\|WP_070388921.1\|4756344_4756872_+\|4Fe-4S-binding-protein	gnl\|CDD\|235637	PRK05888, PRK05888, NADH-quinone oxidoreductase subunit NuoI.	4.70965e-34
NZ_CP016795.1\|WP_031044317.1\|4765401_4765890_-\|YajQ-family-cyclic-di-GMP-binding-protein	gnl\|CDD\|213038	cd11740, YajQ_like, Proteins similar to Escherichia coli YajQ. In Pseudomonas syringae, YajQ functions as a host protein involved in the temporal control of bacteriophage Phi6 gene transcription. It has been shown to bind to the phage's major structural core protein P1, most likely activating transcription by acting indirectly on the RNA polymerase. YajQ may remain bound to the phage particles throughout the infection period. Earlier, YajQ was characterized as a putative nucleic acid-binding protein based on the similarity of its (ferredoxin-like) three-dimensional topology with that of RNP-like RNA-binding domains.	1.85714e-83
NZ_CP016795.1\|WP_037761483.1\|4741905_4742865_-\|M28-family-peptidase	gnl\|CDD\|349873	cd03876, M28_SGAP_like, M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins. Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures.	5.50341e-142
NZ_CP016795.1\|WP_037761007.1\|4743606_4744665_-\|EamA-family-transporter-RarD	gnl\|CDD\|225510	COG2962, RarD, Predicted permeases [General function prediction only].	2.21532e-103
NZ_CP016795.1\|WP_037760991.1\|4757683_4758139_+\|NADH-quinone-oxidoreductase-subunit-NuoK	gnl\|CDD\|180218	PRK05715, PRK05715, NADH-quinone oxidoreductase subunit NuoK.	9.21972e-38
NZ_CP016795.1\|WP_070388919.1\|4753459_4754083_+\|NADH-quinone-oxidoreductase-subunit-B	gnl\|CDD\|235797	PRK06411, PRK06411, NADH-quinone oxidoreductase subunit NuoB.	2.138e-87
NZ_CP016795.1\|WP_051159442.1\|4745867_4746869_-\|2-oxoacid:ferredoxin-oxidoreductase-subunit-beta	gnl\|CDD\|237006	PRK11867, PRK11867, 2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed.	4.36214e-170
NZ_CP016795.1\|WP_037760995.1\|4755317_4756286_+\|NADH-quinone-oxidoreductase-subunit-H	gnl\|CDD\|376297	pfam00146, NADHdh, NADH dehydrogenase.	1.17808e-110

>NZ_CP016795.1|WP_070388919.1|4753459_4754083_+|NADH-quinone-oxidoreductase-subunit-B
MDVNSSGTAPVPLPEPVPLPEPKRLGTLARLAPEPMKVVLNWGRRYSLWVFNFGLACCAIEFIAASMARHDFIRLGVIPFAPGPRQADLMVVSGTVTDKMAPAVKRLYEQMPEPKYVISFGACSNCGGPYWDSYSVTKGVDQIIPVDVYVPGCPPRPEALLQGILKLQEKIARESLGERYGAGHRPSTAALRSGLVPPPAPDPGEAR
>NZ_CP016795.1|WP_078535691.1|4753040_4753469_+|NADH-quinone-oxidoreductase-subunit-A
MATREKERGTHVPEPTVGLAADYFQSYSVVGLLALVGVLFVAVAFGAGRLLRPVVPTPEKLLTYECGVDPVGEGWAHTQVRYYVYAFLYVVFAVDSIFLFPWATVFAAPGYGATTLVEMFIFLGFLAVGLLYAYKKGVLSWT
>NZ_CP016795.1|WP_037761001.1|4751622_4752882_-|sensor-histidine-kinase
MTEDLSRSPFTGRGAGGGTGDRLPPVRLAYDRHTWKEIAHLLANLPASLIGFTYVVTVLSVGVGLTVTVIGLPLLAAGLLGARRLGRLERGRARALLGVRVDEPSPLPVRSGDGFFPRLWMALKDPVGWRTVLYGFVRLPWGILTFVLVLASCFVLWPVLPFLARGLANADRAMVRGLLSPSDELERRIAELESDRGIVVDTAAADLRRIERDLHDGAQARLVNLAMGLGLAKEKLLEDPDAAAAMVDEAHGEVKLALQELRDLARGIHPAVLTDRGLDAALSSVASRCTVPVGVTVDLAERPAAAIEGIAYFTVSELLQNVSKHSAARNASVEVWRASDRLLIQVADDGRGGARVGGGTGMKGLADRLSAVDGLFVVDSPEGGPTTVTAELPWRDRTGDDAAGSAPSGSGRSRQRSGR
>NZ_CP016795.1|WP_031044263.1|4749208_4749880_-|response-regulator-transcription-factor
MEDRVRVVIAEDSVLLREGLTRLLTDRGHEVVAGVGDGEALVKTITELDAQGELPDVVVADVRMPPTHTDEGVRASVRLRKAHPGLGVLVLSQYVEERYATELLAGSSRGVGYLLKDRVAEVREFVDAVVRVAEGGTALDPEVVAQLLGRSRKQDVLAGLTPREREVLGLMAEGRTNSAIARQLVVSDGAVEKHVSNIFMKLGLSPSDGDHRRVLAVLTYLNS
>NZ_CP016795.1|WP_031044260.1|4747008_4748937_-|2-oxoacid:acceptor-oxidoreductase-subunit-alpha
MTSQVSSPAEQADSTVVGEQRKAAGTKDVRRLERVVIRFAGDSGDGMQLTGDRFTSETASFGNDLSTLPNFPAEIRAPAGTLPGVSSFQLHFADHDILTPGDAPNVLVAMNPAALKANVGDLPRGAEIIVNTDEFTRRAMQKVGYDASPLEDGSLDGYHVHPVPLTTLTVEALKEFDLSRKEAERSKNMFALGLLSWMYHRPTEGTEKFLRSKFAKKPDIAAANIAAYRAGWNFGETTEDFAVSYEVAPATTAFPPGTYRNISGNLALAYGLIAASLQTDLPLFLGSYPITPASDILHELSRHKNFGVRTFQAEDEIAGIGAALGAAFGGSLAVTTTSGPGVALKSETIGLAVSLELPLLVVDIQRGGPSTGLPTKTEQADLLQAMYGRNGEAPVPVVAPCTPADCFDAALEAARIAVTYRTPVFLLSDGYLANGSEPWRVPEPGELPDLAVRFAQGPNHSLEDGTEVFWPYKRDPHTLARPWAVPGTPGLEHRIGGIEKQDGTGNISYDPANHDFMVRTRQAKIDGVAVPDLEVDDPDGARTLVLGWGSTYGPITAAVRRLRGAGEAVAQAHLRHLNPFPANLGAVLKRYDKVVVPEMNLGQLATLVRAKYLVDAHSYNQVNGMPFKAEQLAAALKEAIDD
>NZ_CP016795.1|WP_051159442.1|4745867_4746869_-|2-oxoacid:ferredoxin-oxidoreductase-subunit-beta
MKDFKSDQEVRWCPGCGDYAILAAVQGFMPQLGLAKENIVFVSGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLAASRRDLSVWVVTGDGDALSIGGNHLVHALRRNVNLKILLFNNRIYGLTKGQYSPTSEVGKITKSTPMGSVDAPFNPLSLALGAEATFVARTVDSDRKHLTEVLRQAADHPGTALIEIYQNCNIFNDGAFEAIKDKQQAEEAVIRLEHGQPIRFGTDGAKGVVRDAATGDLKIVAVTADNEADILVHDAHAASPTTAFALTRLADPDTLHHTPIGVLRSVERPVYDTLMTDQLDAAVEQNGKGDLAALLAGNDTWTVVG
>NZ_CP016795.1|WP_037761004.1|4744832_4745687_-|SDR-family-oxidoreductase
MSIVVTGATGHLGRLVVRQLLEKAPADQVTAVVRDRDRAADLAALGVRLAVADYNAPETFDGLFAAGDRVLLISGNEFDKGRVQQHTVVIEAAGKAGVALLAYTSAPESLKAALADDHRATEEVLVGSGVPYALLRNGWYHENYTEQLAPVLEHGAVVQAAGEGRVSSASRADYAAAAVAVLTGEGHENKAYELGGDEAWSFAEYAAELSRQTGKEIVYKPVSAEAYTGILAGAGLPATLAEILAGVDASIAKGELVVSTGDLSRLAGRPTTPLAEAVAAALKG
>NZ_CP016795.1|WP_037761007.1|4743606_4744665_-|EamA-family-transporter-RarD
MPGSSRSDQRIGLLNGFAAYGMWGIVPLYWPLLQPAGSGEMLAHRMVWSLVFVAAALLVVRRWAWAVELLRQPRRLALIAVAATVITVNWGVYIWAVNSGHVVEASLGYFINPLVTIAMGVLLLKERLRPAQWAAVGIGFAAVLVLAVGYGEPPWISLCLAFSFATYGLAKKKVNLGGVESLAAETAVLFLPALGYLLWLGTQGQSTFTTGGLGHSALLASTGVVTAIPMVCFGFAAIRVPLSTLGLLQYLAPVFQFLLGVLYFHEKMPPERWAGFGLVWLALTLLTWDALRTARRTARALKEQLDRTGAGVAPVKGSTAARDSEIVASGTPAPEVAEQQSQTRTQARQQTL
>NZ_CP016795.1|WP_037761010.1|4743127_4743598_-|glyoxalase/bleomycin-resistance/dioxygenase-family-protein
MTPTPGPAPLHFKIVVDAAAPHAQAEFWAAALHYEVEDNSALIEKLLGSGAVPVEATVESHGRRAWRDLAAVRHPDDPYQEESGTGLGRRLLFQRVPEAKTGKNRLHLDVHSADGGRAAEVTRLEALGAGVLRRVTEQGGEWVMMADPEGNEFCVH
>NZ_CP016795.1|WP_037761483.1|4741905_4742865_-|M28-family-peptidase
MPRSPLSGRALTAGAVAVATLMAGGSAAGAASAAERPAAVADAPDIPVANVKAHLTQLQSIATANGGNRAHGRPGYQASLDYVRAELDAAGFTTSLQEFTASGSTGYNLIADWPGGDADQVVMSGAHLDSVTSGPGINDNGSGSSAVLETALAVARSGYQPTKHLRFAWWGAEELGLVGSSHYVDSLGSADREKISGYLNFDMIGSPNPGYFVYDDDPTIEKTFKDYFAGLGITTEIETEGDGRSDHAPFKNAGVPVGGLFSGADYRKTSAQAAEWGGTVGEPFDPCYHSSCDTTANVDDTALDRNSDAIAYAVWELSQ
>NZ_CP016795.1|WP_037760995.1|4755317_4756286_+|NADH-quinone-oxidoreductase-subunit-H
MNDALDVTLRLLIVFVVFLAFPLIVGQAEHKVMAHMQGRLGPMYAGGFHGWAQLVADGVKFAQKEDVVPADADRRIFQLAPAVSLLPYLLVLLAIPVGPGEGAVGQVVDAGVFFVLAVMGVGVLGSLMAGWSSANKFSLLGGLRTAAQLLAYELPMLLTAASVAMAAGTVSLVGILDAFEWWWLPWQIVGAIVFFVAGLAELQRPPFDMPVADSEIIFGAYTEYTGLRFALFLLAEYAGIVVLCGLTTVLFLGGWHGPWGADGLGWVWTLLKTAVLAFVVIWLRVTYPRLREDQLQKLSWTFLVPLSLAQIALTGIVKVVIQ
>NZ_CP016795.1|WP_070388921.1|4756344_4756872_+|4Fe-4S-binding-protein
MTKKTVTEQYPDAQPELPPRTRGVIGLFEENCTVCMLCARECPDWCIYIDSHKETVPAAAPGGRDRSRNVLDRFAIDFSLCMYCGICIEVCPFDALFWSPEFEYAETDIRDLTHERDKLREWMWTVPAPPALDPGAEEPKELAAARKSADRLAAQQEAVRAAGPTAPEPGQEGPE
>NZ_CP016795.1|WP_037760991.1|4757683_4758139_+|NADH-quinone-oxidoreductase-subunit-NuoK
MHLAYPAVLSALLFCTGVYGVLARRNAILVLMSVELMLNAVNLNLVAFDVWLSRAAEETLHSGQALTLFTIAIAAAEIGIGLAIVLAVHRNRGTSDIDKLRDTAEGHGPDGLDGPDDSDDPDDPGDPAVPGGPDTDTPATGTAAEKAEATA
>NZ_CP016795.1|WP_037760989.1|4758135_4760130_+|NADH-quinone-oxidoreductase-subunit-L
MTTTTLAVLVPLVPFLGAVAGLLLGRTAPGFVRPLAVLPTLAALVLAVLVAARQGGGAAVDAATELTPTGSVPVELALHVDGFAALVAVLVGTVATCVQLYSTGYLRDDPRYASYAALVSLFTSAMFLVVYSGDLMVLLVGWEIMGICSYFLVGHYWETPEARAASLKAFLVTKLGDVPFLIGLLALATEAGSFRITRILGAVAHGSLDHPTLIALLLLAGVAGKSAQFPLHTWLPDAMAGPTPVSALIHAATMVAAGVYFVARLLPFFEASRAAMVVLAVMAAVTMVGSALAALAQDDIKRVLAYSTIGQLGYLTGALATGDRSAAVFHLLSHGAFKALLFLAAGVIIHAAGTNSLAAMSRMRGLRDRVPDAYWTTTVGLLALAAIPPFSGFFSKESVLGAAEHVATGHTEHAPGAAGWTVLVAGLITALLTAAYATRLWLLAFRGSGAEAPDHGRQPVVMNAVLWVLAIPSLALGGLVFRLLPDWFDGQDLTPTLTTSVLGTGVALVGGIVTYAAWRHTTVLAARTPLGAVAAHPEGDAALVEAEAIASHRPAYGDIAGAPDPADPGRLLLGPLHRPAAAGFHLDAVYTTLFVRPVRAGASLVRFLDREVVDTYVRAAGTWPRWLGAAVRRAQTGNLQTYVSALLAGTVVLAVAAVLVATGA
>NZ_CP016795.1|WP_070388922.1|4760136_4761735_+|NADH-quinone-oxidoreductase-subunit-M
MIDINESVMQFLLALVVVGPLLGAAAALLPAPPGLKGKSPEQAVLRHGVTVTGAVLAAVIVLALGFDHDHPSKMQAGTDISWIPALDVRIHLGIDGISLPLLVLTALLTFLCALYSYFEQRQERLTPRAPRPSPKAFVALLLVLESGTLATFAVLDLVLFFLAFETVLIPMYFLIARWGGESRAAAAWKFILFTLLGSVVMLLGLLLIGLNAGTFDMVALATDNGRSLTASVQVVAVLAIGIGLAVKTPMWPLHSWLPDAHTAAPTVGSVLLAGVLLKMGTYGFVRILLPVAPDGFHTFAPYLAAFAVVGIVYGSLACLALARRGAKGDLKRLIAYSSVGHMGFVLLGIATMTPTGVNGALFANVAHGLITGLLFFLVGALKDRTGTTDLDTLAEESGHALYGRAPRLGGLLAFAAVASLGLPGLAGFWGEMLALFGAFDPHDDLSRPAFLTFMAVAAFGTLLTAAYMLIVVRRVCMGAVPREAPELTDVRGYEFAAWTPLVALTVVAGLWPRTLLGLTDPAVQQLLSGGTR
>NZ_CP016795.1|WP_070388923.1|4761731_4763279_+|NADH-quinone-oxidoreductase-subunit-N
MSFPAQNLAEAASQPPAQNLVQSVDWLAIAPPTITAVVGLVVLVADLFVADRRKPLLGWVSVAGLAASALMLLPLVNGDRSAFCLAGDPGLCSYTADTFTLAVQFLVLGGALLTALLSVTAVKDADRGLPEGEFWFLLLSSAAGAALLPASRDLATLIVALEVASLPAFALVGLRRGDRRSSEAALKFFLSSVTATAVSLLGVSFVYASTGTLYLTQVAERIQHVDGQLTTLAQTGVVLTLVGFAFKTAAVPFHFWVPDTYVGAPLPIAAYLSVVGKAVGFSGLVLVTVVALPSYADVWGPALAALAALTMTVGNVGALRQQGTRAYSAVRLLAWSSVGQAGYLLVPIAAAAYSDDPEGAVGSTVAYALMYAAVNLGAFAVAAVVGRTRSLNRVADYRGLYASNPLTALLLAFFLLCLAGLPPGVIGLFAKVTVFSAAVDAGLGWLAVVMAVNVVIALFYYLQWTAQLFRTPQEATAGHRLPAPLTAAISLTAVLAVALSGAPQLILRFADTALF
>NZ_CP016795.1|WP_037760977.1|4764390_4764807_+|YccF-domain-containing-protein
MKTILNVIWLVLSGFWLFLGYLFAGALLCITIIGIPFGIAAFRIGIYALWPFGYMAVQRRDAGAASCIGNALWLVLAGWWLALGHIVTGILLCVTIIGIPLGVANFKLIPVSLLPLGREIVPTDQPFTVAAANQRTGW
>NZ_CP016795.1|WP_070388924.1|4765013_4765280_+|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein
MTVISWIILGLLAGAIAKFLLPGRDPGGFVGTTLIGIAGAFIGGWISARWLDHPISKGFYDGATWAAAIGGSLVLLIAYRLLFGNSRN
>NZ_CP016795.1|WP_031044317.1|4765401_4765890_-|YajQ-family-cyclic-di-GMP-binding-protein
MADSSFDIVSKVERQEVDNALNQAAKEISQRYDFKGVGASIKWSGEQVLMEANSEDRVNAILDVFQSKLIKRGISLKALDAGEPQLSGKEYKIFASIQEGISQDNAKKVAKLIRDEGPKGVKAQVQGEELRVSSKSRDDLQTVISLLKGQDFDFALQFVNYR
>NZ_CP016795.1|WP_037760970.1|4766382_4767762_-|tyrosine-type-recombinase/integrase
MALTYDVRLYSIEIRKERPKPYRVRWLVGTRKHSKSYTLKIQAEGRRSELMAAVRRGDQFDEETGLPVSELRAKLGSITWYEHSRAYVDRKWALAPAKSRKNYADALATITPALVKTRTGMPDAALMRRALYGWAYNRNRWGETPPDDVARALSWVAKHSLPVSALEDPATVRLALDALSLRLDGKEAAPRTAKRKRACLSDVLGLAVEEQYFSMPVNPIGAVKWTAPKSVEEVDPESVANPRQVRALLAGVREQGPRGRHLEAFFGCLYYAAMRPAEAAALRASQCHLPETGWGTLTLRQGIVRAGRSWTDDGTAHEARHLKARAKNDSRPVPIPPHFVRLLREHVASHGTAPDGRLFRTNRGGLLQETGYGEVWAKARGDVLSDAETASLLARRPYDLRHAGVSFWLSSGVDAMECARRAGHSIAVLHKVYAKVLDQTREHANSRIDAALREWNEPE

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Crispr_ID: NZ_CP016795_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016795_8

6320813-6320894

Orphan

Consensus_repeat	Method
CTCCTCCGTCCGCACCGCCTCCTCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016795_8

>merge|NZ_CP016795|8|6320813-6320894|CRISPRCasFinder
CGCCACGGCCCGCACCGCCTCCTCCGTCCGCACCGCCTCCTCCTCCGTCCGCACCATCTCGTCCGTCTGCACCATCTCGTCC

>NZ_CP016795|8|8|6320813-6320894|CRISPRCasFinder
CGCCACGGCCCGCACCGCCTCCTCC	GTCCGCACCGCCTCCTCCTCCGTCCGCACCAT
CTCGTCCGTCTGCACCATCTCGTCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016795.1\|WP_031043013.1\|6328395_6329100_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224095
NZ_CP016795.1\|WP_037762865.1\|6311788_6313189_+\|UDP-N-acetylmuramate--L-alanine-ligase	unknown	unknown	gnl\|CDD\|234757
NZ_CP016795.1\|WP_070389401.1\|6311213_6311669_+\|indole-3-glycerol-phosphate-synthase	unknown	unknown	unknown
NZ_CP016795.1\|WP_079155076.1\|6327220_6328399_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224050
NZ_CP016795.1\|WP_070389407.1\|6322093_6323527_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP016795.1\|WP_070389408.1\|6326301_6327084_+\|FAD:protein-FMN-transferase	unknown	unknown	gnl\|CDD\|376782
NZ_CP016795.1\|WP_037763261.1\|6330919_6331459_-\|ATP/GTP-binding-protein	unknown	unknown	gnl\|CDD\|367304
NZ_CP016795.1\|WP_031043005.1\|6325883_6326300_+\|FMN-binding-protein	unknown	unknown	gnl\|CDD\|377242
NZ_CP016795.1\|WP_070389400.1\|6310113_6310956_+\|pyrimidine-reductase-family-protein	unknown	unknown	gnl\|CDD\|184482
NZ_CP016795.1\|WP_079155075.1\|6314273_6317774_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276938
NZ_CP016795.1\|WP_070389404.1\|6317863_6319123_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_031042982.1\|6313207_6313615_+\|peptide-methionine-(R)-S-oxide-reductase-MsrB	unknown	unknown	gnl\|CDD\|376583
NZ_CP016795.1\|WP_070389399.1\|6308097_6308502_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|277001
NZ_CP016795.1\|WP_031043016.1\|6329096_6329762_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224095
NZ_CP016795.1\|WP_031043000.1\|6323523_6324267_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_CP016795.1\|WP_123937970.1\|6319134_6319752_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016795.1\|WP_070390459.1\|6324355_6325705_+\|ferredoxin-reductase-family-protein	unknown	unknown	gnl\|CDD\|99795
NZ_CP016795.1\|WP_031042971.1\|6308854_6309973_-\|cell-division-protein-ZapE	unknown	unknown	gnl\|CDD\|224402
NZ_CP016795.1\|WP_031043024.1\|6331529_6331889_-\|DUF742-domain-containing-protein	unknown	unknown	gnl\|CDD\|283084
NZ_CP016795.1\|WP_070389402.1\|6313707_6314169_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP016795.1\|WP_031043013.1\|6328395_6329100_+\|ABC-transporter-permease-subunit	gnl\|CDD\|224095	COG1174, OpuBB, ABC-type proline/glycine betaine transport systems, permease component [Amino acid transport and metabolism].	1.88606e-34
NZ_CP016795.1\|WP_037762865.1\|6311788_6313189_+\|UDP-N-acetylmuramate--L-alanine-ligase	gnl\|CDD\|234757	PRK00421, murC, UDP-N-acetylmuramate--L-alanine ligase; Provisional.	0
NZ_CP016795.1\|WP_070389407.1\|6322093_6323527_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	1.22717e-58
NZ_CP016795.1\|WP_070389408.1\|6326301_6327084_+\|FAD:protein-FMN-transferase	gnl\|CDD\|376782	pfam02424, ApbE, ApbE family. This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalyzing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.	1.78134e-55
NZ_CP016795.1\|WP_037763261.1\|6330919_6331459_-\|ATP/GTP-binding-protein	gnl\|CDD\|367304	pfam03029, ATP_bind_1, Conserved hypothetical ATP binding protein. Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.	8.68397e-46
NZ_CP016795.1\|WP_031043005.1\|6325883_6326300_+\|FMN-binding-protein	gnl\|CDD\|377242	pfam04205, FMN_bind, FMN-binding domain. This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR and NirI regulatory proteins.	6.29519e-10
NZ_CP016795.1\|WP_070389400.1\|6310113_6310956_+\|pyrimidine-reductase-family-protein	gnl\|CDD\|184482	PRK14059, PRK14059, pyrimidine reductase family protein.	1.74282e-93
NZ_CP016795.1\|WP_031043000.1\|6323523_6324267_-\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	3.05444e-77
NZ_CP016795.1\|WP_031042982.1\|6313207_6313615_+\|peptide-methionine-(R)-S-oxide-reductase-MsrB	gnl\|CDD\|376583	pfam01641, SelR, SelR domain. Methionine sulfoxide reduction is an important process, by which cells regulate biological processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides in proteins, has been known for four decades and has been extensively characterized with respect to structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides. Because oxidized methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the activity that is different but complementary to that of MsrA. Thus, these proteins, working together, could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins and fused with the peptide methionine sulfoxide reductase enzymatic domain pfam01625. The domain has two conserved cysteine and histidines. The domain binds both selenium and zinc. The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of the family. This family has methionine-R-sulfoxide reductase activity.	4.76666e-78
NZ_CP016795.1\|WP_070389399.1\|6308097_6308502_-\|hypothetical-protein	gnl\|CDD\|277001	cd15526, PHD1_MOZ_d4, PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 gene family proteins. MOZ is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity and to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF) is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphoma genesis and bone development, and its homologs. This family also includes three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes via changing the condensed/decondensed state of chromatin in nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro specific gene clusters. All family members contain two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.	0.00738083
NZ_CP016795.1\|WP_031043016.1\|6329096_6329762_+\|ABC-transporter-permease	gnl\|CDD\|224095	COG1174, OpuBB, ABC-type proline/glycine betaine transport systems, permease component [Amino acid transport and metabolism].	1.63368e-45
NZ_CP016795.1\|WP_079155075.1\|6314273_6317774_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|276938	cd15831, BTAD, Bacterial Transcriptional Activation (BTA) domain. The Bacterial Transcriptional Activation (BTA) domain is present in the putative transcriptional regulator Mycobacterium EmbR and the related Streptomyces antibiotic regulatory protein (SARP) family of transcription factors, which includes DnrI and AfsR, among others. Members of this family contain an N-terminal DNA-binding domain, followed by the BTA domain, and many have diverse domains at the C-terminus. EmbR contains an C-terminal forkhead-associated (FHA) domain, which mediates binding to threonine-phosphorylated sites in a sequence-specific manner. The BTA domain of EmbR contains three Tetratricopeptide repeats (TPRs) and two C-terminal helices. The TPR motif typically contains 34 amino acids, and 5 or 6 tandem repeats of the motif generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein.	2.72501e-27
NZ_CP016795.1\|WP_070390459.1\|6324355_6325705_+\|ferredoxin-reductase-family-protein	gnl\|CDD\|99795	cd06198, FNR_like_3, NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.	2.04366e-71
NZ_CP016795.1\|WP_031042971.1\|6308854_6309973_-\|cell-division-protein-ZapE	gnl\|CDD\|224402	COG1485, COG1485, Predicted ATPase [General function prediction only].	2.36191e-60
NZ_CP016795.1\|WP_031043024.1\|6331529_6331889_-\|DUF742-domain-containing-protein	gnl\|CDD\|283084	pfam05331, DUF742, Protein of unknown function (DUF742). This family consists of several uncharacterized Streptomyces proteins as well as one from Mycobacterium tuberculosis. The function of these proteins is unknown.	6.74298e-35
NZ_CP016795.1\|WP_079155076.1\|6327220_6328399_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224050	COG1125, OpuBA, ABC-type proline/glycine betaine transport systems, ATPase components [Amino acid transport and metabolism].	1.00446e-138

>NZ_CP016795.1|WP_123937970.1|6319134_6319752_+|hypothetical-protein
MASLTATALTADRADGGAVHRVRTVLVDPVSGALTVDEHVRVRCSAPTGWAILGDVLIAPGAGARWAARLAYSCPGALVVAVHSGGRCWLRAGAGGAAAAAVGPVAVSVAVFEVRGPGRARQTWDRLASLAHSCLVAGVPGTELGAAVAALEPAVGSLSPGRVGSGTRSAYRPEASPSSRSSRSSRSSRSRSASAPAEPDRPAEA
>NZ_CP016795.1|WP_070389404.1|6317863_6319123_+|hypothetical-protein
MSLTVPEPHARHVPVRMDVDRWATHRSRRRLLVVVHTVVTGQRLLDAIRLLEGDNRVQTFFTQAPDVFSNGVEAFLERLGGLVLPWNQAVLTRFDLALAAGHGNLHDLQTPVVVLPHGAGHNKVVHAVPGNRPAVHRGAYGLSRQRLMRDGAVVPEAIVLAHQEELTRLGQDCPEAVPAAEVVGDPCFDRVAASLPLRALYREALGVRGRLRLVLACSTWGPDSLLGHGWSTLERLVAELPKDEYRTAALLHPHVWNAHGHWQVRAWLAELVRAGLILVSPHADWTGAVVAADHIVGDHGSVSLYGAMTGAPVLMAGRSDAAVDPGSPMAELMSFAPRLREDRPVWQQLKRSSVLRRAQRYERVAARITSEPGRFARRMRALLYRKLRLRAPAVRGPVAEPAGLPLTVRYDDPGAGVSR
>NZ_CP016795.1|WP_079155075.1|6314273_6317774_-|tetratricopeptide-repeat-protein
MPGGLDGGLAGILHSCGSPPAAGVRAPRRCPRAPAIPPLTPRCDRRTVVRVTPAPRPWYAAHPSGETVDLLVLGPLELWHDQRQHALGSLKERCVLAVLLHARGEPVTVDTLMDRVWDGEPPPTAVDTLHTYLSRLRRRLRRAVGDDLAQVRRHSSRAYQLRADPGDIDLLRFNRLRSQAVAAAGRDREVAVGLLRAAEAQWHGEPLAEFADNSWAQSTRARLAEDHRRVREERIRLEMELGRHADLLGELQELASQNPFAQRVIGSLMLALYRSGRHDEALTVFRDTRTRLHRSQGIEPTAELQQLHLRMLEQDHDLLRTGAAGTDTPPVPAALPVSAAPAESLNCLPRDIPDFVGRSGELRILLAGTGTRAGGGREATGGGAGTALPVTVIHGMPGIGKTALAVHAAHQLAPVYPDAQFYVDLRGHSGQQPLDPSDALAVLLHSTGCDGTLPATLDERAAKWREWTARRRALLVLDNVRDAAQVAPLLPGSPACRVLVTTRNRLAGLDGAAPLLLDTLSGQEAESLFTRVAGASRVAADPENLRRIAAACACHPLALQVLASRFRHRGAWDLRHLLDRLRHASRPLQEFDSLISAVFRFSYAELGAPAQELFRLLALHPGPDLALPAATALTGAEDPALLEQCVEELLDASLLEEPVLGRYRLHDLTRSYAAQVGLDTDTERTRTAATGRLAHHYLATAHRADLLIRPHRRAFPLPPPRQTTASVPALSDADEASVWLTVERANLTAVARMAADRHPQYAALFPRVLAGPLKLWGAWGDASRLFEAALPVLRGSGDRALLARTLTDRADLLAQRNHGEALDCATEALAIHEELHDEHGRADALFQSGRARLAAGHGESALPVLEEARALYRTVGDPAGEADCLNVQGAALSYLGRYDQALEKVERMGTIHESLHDLHGLARAQNNRGELHFLQGRYADARACYEESLVWMRRYGGRTDVATVSTNLGAVHQAMGRTDEALTHFRRTLAVHRASGDSLGEADALILAGRAYAESGRRGEALLHFAMAERVAADIDNPYETIRASLGAADVQRESGRLDLASQGYERALEVAERIHYALGSAQALAGLARTTVLSRRTVGLAETYGERAAARYRALGAETEAAELLRFLAGHRPAGPRRPASGTGTGGVTRSSGRPLGPPGPNPGR
>NZ_CP016795.1|WP_070389402.1|6313707_6314169_+|hypothetical-protein
MEAELAALAASGATTLVGLMVSETWEQARHRLSRFFARDGDENAVAAELRSSRSDLVAARDGADAEAVADIEAAWRARLRRALLSDPEAARELRALLAEIAPSDGAGEAAGAVHNTVSGGVQHGPVLQGGRFSGVSFHEVASSDGELGQNASG
>NZ_CP016795.1|WP_031042982.1|6313207_6313615_+|peptide-methionine-(R)-S-oxide-reductase-MsrB
MSYDVEKPDEQWRKELAPAEYAVLREAATEPAFTGEYTDTKTEGVYSCRACGAELFTSTTKFESHCGWPSFFDPKDTDAVELIEDRSHGMVRTEVRCARCGSHLGHVFKGEGYPTPTDQRYCINSISLRLEPERG
>NZ_CP016795.1|WP_037762865.1|6311788_6313189_+|UDP-N-acetylmuramate--L-alanine-ligase
MAPGLPTAMDRPHFIGIGGAGMSGIAKVLAQRGAAVAGSDAKESATAGALRALGATVHIGHAAGHLADDASCVVVSSAIREDNPELARAAELGIPVVHRSDALAALMNGLRPLAVAGTHGKTTTTSMLAVSLSELGLNPSYAIGGDLDEPGSNALHGSGEIFVAEADESDRSFHKYAPEVAIVLNVELDHHANYASMDEIYESFETFADRIVPGGTLVIAADHEGARELTRRLAGTVRTVTYGESEDADVRILSVVPQGLKSEVTVVLDGAELTFGVSVPGRHYAHNAVAALAAGAALGVPAAELAPALAAYTGVKRRLQLKGEAAGVQVVDSYAHHPTEMTADLEAMRAAVGDARILVLFQPHLFSRTQELGKEMGQALALADASVVLDIYPAREDPIPGITSDLIVEAARAAGADVTPVHDKDAASAAVAGMAKAGDLVLTMGAGDVTDLGPRILDELSSQANQ
>NZ_CP016795.1|WP_070389401.1|6311213_6311669_+|indole-3-glycerol-phosphate-synthase
MIEKALTSADVEFVTTLHGEETVGFHVLLQPRGDQADRLLRAIDDVALGELDDAVRENETPEGDDAQGVGRRALEVSLTALRASGAEAEGRLIEDHPLDELKSLVLEIGADEVIVLTDPHYVEEFFHRDWASRARHKVGVPVLKLFSHSKA
>NZ_CP016795.1|WP_070389400.1|6310113_6310956_+|pyrimidine-reductase-family-protein
MRRLFPVTDRTAGPDPAPSGARSGADAGSGADATEGDRDREWSLAELAAAYAYPVPDGRRQTWLRANMVSTLDGAAQHDGRSQPISSAADMRVFGTLRALADVVIAGAETVRQEGYRPARARAEFAEARRAAGQASVPAVAVVSASLELDFSLPLFTAPAVPTLVLTGAAAAPDRIAAAERAGARVVIAGDGVGVDPARALRELAALGHTRLLTEGGPRLLGQFVAAGVLDELCLTLSPMLAAGDAQRIAGGPSVEVPRRFTLASLLEEEGFLFSRYRRA
>NZ_CP016795.1|WP_031042971.1|6308854_6309973_-|cell-division-protein-ZapE
MTTVSPSSTPASDRTPIAGTAPLSLCSREPRVPADRLVAEMVPPPRFDSVRFSTYLPDPNQPSQREAVHVLEEFANGLGQAPGPAAGRRGLFGFGRGRAPKVPAGPRGVYLDGGYGVGKTHLLASLWHATDAEPSRKAFGTFVELTNLVGALGFQQTVQTLSGHRLLCIDEFELDDPGDTVLVSSLLARLVEAGVALAATSNTLPGKLGEGRFAAADFMREIQGLSAHFRALRIDGEDYRHRGLPEAPAPYSEEQVTRAARATEGASLDDFTALLDHLARVHPSRYGALTDGLSAVCLTGVRPVPDQSTALRLVVLADRLYDREVPVLTSGEPFDRLFGEEMLKGGYRKKYFRAISRLTALARDAAPLVDAR
>NZ_CP016795.1|WP_070389399.1|6308097_6308502_-|hypothetical-protein
MFRGSNTRLRIPLLAALLVALQFLAPSASFAIAHTHRDVMANAQSGIIASGPSSHEERVACHDTGRSGHPHGPARVRGDRHRATTAPRPELPEHPLRGQRDPAADTPLLSGGAAGPRSRAAADHSPAALQVFRC
>NZ_CP016795.1|WP_070389407.1|6322093_6323527_-|HAMP-domain-containing-histidine-kinase
MIRRLWRAYRGLRLGTRLALGLGVLSLVVFAVVGTVLTAYMRDYLERQLADQMKLVQVVQSKDAAAHGTVQRKPYYGWYTAVYDVSGGSADLRTPAEVPADSRSLTELARTMARSEKDITRTVRIGGHGPYLLRACAVEPGVVLVSAAPMGDVEDTVDQLVTVQVIVFGLALAALVVFGRRMLRRGLKPLSDMASTAHGIASHDLTESAARLPLRADGRDGGQEVAELRTAFNTMLEHIDASLAVRAEAEQRLRRFVADASHELRTPLMSVRGYADLFQYAAANEPAERERHLARLRAEAARMGGLLDDLLLLARLDADEVEAPLRREDTDLTELVRQAADAFRAGHPGHPLTLRAGPAAVRAHLDPQRVRQVLDNLLTNAAVHTPPGTAVSVTLSGTPEAARVSVADTGPGIPAADRERIFDRFYRVDKARSRDRGGSGLGLSVAASLVRAHGGTVELTGEPGATVFTVTLPATGH
>NZ_CP016795.1|WP_031043000.1|6323523_6324267_-|response-regulator-transcription-factor
MGRGRPVAQYERVEKVRLLVVDDDPPIADLVATVARYEGWEAVTANSGEQALRLAGDFRPDIVVLDLMLPDVDGFGVLDRLRRSGTMVPVVFLTARDGVADRVAGLTRGGDDYLVKPFAVEELMARLRTVLRRSAGPGFQRSVLRVADLTMDEDTREVRRGERRLSLTPTEYEVLRYLMRKSPTVLTKAQILDHVWEYGFGGRSNVVELVVSRLRRKLDETAPDADGAEPLIQTVRGFGYALRRAAR
>NZ_CP016795.1|WP_070390459.1|6324355_6325705_+|ferredoxin-reductase-family-protein
MTTVPSAPHRPPPPAPALRPKAVARTGLYAILAANAVAVAVLFAQAGFAANTLVVLGRLTGLYGALLMAFQLVLVARLPWFDRRIGMDRLTSWHRWTGFAVLWTLLAHVVFITFGYGRSSGMDPLNQLVDLAETVEGVLRALVALALLVVVGAVSARAARRRMAYETWHFLHLYTYVAVVLAFTHQVAAGTSFTSSPAATAYWYTLWGAALGAVLAGRVVLPLWRNLRHRLRVTAVVPENDHVVSVYLTGRDLDRLPARAGQFFLWRFLTRDRWWQANPFSLSMAPDGRQLRLTVKTAGDGTAALRRIEPGTRVFAEGPYGAFTALHRTRPDTLLVAGGVGVTPIRALLEELPGHAVLVYRVATDRDAVLHDELRDLAHAKGAELHLVTGPAVPDRLGPRDLAALVPDVADRDVYVCGPPGMTTAVLATLRELGVPKAQIHAERFSLAG
>NZ_CP016795.1|WP_031043005.1|6325883_6326300_+|FMN-binding-protein
MKRALPVLVLSIAGLVPVWRYAPSPEAVTAPAASSEASVAPAAPSGGSTVAAGPVVGTEKGPVQVEVTFEERRITAVRMLQQPDHPQTTAAVPRLIEETLDAQSADVDTVSGATITSDGYRESLQAAIDAQAAQGAGA
>NZ_CP016795.1|WP_070389408.1|6326301_6327084_+|FAD:protein-FMN-transferase
MRRVEHVMGFPVSLRLDDPVGPGGVPEAAVDGVFAWLREVDARFSPFRPDSEVSRLDRGEVPRPSAELREVLDLCEEYRAATGGAFDVRLPGRGLDPCAVVKGWSVQRAAESLRAAGARGFCLNAGGDVVAAGGPWRVGVRHPEHADRLCTVLEVADGAVATSARYERGDHIVDGRTGRPATGLLAVTVVAPTLTEADAVATAAFAMGAEGVAWAAAREGCEVFAVDAGRRVLRTPGLPVAGAAPGPGPAAGKEHTATPV
>NZ_CP016795.1|WP_079155076.1|6327220_6328399_+|ABC-transporter-ATP-binding-protein
MIRMESVTKRYADGTVAVDRLSLEIPDRAITVLVGPSGCGKTTTLRMINRMVEPSEGTILLDGEDLQQQPVTTLRRSMGYVIQNAGLFQHRTILDNIATVPRMTGWGKQKSRERAAELMERVGLDSSLGKRYPYQLSGGQQQRVGVARALAADPPVLLMDEPFSAVDPVVRKGLQDELLRIQDELGKTIVFVTHDIDEAIKLGTMVAVMRTGGHLAQFAPPAELLSDPADAFVEDFLGADRGIRGLSFFPSTGLELATGPVVRVDATAEQLTAPGAPYLLVTDADDRPLGWAEPRELRAGEITADALLPYGRPFVAGTDSLRAALDCAVLSPTGWAVAVDAEGRVTGVASQATIGEAIRAAHGTGSTGGARAGERTGDAAADGPADVTKVAP
>NZ_CP016795.1|WP_031043013.1|6328395_6329100_+|ABC-transporter-permease-subunit
MNGFFDIPSDLDNTYFGLIGLHLREALLPVLVGLLAALPVAQLCVRFRWLYPPVLGVTTVFYAVPSLAVFVVLIDYTGQTELTVMIPLAVYSLVVLVPAIVDGVRSVPEETLAASTAMGFGPVRRYLQVQLPIAVPAILAGLRVAVSASISLVSVGALIGNQGALGNLLADAQKYGRPELAVNSVLTTAVLAVLCDALLVLVRNLLTPWMPRGGGGRRPKQAAERPEPQEAATR
>NZ_CP016795.1|WP_031043016.1|6329096_6329762_+|ABC-transporter-permease
MNVLNFVNAFFSDSAHWHGYDGIPQRLLEHVQYTLMALGLAAAVGLPVGLLTGHTGRGGNAVAFVATAARALPSFGLLVLIAVVVGIGLLPVMVPLVVLAIPPILVTTYEAVRSVDPSPVDAARGMGMHESSILFRVELPVALPLVLSGLRSAAIQVVSTATIAAYVSLGGIGRYIIDGLYQRNYEKVVGGASLVAVLALVTLAVFWAAGRLAVSPGVRRR
>NZ_CP016795.1|WP_037763261.1|6330919_6331459_-|ATP/GTP-binding-protein
MLIAGGFGVGKTTMVGSVSEIAPLRTEEPLTAAGLDIDDLAGIEEKRATTVALDFGRITITRDLVLYLFGTPGQQRFWFMWNDLAIGALGAVVLVDVRRPESSFAAIDFFERRGIPFVVGVNGFHGRHPYPAAEIREALALPDHVQVLLCDARERTSSRDVLIALIDQLIDAATGAAAS
>NZ_CP016795.1|WP_031043024.1|6331529_6331889_-|DUF742-domain-containing-protein
MTGGDAGGRLVRPFTLTGGRTRPSRADFTLITTVTACDPQPDRAARPQPEHLRILRLCARPVAVAEVAARLDLPVSVVVILLSDLVEADRITARPPHPVNLATPDLDLLQKVRDGLGRL

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP016795_7	7.2\|4754852\|18\|NZ_CP016795\|CRISPRCasFinder	4754852-4754869	18	NZ_CP016795.1	4754894-4754911	0	1.0

1. spacer 7.2|4754852|18|NZ_CP016795|CRISPRCasFinder matches to position: 4754894-4754911, mismatch: 0, identity: 1.0

ggaccccggccggcggtg	CRISPR spacer
ggaccccggccggcggtg	Protospacer
******************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP016795_2	2.2\|1537093\|25\|NZ_CP016795\|CRISPRCasFinder	1537093-1537117	25	NZ_CP010857	Marinovum algicola DG 898 plasmid pMaD2, complete sequence	237019-237043	6	0.76
NZ_CP016795_6	6.1\|2272634\|30\|NZ_CP016795\|CRISPRCasFinder	2272634-2272663	30	NC_010625	Paraburkholderia phymatum STM815 plasmid pBPHY01, complete sequence	849418-849447	7	0.767
NZ_CP016795_6	6.1\|2272634\|30\|NZ_CP016795\|CRISPRCasFinder	2272634-2272663	30	NC_013857	Azospirillum sp. B510 plasmid pAB510c, complete sequence	207231-207260	7	0.767
NZ_CP016795_6	6.1\|2272634\|30\|NZ_CP016795\|CRISPRCasFinder	2272634-2272663	30	NZ_CP054615	Azospirillum oryzae strain KACC 14407 plasmid unnamed1, complete sequence	164266-164295	7	0.767
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	KX853513	Uncultured virus isolate Rctr41k, partial genome	14502-14533	7	0.781
NZ_CP016795_1	1.2\|755599\|34\|NZ_CP016795\|CRISPRCasFinder	755599-755632	34	NZ_CP021374	Rhizobium sp. ACO-34A plasmid pRACO34Ab, complete sequence	291564-291597	8	0.765
NZ_CP016795_6	6.1\|2272634\|30\|NZ_CP016795\|CRISPRCasFinder	2272634-2272663	30	NZ_CP019319	Tateyamaria omphalii strain DOK1-4 plasmid pDOK1-4-7, complete sequence	11969-11998	8	0.733
NZ_CP016795_6	6.1\|2272634\|30\|NZ_CP016795\|CRISPRCasFinder	2272634-2272663	30	NZ_LT969519	Pseudomonas aeruginosa isolate RW109 genome assembly, plasmid: RW109 plasmid 1	314521-314550	8	0.733
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NZ_CP035513	Haematobacter massiliensis strain OT1 plasmid pOT1-3, complete sequence	237202-237233	8	0.75
NZ_CP016795_6	6.1\|2272634\|30\|NZ_CP016795\|CRISPRCasFinder	2272634-2272663	30	NC_005241	Cupriavidus necator H16 megaplasmid pHG1, complete sequence	145899-145928	9	0.7
NZ_CP016795_6	6.1\|2272634\|30\|NZ_CP016795\|CRISPRCasFinder	2272634-2272663	30	NZ_CP039289	Cupriavidus necator H16 plasmid pHG1, complete sequence	145898-145927	9	0.7
NZ_CP016795_6	6.1\|2272634\|30\|NZ_CP016795\|CRISPRCasFinder	2272634-2272663	30	NZ_CP027237	Actinomyces sp. oral taxon 897 strain F0631 plasmid unnamed1, complete sequence	2453-2482	9	0.7
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_016587	Azospirillum lipoferum 4B plasmid AZO_p4, complete sequence	465210-465241	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	KX550443	Mycobacterium phage Magnito, complete genome	28154-28185	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MN369760	Mycobacterium phage KyMonks1A, complete genome	29005-29036	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MH371123	Mycobacterium phage Sandalphon, complete genome	25474-25505	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MH371110	Mycobacterium phage Magnar, complete genome	28402-28433	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MT889374	Mycobacterium phage Firehouse51, complete genome	25477-25508	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MN369755	Mycobacterium phage Minnie, complete genome	25460-25491	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MN586000	Mycobacterium phage Sagefire, complete genome	29512-29543	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MH576974	Mycobacterium phage Sibs6, complete genome	27653-27684	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MK524531	Mycobacterium phage Rutherferd, complete genome	29340-29371	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MN585997	Mycobacterium phage Traft412, complete genome	29582-29613	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_004688	Mycobacterium phage Omega, complete genome	38968-38999	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MK524506	Mycobacterium phage Zeuska, complete genome	29214-29245	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	AY129338	Mycobacterium virus Omega, complete genome	38968-38999	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	KR080201	Mycobacterium phage Nerujay, complete genome	29144-29175	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MH651178	Mycobacterium phage KristaRAM, complete genome	25591-25622	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MH590595	Mycobacterium phage NEHalo, complete genome	28476-28507	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MK359304	Mycobacterium phage SpikeBT, complete genome	29582-29613	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	JN572689	Mycobacterium phage Perseus, complete genome	29563-29594	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	KM597531	Mycobacterium phage Abrogate, complete genome	29444-29475	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_023723	Mycobacterium phage Aeneas, complete genome	29022-29053	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_028941	Mycobacterium phage Turj99, complete genome	28424-28455	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MN428054	Mycobacterium phage JackSparrow, complete genome	29029-29060	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_022329	Mycobacterium phage PhrostyMug, complete genome	28726-28757	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MN369752	Mycobacterium phage Flathead, complete genome	24785-24816	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_042321	Mycobacterium virus Lesedi, complete genome	28430-28461	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	EU744249	Mycobacterium phage Lockley, complete genome	28617-28648	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	HQ728524	Mycobacterium phage Wee, complete genome	25490-25521	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	MK359300	Mycobacterium phage AFIS, complete genome	28769-28800	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_042327	Mycobacterium virus BBPiebs31, complete genome	28986-29017	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	JN020142	Mycobacterium phage Mutaforma13, complete genome	24964-24995	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	KF279416	Mycobacterium phage SargentShorty9, complete genome	28735-28766	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	JQ698665	Mycobacterium phage Nepal, complete genome	29024-29055	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_023728	Mycobacterium virus DeadP, complete genome	24949-24980	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	EU744252	Mycobacterium phage DD5, complete genome	29383-29414	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	NC_025433	Mycobacteriophage Taj, complete genome	24951-24982	9	0.719
NZ_CP016795_8	8.1\|6320838\|32\|NZ_CP016795\|CRISPRCasFinder	6320838-6320869	32	KF024724	Mycobacterium phage Trouble, complete genome	29485-29516	9	0.719

1. spacer 2.2|1537093|25|NZ_CP016795|CRISPRCasFinder matches to NZ_CP010857 (Marinovum algicola DG 898 plasmid pMaD2, complete sequence) position: , mismatch: 6, identity: 0.76

aagtaacggaagcagcggaagaaac	CRISPR spacer
cctggccggaagcagcggaagaaac	Protospacer
    . *******************

2. spacer 6.1|2272634|30|NZ_CP016795|CRISPRCasFinder matches to NC_010625 (Paraburkholderia phymatum STM815 plasmid pBPHY01, complete sequence) position: , mismatch: 7, identity: 0.767

cacctgcgcgccgtgggtcaggtcggtggt	CRISPR spacer
caccttcgcgccgtgcgtcaggtggccgcc	Protospacer
***** ********* ******* * .* .

3. spacer 6.1|2272634|30|NZ_CP016795|CRISPRCasFinder matches to NC_013857 (Azospirillum sp. B510 plasmid pAB510c, complete sequence) position: , mismatch: 7, identity: 0.767

cacctgcgcgccgtgggtcaggtcggtggt	CRISPR spacer
caccggcgagccgtgggtcaggtggccgcc	Protospacer
**** *** ************** * .* .

4. spacer 6.1|2272634|30|NZ_CP016795|CRISPRCasFinder matches to NZ_CP054615 (Azospirillum oryzae strain KACC 14407 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.767

cacctgc-----gcgccgtgggtcaggtcggtggt	CRISPR spacer
-----gctgaaggcgccgggggtcaggtcgatggt	Protospacer
     **     ****** ***********.****

5. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to KX853513 (Uncultured virus isolate Rctr41k, partial genome) position: , mismatch: 7, identity: 0.781

gtccgcac---cgcctcctcctccgtccgcaccat	CRISPR spacer
---cgcgcgcgcgcctcctccaccttccgcaccag	Protospacer
   ***.*   ********** ** *********

6. spacer 1.2|755599|34|NZ_CP016795|CRISPRCasFinder matches to NZ_CP021374 (Rhizobium sp. ACO-34A plasmid pRACO34Ab, complete sequence) position: , mismatch: 8, identity: 0.765

acgacggcggggcccgtcagccgagccagcccgg------	CRISPR spacer
acgagggcggggctcgtcagccga------ccggcagtca	Protospacer
**** ********.**********      ****

7. spacer 6.1|2272634|30|NZ_CP016795|CRISPRCasFinder matches to NZ_CP019319 (Tateyamaria omphalii strain DOK1-4 plasmid pDOK1-4-7, complete sequence) position: , mismatch: 8, identity: 0.733

cacctgcgcgccgtgggtcaggtcggtggt	CRISPR spacer
atgctgcacgccgcgggtcaggtcggtccg	Protospacer
   ****.*****.*************

8. spacer 6.1|2272634|30|NZ_CP016795|CRISPRCasFinder matches to NZ_LT969519 (Pseudomonas aeruginosa isolate RW109 genome assembly, plasmid: RW109 plasmid 1) position: , mismatch: 8, identity: 0.733

cacctgcgcgccgtgggtcaggtcggtggt	CRISPR spacer
caccttggcgccgtgggtcaggtggccacc	Protospacer
*****  **************** * .. .

9. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NZ_CP035513 (Haematobacter massiliensis strain OT1 plasmid pOT1-3, complete sequence) position: , mismatch: 8, identity: 0.75

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
atgcgccgcgcctcctcctccgtccgggcctc	Protospacer
.* ***  ****************** .** .

10. spacer 6.1|2272634|30|NZ_CP016795|CRISPRCasFinder matches to NC_005241 (Cupriavidus necator H16 megaplasmid pHG1, complete sequence) position: , mismatch: 9, identity: 0.7

cacctgcgcgccgtgggtcaggtcggtggt	CRISPR spacer
gcgtggcgcgccgtgggttaggttggtgtg	Protospacer
   . *************.****.****

11. spacer 6.1|2272634|30|NZ_CP016795|CRISPRCasFinder matches to NZ_CP039289 (Cupriavidus necator H16 plasmid pHG1, complete sequence) position: , mismatch: 9, identity: 0.7

cacctgcgcgccgtgggtcaggtcggtggt	CRISPR spacer
gcgtggcgcgccgtgggttaggttggtgtg	Protospacer
   . *************.****.****

12. spacer 6.1|2272634|30|NZ_CP016795|CRISPRCasFinder matches to NZ_CP027237 (Actinomyces sp. oral taxon 897 strain F0631 plasmid unnamed1, complete sequence) position: , mismatch: 9, identity: 0.7

cacctgcgcgccgtgggtcaggtcggtggt	CRISPR spacer
gatgctggcgccctgggtcaggtcggtgac	Protospacer
 *. .  ***** ***************..

13. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_016587 (Azospirillum lipoferum 4B plasmid AZO_p4, complete sequence) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
gcgcgcagcgcctcctcctccgcccggccggg	Protospacer
*. **** **************.***  * .

14. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to KX550443 (Mycobacterium phage Magnito, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

15. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MN369760 (Mycobacterium phage KyMonks1A, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

16. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MH371123 (Mycobacterium phage Sandalphon, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

17. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MH371110 (Mycobacterium phage Magnar, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

18. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MT889374 (Mycobacterium phage Firehouse51, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

19. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MN369755 (Mycobacterium phage Minnie, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

20. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MN586000 (Mycobacterium phage Sagefire, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

21. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MH576974 (Mycobacterium phage Sibs6, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

22. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MK524531 (Mycobacterium phage Rutherferd, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

23. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MN585997 (Mycobacterium phage Traft412, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

24. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_004688 (Mycobacterium phage Omega, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

25. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MK524506 (Mycobacterium phage Zeuska, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

26. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to AY129338 (Mycobacterium virus Omega, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

27. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to KR080201 (Mycobacterium phage Nerujay, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

28. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MH651178 (Mycobacterium phage KristaRAM, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

29. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MH590595 (Mycobacterium phage NEHalo, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

30. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MK359304 (Mycobacterium phage SpikeBT, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

31. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to JN572689 (Mycobacterium phage Perseus, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

32. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to KM597531 (Mycobacterium phage Abrogate, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

33. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_023723 (Mycobacterium phage Aeneas, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

34. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_028941 (Mycobacterium phage Turj99, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

35. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MN428054 (Mycobacterium phage JackSparrow, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

36. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_022329 (Mycobacterium phage PhrostyMug, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

37. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MN369752 (Mycobacterium phage Flathead, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

38. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_042321 (Mycobacterium virus Lesedi, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

39. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to EU744249 (Mycobacterium phage Lockley, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

40. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to HQ728524 (Mycobacterium phage Wee, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

41. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to MK359300 (Mycobacterium phage AFIS, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

42. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_042327 (Mycobacterium virus BBPiebs31, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

43. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to JN020142 (Mycobacterium phage Mutaforma13, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

44. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to KF279416 (Mycobacterium phage SargentShorty9, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

45. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to JQ698665 (Mycobacterium phage Nepal, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

46. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_023728 (Mycobacterium virus DeadP, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

47. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to EU744252 (Mycobacterium phage DD5, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

48. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to NC_025433 (Mycobacteriophage Taj, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

49. spacer 8.1|6320838|32|NZ_CP016795|CRISPRCasFinder matches to KF024724 (Mycobacterium phage Trouble, complete genome) position: , mismatch: 9, identity: 0.719

gtccgcaccgcctcctcctccgtccgcaccat	CRISPR spacer
aacccggccgcctcctccgccgcccgcacctg	Protospacer
. **  .*********** ***.*******

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

3438672 : 3493472

Bacillus_phage(42.86%)

tRNA,protease,plate,tail

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_037769751.1\|3438672_3440274_+\|tail	phage tail sheath family protein	J9PVC2	Bacillus_phage	3.1e-62	33.0
WP_031038304.1\|3440380_3440827_+\|tail	phage tail protein	NA	NA	NA	NA
WP_031038305.1\|3440826_3441357_+	hypothetical protein	NA	NA	NA	NA
WP_164711394.1\|3441353_3441512_+	hypothetical protein	NA	NA	NA	NA
WP_070388404.1\|3441810_3443061_-	hypothetical protein	NA	NA	NA	NA
WP_123937895.1\|3443864_3444452_-	hypothetical protein	NA	NA	NA	NA
WP_107405301.1\|3445010_3445592_+	extensin	NA	NA	NA	NA
WP_031045606.1\|3445671_3446094_+\|tail	phage tail protein	NA	NA	NA	NA
WP_031045602.1\|3446126_3446846_+	LysM peptidoglycan-binding domain-containing protein	NA	NA	NA	NA
WP_037769753.1\|3446845_3448762_+	VgrG-related protein	NA	NA	NA	NA
WP_031045595.1\|3448832_3449303_+	GPW/gp25 family protein	A0A1D8KR06	Synechococcus_phage	2.8e-11	30.5
WP_031045592.1\|3449302_3451261_+\|plate	putative baseplate assembly protein	NA	NA	NA	NA
WP_051159849.1\|3451320_3451830_+\|tail	phage tail protein	NA	NA	NA	NA
WP_070388406.1\|3451826_3453194_+	zinc ribbon domain-containing protein	NA	NA	NA	NA
WP_070388407.1\|3453643_3455314_+	alpha/beta hydrolase	NA	NA	NA	NA
WP_079154950.1\|3455403_3456228_+	putative protein N(5)-glutamine methyltransferase	NA	NA	NA	NA
WP_031045577.1\|3456558_3457695_+	diacetylchitobiose ABC transporter ATP-binding protein MsiK	Q6GZ03	Mycoplasma_phage	3.2e-21	38.4
WP_031045575.1\|3457960_3458416_+	hypothetical protein	NA	NA	NA	NA
WP_031045573.1\|3458494_3459232_+	nucleotidyltransferase family protein	NA	NA	NA	NA
WP_079154951.1\|3460707_3461853_-	diaminopimelate epimerase	NA	NA	NA	NA
WP_070390302.1\|3461849_3462197_-	hypothetical protein	NA	NA	NA	NA
WP_070388411.1\|3462457_3463324_-	hypothetical protein	NA	NA	NA	NA
WP_079155190.1\|3464599_3465013_-	ATP-binding protein	NA	NA	NA	NA
WP_070388414.1\|3465180_3466056_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_070388415.1\|3466052_3466262_+	DUF397 domain-containing protein	NA	NA	NA	NA
WP_079154952.1\|3466332_3468045_-	DoxX family membrane protein	NA	NA	NA	NA
WP_037769772.1\|3468173_3469115_-	23S rRNA (guanosine(2251)-2'-O)-methyltransferase RlmB	NA	NA	NA	NA
WP_070388417.1\|3469237_3470638_-\|tRNA	cysteine--tRNA ligase	A0A1V0SAQ2	Catovirus	1.3e-40	29.9
WP_070388418.1\|3470966_3471491_-	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase	NA	NA	NA	NA
WP_070388419.1\|3471480_3472269_-	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase	NA	NA	NA	NA
WP_003953493.1\|3472611_3473094_-	CarD family transcriptional regulator	NA	NA	NA	NA
WP_078536021.1\|3473055_3473268_+	hypothetical protein	NA	NA	NA	NA
WP_037769780.1\|3473736_3474474_+	hypothetical protein	NA	NA	NA	NA
WP_003974745.1\|3474569_3475250_-	response regulator transcription factor	W8CYM9	Bacillus_phage	1.1e-40	39.0
WP_031045533.1\|3475246_3476518_-	two-component sensor histidine kinase	W8CYF6	Bacillus_phage	1.6e-29	31.5
WP_037769786.1\|3476742_3477432_+	phosphate signaling complex protein PhoU	NA	NA	NA	NA
WP_164711395.1\|3477547_3477703_+	hypothetical protein	NA	NA	NA	NA
WP_070388420.1\|3478006_3478363_+	hypothetical protein	NA	NA	NA	NA
WP_070388421.1\|3478412_3479681_+	lanthionine synthetase C family protein	NA	NA	NA	NA
WP_031045521.1\|3480694_3481075_-	VOC family protein	NA	NA	NA	NA
WP_070388422.1\|3481376_3482864_+	peptide MFS transporter	A0A0P0IY73	Acinetobacter_phage	2.1e-60	34.5
WP_031045512.1\|3486009_3486444_+	SgcJ/EcaC family oxidoreductase	NA	NA	NA	NA
WP_070388423.1\|3486591_3487563_-	GntR family transcriptional regulator	NA	NA	NA	NA
WP_070388424.1\|3487749_3488979_+	NAD(P)-binding protein	NA	NA	NA	NA
WP_031045504.1\|3489031_3489487_+	VOC family protein	NA	NA	NA	NA
WP_070390303.1\|3489618_3490599_+	hypothetical protein	NA	NA	NA	NA
WP_070388425.1\|3490689_3491652_-	aminoglycoside phosphotransferase family protein	NA	NA	NA	NA
WP_070390304.1\|3491897_3493472_+\|protease	trypsin-like serine protease	NA	NA	NA	NA

DBSCAN-SWA_2

8042388 : 8090083

Mycobacterium_phage(33.33%)

integrase,transposase

attL 8062416:8062432|attR 8095690:8095706

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_070387189.1\|8042388_8043714_+\|transposase	ISL3 family transposase	A0A2H4PDF8	Mycobacterium_phage	7.0e-193	76.3
WP_158710948.1\|8044107_8044269_+	hypothetical protein	NA	NA	NA	NA
WP_070387188.1\|8045211_8046216_+	nucleotidyltransferase	NA	NA	NA	NA
WP_070387187.1\|8046212_8047679_+	ThiF family adenylyltransferase	NA	NA	NA	NA
WP_070387186.1\|8048718_8049045_-	hypothetical protein	NA	NA	NA	NA
WP_070390084.1\|8049151_8050225_-	ATP/GTP-binding protein	NA	NA	NA	NA
WP_070390085.1\|8050224_8052621_-\|integrase,transposase	DDE-type integrase/transposase/recombinase	NA	NA	NA	NA
WP_070390551.1\|8052617_8053325_-	hypothetical protein	NA	NA	NA	NA
WP_123937986.1\|8054468_8058035_-	DNA-binding protein	NA	NA	NA	NA
WP_070390552.1\|8058050_8059061_-	AAA family ATPase	NA	NA	NA	NA
WP_107405229.1\|8061266_8062250_-\|transposase	TnsA-like heteromeric transposase endonuclease subunit	NA	NA	NA	NA
8062416:8062432	attL	NA	NA	NA	NA
WP_079155150.1\|8063901_8064456_-	GNAT family N-acetyltransferase	NA	NA	NA	NA
WP_070390090.1\|8064889_8065825_+	hypothetical protein	NA	NA	NA	NA
WP_070390554.1\|8066764_8067721_+\|transposase	IS481 family transposase	NA	NA	NA	NA
WP_164711440.1\|8067750_8070510_+	serine/threonine protein kinase	M1I231	Acanthocystis_turfacea_Chlorella_virus	2.5e-14	31.8
WP_070390092.1\|8070564_8071245_+	hypothetical protein	NA	NA	NA	NA
WP_070390093.1\|8071241_8073329_+	hypothetical protein	NA	NA	NA	NA
WP_070390094.1\|8073378_8075418_+	hypothetical protein	NA	NA	NA	NA
WP_079155152.1\|8075505_8077569_-	helicase	A0A2H4UVA3	Bodo_saltans_virus	2.4e-06	28.7
WP_070390555.1\|8078859_8081727_+	CRISPR-associated endonuclease Cas3''	NA	NA	NA	NA
WP_164711419.1\|8082042_8083251_-\|transposase	IS701 family transposase	NA	NA	NA	NA
WP_079155248.1\|8083538_8085026_+	type I-E CRISPR-associated protein Cse1/CasA	NA	NA	NA	NA
WP_051159998.1\|8085025_8085670_+	type I-E CRISPR-associated protein Cse2/CasB	NA	NA	NA	NA
WP_037772151.1\|8085887_8087051_+	type I-E CRISPR-associated protein Cas7/Cse4/CasC	NA	NA	NA	NA
WP_037772153.1\|8087047_8087857_+	type I-E CRISPR-associated protein Cas5/CasD	NA	NA	NA	NA
WP_070390095.1\|8087853_8088498_+	type I-E CRISPR-associated protein Cas6/Cse3/CasE	NA	NA	NA	NA
WP_063741599.1\|8088523_8090083_+\|integrase,transposase	DDE-type integrase/transposase/recombinase	NA	NA	NA	NA
8095690:8095706	attR	NA	NA	NA	NA

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP016795

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection