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_LT906452	Legionella pneumophila strain NCTC11985 chromosome 1	1 crisprs	DEDDh,DinG,cas3,PD-DExK,WYL,csa3	0	0	3	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_LT906452_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906452_1

2770606-2770798

Orphan

Consensus_repeat	Method
TGACTTCACTGGATTTAAGCTGGAATG	PILER-CR

2 spacers

The CRISPR arrays of NZ_LT906452_1

>merge|NZ_LT906452|1|2770606-2770798|PILER-CR
ACTGCCCTGGATTTAAGCTGGAATGATTTAAGTAGTAAAAGCAGCTCAGAATTAGCGCAAGTCCTCGCAGCTATCCCTGCCCATTTGACATCATTAGATTTAAGCTGGAATGCTCTATACCGTAATCCAGGTTTAACTCGATCCTCTGCTGCTATTCTTGTTGGTATGACTTCACTGAATTTAAGCTGGAATT

>NZ_LT906452|1|1|2770606-2770798|PILER-CR
ACTGCCCTGGATTTAAGCTGGAATGAT	TTAAGTAGTAAAAGCAGCTCAGAATTAGCGCAAGTCCTCGCAGCTATCCCTGCCCATTTG
ACATCATTAGATTTAAGCTGGAATGCT	CTATACCGTAATCCAGGTTTAACTCGATCCTCTGCTGCTATTCTTGTTGGTATG
ACTTCACTGAATTTAAGCTGGAATT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906452.1\|WP_014842435.1\|2772904_2773825_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176155
NZ_LT906452.1\|WP_014842441.1\|2779982_2780288_-\|lpg2407-family-Dot/Icm-T4SS-effector	unknown	unknown	unknown
NZ_LT906452.1\|WP_014842439.1\|2777215_2778370_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906452.1\|WP_014842438.1\|2776730_2777132_+\|NUDIX-hydrolase	unknown	unknown	gnl\|CDD\|239217
NZ_LT906452.1\|WP_014842436.1\|2774008_2775523_-\|cytochrome-P450	unknown	unknown	gnl\|CDD\|365848
NZ_LT906452.1\|WP_014842434.1\|2771422_2772928_+\|serine-hydrolase	unknown	unknown	gnl\|CDD\|365903
NZ_LT906452.1\|WP_027220836.1\|2767384_2768731_-\|YdgA-family-protein	unknown	unknown	gnl\|CDD\|377603
NZ_LT906452.1\|WP_014842423.1\|2758722_2759955_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340927
NZ_LT906452.1\|WP_014842442.1\|2780510_2781170_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906452.1\|WP_014842437.1\|2775819_2776734_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906452.1\|WP_014842431.1\|2766623_2767196_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|275224
NZ_LT906452.1\|WP_014842440.1\|2778703_2779801_+\|Dot/Icm-T4SS-effector-Lem23	unknown	unknown	unknown
NZ_LT906452.1\|WP_014842422.1\|2756884_2758162_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906452.1\|WP_014842424.1\|2759995_2761300_-\|Dot/Icm-T4SS-effector-SdbC	unknown	unknown	unknown
NZ_LT906452.1\|WP_014842443.1\|2781495_2782314_+\|Dot/Icm-type-IV-secretion-system-effector-Ceg29	unknown	unknown	gnl\|CDD\|372614
NZ_LT906452.1\|WP_014842428.1\|2763438_2763798_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906452.1\|WP_014842425.1\|2761569_2762454_+\|Dot/Icm-T4SS-effector-LegL6	unknown	unknown	gnl\|CDD\|238064
NZ_LT906452.1\|WP_014842430.1\|2765369_2766569_-\|M23-family-metallopeptidase	unknown	unknown	gnl\|CDD\|366703
NZ_LT906452.1\|WP_011216283.1\|2762574_2763039_-\|bacterioferritin	unknown	unknown	gnl\|CDD\|225104
NZ_LT906452.1\|WP_014842429.1\|2763925_2764996_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|316372

Protein	Function_ID	Function_description	E-value
NZ_LT906452.1\|WP_014842435.1\|2772904_2773825_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176155	cd08466, PBP2_LeuO, The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an activator of leucine synthesis operon, contains the type 2 periplasmic binding fold. LeuO, a LysR-type transcriptional regulator, was originally identified as an activator of the leucine synthesis operon (leuABCD). Subsequently, LeuO was found to be not a specific regulator of the leu gene but a global regulator of unrelated various genes. LeuO activates bglGFB (utilization of beta-D-glucoside) and represses cadCBA (lysine decarboxylation) and dsrA (encoding a regulatory small RNA for translational control of rpoS and hns). LeuO also regulates the yjjQ-bglJ operon which coding for a LuxR-type transcription factor. In Salmonella enterica serovar Typhi, LeuO is a positive regulator of ompS1 (encoding an outer membrane), ompS2 (encoding a pathogenicity determinant), and assT, while LeuO represses the expression of OmpX and Tpx. Both osmS1 and osmS2 influence virulence in the mouse model of Salmonella. In Vibrio cholerae, LeuO is involved in control of biofilm formation and in the stringent response. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. 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.	5.08073e-60
NZ_LT906452.1\|WP_014842436.1\|2774008_2775523_-\|cytochrome-P450	gnl\|CDD\|365848	pfam00067, p450, Cytochrome P450. Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.	6.65304e-21
NZ_LT906452.1\|WP_014842434.1\|2771422_2772928_+\|serine-hydrolase	gnl\|CDD\|365903	pfam00144, Beta-lactamase, Beta-lactamase. This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	1.04514e-19
NZ_LT906452.1\|WP_014842438.1\|2776730_2777132_+\|NUDIX-hydrolase	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.	3.24357e-18
NZ_LT906452.1\|WP_014842423.1\|2758722_2759955_-\|MFS-transporter	gnl\|CDD\|340927	cd17369, MFS_ShiA_like, Shikimate transporter and similar proteins of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.76982e-78
NZ_LT906452.1\|WP_014842430.1\|2765369_2766569_-\|M23-family-metallopeptidase	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	4.14344e-17
NZ_LT906452.1\|WP_014842443.1\|2781495_2782314_+\|Dot/Icm-type-IV-secretion-system-effector-Ceg29	gnl\|CDD\|372614	pfam13475, DUF4116, Domain of unknown function (DUF4116).	2.09851e-05
NZ_LT906452.1\|WP_014842425.1\|2761569_2762454_+\|Dot/Icm-T4SS-effector-LegL6	gnl\|CDD\|238064	cd00116, LRR_RI, Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).	1.00468e-06
NZ_LT906452.1\|WP_011216283.1\|2762574_2763039_-\|bacterioferritin	gnl\|CDD\|225104	COG2193, Bfr, Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism].	2.23076e-20
NZ_LT906452.1\|WP_014842431.1\|2766623_2767196_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|275224	TIGR04431, aminoglycoside-6'-N-acetyltransferase_type_Ib, aminoglycoside N(6')-acetyltransferase, AacA4 family. Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model. [Cellular processes, Toxin production and resistance].	4.30832e-20
NZ_LT906452.1\|WP_027220836.1\|2767384_2768731_-\|YdgA-family-protein	gnl\|CDD\|377603	pfam06097, DUF945, Bacterial protein of unknown function (DUF945). This family consists of several hypothetical bacterial proteins of unknown function.	9.17941e-75
NZ_LT906452.1\|WP_014842429.1\|2763925_2764996_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|316372	pfam13847, Methyltransf_31, Methyltransferase domain. This family appears to have methyltransferase activity.	4.9227e-26

>NZ_LT906452.1|WP_027220836.1|2767384_2768731_-|YdgA-family-protein
MRKWIISLLLLIIIVLCSYPIIGMMALSTVKKNVDNIPKSPFLTWQLKDNQSGWFCSTAVLNLLVDLPAQENKDAQGNIKIQPALHLSMDFPMIVRHGPFIMTNNGLRFGLAWVTTKPETHYGALINYLNQTAVSYSLPSINMKGTNNGDQGKFVFVWQGLSASLKVNPRIDKASGHVTMYGMSTQVQETDVRIGKVKVNFALNRYMDNLWLGDSSIMLSSISTVTNSQPVFDLQNLGMDAWAGVNNNLLDFNLQLSLNKFLMNNNSYGPGQLKIEVKNLDPQAMAKLNHLNYDYPSNQIAILAEIFNLLSKGATLNLNQELDTPQGHLSSSLNLALTKSSFSNPGDLLQNLKGNGQFKAPIKLVKQLLFESIKSKTATPAADMSQSQVTEPLVDADAEAHKQTEELLQKLVSKGILKVEGDYYQASFTLENTKFTVNGQPFDPALLN
>NZ_LT906452.1|WP_014842431.1|2766623_2767196_-|GNAT-family-N-acetyltransferase
MALIRDSKSQVMSVFKFQPLGIKDLNQLYQWFQEPIINHWYARDKSWSLDEITEKYEPRIAGMEHVPSFIVYKYDLPFGFVQFYLLTDSLPDGIDGYESLLFEKYNPRDLAGIDLFIAESEGRGRGLGVELINRFIDKFLTRFKAVVVDPDVNNQQAIRCYEKAGFQQTGFSQDPNHLIMIKPLSLITGN
>NZ_LT906452.1|WP_014842430.1|2765369_2766569_-|M23-family-metallopeptidase
MIKSFRVTIFLFLVSGLILARDMHAFPSGLESNQDKLVYFQLEAETFYSPKPVTIEGQLYLTYEVFLANVGDYLFSLENVEVLNGRKPYKVLFSYNQEELRKMIYSFSGHSNHLTSDLTLRPGERGLLFFMVKFDSLDEIPEKIMHRFHLYSSKTKISEEDVRYSFLAAPAYVKITKPLVIANPLDGKHWMAINGPSNHSIHRRARVAAHGIVYYPERYAIDFMQFGADGHVYKENPNKNENYYSYGANVYSVADGEVVAVYDGVPDNTPPGRDYPVTLSNMAGNHVIIKIGKHQYALYAHLIPHSIKVTKGELVRKNQLIAKLGNSGNSDAPHLHFHVIDKPSPLIGQGIPYAFEHFSTEEYRFAGDEWESPIVYEGRLTEHHHELVHENALMNFEEK
>NZ_LT906452.1|WP_014842429.1|2763925_2764996_-|class-I-SAM-dependent-methyltransferase
MKTGRFDQARADAFAERLLSVLNDAALTLMISIGHRTGLFDVMDELDFASSEVIAEAAGCNERYVREWLNALVVGGIVDYDAHAKAYQLPAEHASFLTRKSSPQNMAVVAQFISVLAYVENGVVHAFKHGGGVPYEAYHRFHEVMAEESGQTILSSLTDKILPMVHGLVDKLNQGIQVLDIGCGYGRALILMAKTYPQSQFTGYDLCDETIAHAVHAAKKNKIQNIHFEKMDLSVWDEQEKYDLITSFDVIHDQAKPAQVLRNVFKALKPQGIFLMQDIKTSSDVAGNVHHPLGALIYTISCMHCMTVSLSQNGLGLGAAWGEELAEKMLVEAGFGKIEKHYLEHDIMNTYYVMRK
>NZ_LT906452.1|WP_014842428.1|2763438_2763798_+|hypothetical-protein
MSNKAKNTHLKNGDSQTKQAYTNQASPLFFSQKQITPSSGTLETKKPQEGKQPTQEISLETTTDILLAAILQELKTQNMIELMKLKAQQEQEQEELETIEAMKEKDDARFNEIRQTMYA
>NZ_LT906452.1|WP_011216283.1|2762574_2763039_-|bacterioferritin
MKHRRSETQDIDDAIIKTLNKLLEIELAGVVRYTHYSFMVFGFNRIPICKWMRDQAQESLNHAHLIGELITHFSYHPTLKIGKLLETHEHNISNILEESLEHERQSLDLYYQLLQYSENKSVLVEEFARQMIQEEEMHLGEISKMLNSPTTFKD
>NZ_LT906452.1|WP_014842425.1|2761569_2762454_+|Dot/Icm-T4SS-effector-LegL6
MFYELILTRTSNLIQEFISIPHGVISLDLSLNELGNISNAELIQAFQYIPDSVISLDLANNHLCDKSGAELAQLLAAIPANVTSLNLSCNDLHKKSGAELAQAFAAIPASVTSLNLHCNYLGNNRGVELAQAFAAIPENVTSLDLSMNYFDLESSADLSQIFTSIPPHVASLNLSFNSLHEVPFEKLVLLKDSLKHVQTVYFSFYSVKEMSKEQRRALGAAFPNTQKIILIDDYGHEIQPSITISNLIRELSGKADAPSLLNQCILFTQRHQKDSDNKIIPKELEESIRTFNSR
>NZ_LT906452.1|WP_014842424.1|2759995_2761300_-|Dot/Icm-T4SS-effector-SdbC
MPNSSIQIWLQRQIALRTFPPNREDWYVKNGFGNSEMSLEERFACFVEVMRQEDSPYHEQLSGIDFHRFEIEVTLANQKTCMTEVIGFQNNSNQSSSLLNEKVKAVGKGKHVIYFTGIGTQYQDCLIDIAKAVQITGAHYYAFEYPGMRKLGGEVLEVNDMVNTGIALANTLLEKGISIDDILFQGDSFGAAVAKKVSDQFKLQSNVTVRCILNNTFSTFQAAVEGNLGAFSTLRYTVRPLLRYTGWDIRPGDNYGLDTPYQIHINHTGDLTLGAGHATLAESVESNSQLEHFVDPCPEEYRIKRDIYKQWHWASLSEQGIRFLETKYGRNSDGQLDTHLADLYLLKYDTGLGVYESFICKYLEDSNDYIANHPQKLSLEELPSPLESETVSLGQLIVSVLPSRPSIAGFFGRPKPVKDEVDAENQAQKSIELK
>NZ_LT906452.1|WP_014842423.1|2758722_2759955_-|MFS-transporter
MDKKIIAAASFGTLFEMYDYAIYGFMAPILAPLFFPATDKHTALIATFGIFAAGFLVRPFSAYWLGDLGDKIGRKKTLTMTLMVMTFSSSFIGLLPTYQEAGILAPILLTLCRLTQGVSVAGEMTLASIYIYENVNMRHKGLAVSFVTLGSICGLLLAIIVSKITLIFFSSQFPDFLWRFPFLIGIFVGFIGLYLRSQTRELTDFAKVIVQRQSHPILNAWRYRKKAIAAIFLLAIYCNSSFYTFFVYMPSYLQQQELPLTTAMDVIIIGMICYSMGLLLSGFTSDILGRRFPLAVSLIATLCTVLVINYLINTGTLLQITVACSVLAVIISFFIGSAFTASLEQLPQEERASGFTLFFNLSNSLFGGTAPLIILLLSYAFIHFAFSIYLMVMALLTLPALWLIQEKGTN
>NZ_LT906452.1|WP_014842422.1|2756884_2758162_-|hypothetical-protein
MKNNKRTNDQNADQKSSQYIYVEKKEIGGIDTEIITESHYPIPWGSASERPLDYYEKQSKIITYYKEDIDLDGNPFSKRIEIEIPEVEEGENRHRRIKVKVDGNPIIFQDDNILDMDETFNIRDVNLLIHMVLNNFHPKSNSTCFQTITPFIHLPGTGGDKDYEFNQKNNGDVSKVLLPYVQEMCSLNNSSVVRQLLIPVATKGGPHHWNLCMLFIDENNIPSLYYIESENLLTSFDYYTYMYYMEDYKMHILPEVNALLAKFHYPAIDKVNFCQAKQFSQEGCGIAMGLNMQKILEEKYPQVICYSNTPRKGIPSRTEIRCLSSNVSIEEDALMRVELAFKIQARASIIAEGALDAEMVEKKSLVCSEILSDSRSLNVKAKEAFGFFQSAQPGISSEMHSVMAQDKGNDETSSSDINAEACRLW
>NZ_LT906452.1|WP_014842434.1|2771422_2772928_+|serine-hydrolase
MSYMKIEELLLKDTMRRAQIPGVSIAYINHQGVISTQEIGLTDGCGLVKMSSDPTQCPFQELVIGSNNKLGVGTKNTVIAFNKELYYVDQAEKNVRKIPLTEANKIAYETLHAKCTETYQLADSNEHELIATLTGRMPPTEVKPETVFGAASLSKPVFAYLVQKLIQTNAKNQSEAGFDQFILPEKLKHFDLDTPLFHMIPLEEFNIDGMKFDLSDESIVAHSKILTARTVLSHTTGLAHGEMKFQFLPNSEEKEHGYSNVGIIYLQQVIEKLTGSDLETLAQKHVFEPCGMIHSTYGLKACAANSLRTTACDYANFVKHLIHDSTIENPFVPHAYMTKDKGQAGAIGIAKGNIPDSILQHVAWGLGWGLQTNDEGRVITAYHSGDMNDYRAWVVIDLQDKDKKNAVVFFANSHNGHILAEQIIPKTMQMEQAANYFFSKWGFARNLAELGGKTTRLGIKSSSDSSPDTSIQDEPVEIKKETEKSDTSSIETYTSGWTFNA
>NZ_LT906452.1|WP_014842435.1|2772904_2773825_-|LysR-family-transcriptional-regulator
MAIPFKRINLNLILHLDALLSERSVSAAAEKVFVSQPAMSSSLKQLRELFKDPLLIPGKGEYYLSPKAKELQPQLEQVMFFIRNILQPNERFDPFQTKRSFKIALPDYVELILLPSLMAALEKLPHIVIETTIQSMADDPHLFIDENVDLAIGAINENSLSAQLKVEKLYEEEIICFASKNNPLINRPLSLEDYISNKHIAFSFNQERYSHSAEYLYKRKLVRNDMLFVKNILPAIFAVANSDAVISTAPSFLINMFARQFNLGMQPLPFNLEPTPIYLVTHSKSQYDEGVSWLAKLVSSSIKSPS
>NZ_LT906452.1|WP_014842436.1|2774008_2775523_-|cytochrome-P450
MFGELFASSIVLGVRYYSNQAYQAVVGILGQIERFGIGYTREFIRDPKSMIQSLTSKARSSEAGYSVVSLGYLGGNYAVITPKSQSQLTELLNQFDQEKSGRRGHASFKFFSGNDFFIISDTGHAALSSRKNLSRFLVPSRLVSPTITEVEKRVDCDADIQLRHTICGIVRAVMVENMLGIKQLPDNTYDVMESYRNDVKRWGAFPFPELLNFMPSLRQKRDVYRAFSKGILEQEFEKLVEVLHADPNPGNTNLIAASVVSLFKDENPTLSNEELLSALRSLSIEDIRKYFDNPIVQSLPMILKAADNLTDAIVLCLEQIASDPDKFVMLRDEMDRSHLVIEEGIDVRALKTLPVLDAFYKESVRFDAPVAVPRYTQNGYSSDSMTIPPNTMMIFDLHALAKGEQYWTNPEEFDPTRFLQQEKKQVTEEGGMNSNNKNHTVGQFPFIPFSVGLRNCPAFAVTESLFKVTIAKFVSDYQLQLVKKDEEDSTLHITSRDKSFGLMQ
>NZ_LT906452.1|WP_014842437.1|2775819_2776734_+|hypothetical-protein
MATTLIQKPSYTKNLTLNLDDYPGGVAIWGALPALFDTSNQGFDRGVHVHARLADSSKKVIDATYGHVTVISGYRIFTITEEAAVHFSMSAIFDIKITSLTCQHCSQLITSVGYAAVMPSRQHQCNHCGEITTTTSDCISNPIMLLKELIGDEQVKRPAVIPNRTIAIDPDKYSGGIQIWGSNPSIIWTAKRLEESAIHIHAYNENGKRIIDNTYGSVSLDGHKLDIEMIRVLQIQLALPNLALLLTTVYCPHCGVEQFDRGIWAVSAHNHRVCLLCKQTFISQDVISNPAFDVLTHVSGVISQ
>NZ_LT906452.1|WP_014842438.1|2776730_2777132_+|NUDIX-hydrolase
MSTLKTIFKIGALIFNEKNQLLAVHKKGKPPMELIVPGGVMEENESDEETLRREIKEELDSDIISFQFYKQFEDKAIYEEKWLVMRTYIVTLGNAPKPANEIDQLVWLGHDYHQRGYRFGSILGKQIIPDFFK
>NZ_LT906452.1|WP_014842439.1|2777215_2778370_-|hypothetical-protein
MKVLFDKTVQNNPGSGITPSSKSNEICTSSICMKSKLPADVVAKHLHGLQSTMVDRRNPDLSDSKSLMKSAKAHAILKTGTEIDMLTATGISEDDLPSSKGAIPMTAPEELTMKATWKNKNQERGISGRDASVFGGLGVLVISPDTKVMNIPKMNALAVPASFLAKYGAELIPLDQPFTLDTVDKSSLENLYLVEYQWDADYIQDYVMNIRGGGGLFVETHPFPHVFTPLSPACRGALILGVERKDGAFDFAAFEIPFGYTMKIASNVIHGDSFFVGPYAIALTETELADSVLLKQDTPQRDIQRVTQVPTKVFTIFLIEETKLASQINRKMMADKICHEGLSGKRLGFFKESSPKVSTEVRHCSDAEQDIHDQQFGLVPCLTK
>NZ_LT906452.1|WP_014842440.1|2778703_2779801_+|Dot/Icm-T4SS-effector-Lem23
MKRKDEQNNLTKGKVNEQNTVSTNTNLLFSKPPGINADTTNHMASSIDRLKDFDSSKQSLWLKYSEEIINEFCALLPEFPKKKPKVREDIRCPEEALLTQVGCAYAFLASKRREVAKLLKHGPLRHQFGLFNKPGFASIDDFNLSKDIPSQKDKIYEHLSLLISQPNPFIEVKKNHREAEGFSIYTITFKMKPDEIEQVHKKNLDSNKPFIENDTVLTITFNDYGKNDNRTSIVIDHRPTPFAENYTNESSYFKVQFELIEPYFQACQTWEASDGIDQFLENAGRIAYILARMQPVGRGNSAIVEWMIRGLAQTKNIELGPFNPDEKIGWDFKAFLTPEIQDYAHWFSEKAFAYSQLKNVTSLGH
>NZ_LT906452.1|WP_014842441.1|2779982_2780288_-|lpg2407-family-Dot/Icm-T4SS-effector
MYNVVSFNNEGVEHMKPTNEKSKEIRKKYKAPGASDEQLANSIKVASEFEYKNSSTFGWGGVYMVDRFQSMITGRAITNNTQRLLDAQALEEEASKANLKQ
>NZ_LT906452.1|WP_014842442.1|2780510_2781170_+|hypothetical-protein
MLTKNLNEALSAIKYVKSKLVYGSNTEENSKKPNWEPGRIILLRKEVHALAVVYARSHNGKAGFDIISKLTHAALLKYGFGNCGEQAQTAFCYLQSRGVAPLDYCQTSIGEHCLIVIGRVSGSDPNDISTWGEDAVICDPWAEKAYPLSEFRAMQSPDNDIRYPEICYANGKSPKPYLAGELISHHRIEPASKASSLSFFKKENYEHSQLNSATPMLIA
>NZ_LT906452.1|WP_014842443.1|2781495_2782314_+|Dot/Icm-type-IV-secretion-system-effector-Ceg29
MTNSNHLRNPVTKSLNDLCQDELSVIGSYLGAWNDLWSLTFTSSEMKKCLIHQQTDELWKFFFKEFFPYIPLPTEDFYKNFMKNYKTWYQTLYRVKQDPFFLMYLDKLKEDPAHLFRNDKEIIIAAIEKQPFLYKNFSRGYKEDEEVILCALKNNRFIIHDVPRTVREGFKEIADIKEDKARVDACDQLIEKLSPQRVSKIKSLDLFKSQLTLQAQNITKKSGEQVNNRQLQRSTAPITPEGITSLVHLGLFRDTQIQYEEKEESLHNKYRK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

979744 : 986583

Acinetobacter_phage(42.86%)

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_011945950.1\|979744_980521_-	indole-3-glycerol phosphate synthase TrpC	A0A0P0IR83	Acinetobacter_phage	1.9e-57	48.2
WP_027220911.1\|980513_981548_-	anthranilate phosphoribosyltransferase	A0A0N7IRD9	Acinetobacter_phage	4.6e-75	47.6
WP_027220912.1\|981525_982104_-	aminodeoxychorismate/anthranilate synthase component II	A0A0P0IKJ1	Acinetobacter_phage	7.8e-56	53.2
WP_010946572.1\|982137_982863_-	LPS export ABC transporter ATP-binding protein	G9BWD6	Planktothrix_phage	3.1e-17	28.3
WP_027220913.1\|982859_983369_-	lipopolysaccharide transport periplasmic protein LptA	NA	NA	NA	NA
WP_011215025.1\|983349_983919_-	LPS export ABC transporter periplasmic protein LptC	NA	NA	NA	NA
WP_027220914.1\|983915_984443_-	3-deoxy-manno-octulosonate-8-phosphatase KdsC	A0A140XBD6	Dickeya_phage	5.3e-27	47.0
WP_010946576.1\|984456_985419_-	KpsF/GutQ family sugar-phosphate isomerase	A0A2P0VNK5	Tetraselmis_virus	4.2e-38	34.1
WP_011215026.1\|985785_986583_+	ABC transporter ATP-binding protein	G9BWD6	Planktothrix_phage	1.7e-21	33.8

DBSCAN-SWA_2

1264956 : 1270893

Staphylococcus_phage(50.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_027220755.1\|1264956_1266030_+	bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD	A0A2H4PQS8	Staphylococcus_phage	2.1e-30	28.6
WP_027220754.1\|1266014_1266629_+	riboflavin synthase	A0A2I2L4R9	Orpheovirus	6.0e-22	38.4
WP_027220753.1\|1266625_1267834_+	bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II	A0A2H4PQS2	Staphylococcus_phage	3.5e-98	48.5
WP_050598095.1\|1267841_1268309_+	6,7-dimethyl-8-ribityllumazine synthase	A0A2H4PQS3	Staphylococcus_phage	9.2e-23	49.1
WP_010946915.1\|1268434_1270072_+	CTP synthase	A0A1J0FA14	Only_Syngen_Nebraska_virus	3.6e-154	52.3
WP_010946916.1\|1270068_1270893_+	3-deoxy-8-phosphooctulonate synthase	E3T537	Cafeteria_roenbergensis_virus	1.8e-53	43.9

DBSCAN-SWA_3

2185038 : 2195162

Bacillus_phage(16.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_011214266.1\|2185038_2186727_-	S8 family serine peptidase	A0A1B0T6A2	Bacillus_phage	8.0e-16	30.4
WP_011214267.1\|2186858_2187866_-	AraC family transcriptional regulator	NA	NA	NA	NA
WP_014844301.1\|2187989_2189315_-	adenosylhomocysteinase	S4VPF6	Pandoravirus	1.1e-47	31.2
WP_011214269.1\|2189334_2190483_-	methionine adenosyltransferase	A0A2H4PQS6	Staphylococcus_phage	7.6e-127	58.5
WP_027220141.1\|2190691_2191804_-	glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit	R4TGJ8	Halovirus	2.3e-51	35.4
WP_010947740.1\|2191899_2193039_-	molecular chaperone DnaJ	A0A1V0SBY2	Catovirus	1.6e-23	26.9
WP_011946925.1\|2193227_2195162_-	molecular chaperone DnaK	G8DDB7	Micromonas_pusilla_virus	1.3e-147	49.6

Anti-CRISPR protein detection

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