CRISPRimmunity

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_CP025257	Mesoplasma syrphidae strain YJS isolate ATCC 51578 chromosome, complete genome	1 crisprs	DEDDh	0	1	0	0

1. NZ_CP025257

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP025257_1

• CRISPR_ID: NZ_CP025257_1
• CRISPR_location: 316116-316353
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 2 spacers

Consensus repeat of NZ_CP025257_1

Consensus_repeat	Method
AAAGGTGACAAAGGTGAAAAAGGTGACAAGGGTGACAAAGGAGTAGCTGGAAAAGATG	PILER-CR

spacers of NZ_CP025257_1

>1.1|316174|29|NZ_CP025257|PILER-CR
AAGATGGAACTAATGGTAAAGATGGAGCC
>1.2|316261|41|NZ_CP025257|PILER-CR
GAACTAATGGTAAAGATGGTAAAGACGGAGCCAAAGGTGAA

CRISPR arrays and Neighbor proteins around NZ_CP025257_1

CRISPR arrays

The CRISPR arrays of NZ_CP025257_1

>merge|NZ_CP025257|1|316116-316353|PILER-CR
AAAGGTGACAAGGGTGAAAAAGGTGACAAGGGTGATCAAGGAGTAGCTGGAAAAGATGGAACTAATGGTAAAGATGGAGCCAAAGGTGACAAAGGTGAAAAAGGTGACAAAGGTGACAAAGGAGTAGCTGGAAAAGATGGAACTAATGGTAAAGATGGTAAAGACGGAGCCAAAGGTGAAAAAGGTGACAAAGGCGAAAAAGGTGACAAGGGTGACAAAGGAGTTGCTGGAAAAGATG

>NZ_CP025257|1|1|316116-316353|PILER-CR
AAAGGTGACAAGGGTGAAAAAGGTGACAAGGGTGATCAAGGAGTAGCTGGAAAAGATG	GAACTAATGGTAAAGATGGAGCCAAAGGT
GACAAAGGTGAAAAAGGTGACAAAGGTGACAAAGGAGTAGCTGGAAAAGATGGAACTA	ATGGTAAAGATGGTAAAGACGGAGCCAAAGGTGAAAAAGGT
GACAAAGGCGAAAAAGGTGACAAGGGTGACAAAGGAGTTGCTGGAAAAGATG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP025257.1|WP_101305120.1|305763_306780_+|restriction-endonuclease-subunit-S	unknown	unknown	gnl|CDD|341175
NZ_CP025257.1|WP_027048636.1|311518_313684_+|glycosyl-hydrolase-53-family-protein	unknown	unknown	gnl|CDD|311610
NZ_CP025257.1|WP_036256623.1|317098_317935_-|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|187632
NZ_CP025257.1|WP_027048616.1|318975_320085_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP025257.1|WP_027048638.1|314551_315076_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP025257.1|WP_036256628.1|324370_324952_+|lipoprotein	unknown	unknown	gnl|CDD|275340
NZ_CP025257.1|WP_027048631.1|302149_303136_+|aldo/keto-reductase	unknown	unknown	gnl|CDD|381304
NZ_CP025257.1|WP_027048617.1|320328_321744_+|NADP-dependent-glyceraldehyde-3-phosphate-dehydrogenase	unknown	unknown	gnl|CDD|143401
NZ_CP025257.1|WP_101305122.1|321895_324250_+|lipoprotein	unknown	unknown	gnl|CDD|224117
NZ_CP025257.1|WP_027048188.1|330691_330919_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP025257.1|WP_051591905.1|318376_318799_+|MerR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|133384
NZ_CP025257.1|WP_027048635.1|308321_311384_-|HsdR-family-type-I-site-specific-deoxyribonuclease	unknown	unknown	gnl|CDD|273028
NZ_CP025257.1|WP_027048187.1|331448_335840_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP025257.1|WP_101305119.1|305025_305748_+|tyrosine-type-recombinase/integrase	unknown	unknown	gnl|CDD|274042
NZ_CP025257.1|WP_027048634.1|306802_308320_-|N-6-DNA-methylase	unknown	unknown	gnl|CDD|280533
NZ_CP025257.1|WP_101305118.1|303736_304945_-|restriction-endonuclease-subunit-S	unknown	unknown	gnl|CDD|341141
NZ_CP025257.1|WP_027048186.1|335957_336920_+|GMP-reductase	unknown	unknown	gnl|CDD|235479
NZ_CP025257.1|WP_051591909.1|303208_303583_-|MerR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|133384
NZ_CP025257.1|WP_084497562.1|337598_338858_+|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl|CDD|224054
NZ_CP025257.1|WP_027048637.1|313777_314542_+|RNA-methyltransferase	unknown	unknown	gnl|CDD|223640

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP025257.1|WP_101305120.1|305763_306780_+|restriction-endonuclease-subunit-S	gnl|CDD|341175	cd17286, RMtype1_S_Lla161ORF747P_TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit TRD-CR, similar to Lactococcus lactis subsp. lactis Dephy 1 S subunit (S.Lla161ORF747P) TRD1-CR1, and Lactococcus lactis IO-1 S subunit (S2.LlaIO1ORF1141P) TRD2-CR2. The recognition sequences of Lactococcus lactis subsp. lactis Dephy 1 S subunit (S.Lla161ORF747P) and Lactococcus lactis IO-1 S subunit (S2.LlaIO1ORF1141P) are undetermined. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It may also include TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases and type I DNA methyltransferases.	1.08347e-26
NZ_CP025257.1|WP_027048636.1|311518_313684_+|glycosyl-hydrolase-53-family-protein	gnl|CDD|311610	pfam07745, Glyco_hydro_53, Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.	9.44592e-64
NZ_CP025257.1|WP_036256623.1|317098_317935_-|SDR-family-oxidoreductase	gnl|CDD|187632	cd05374, 17beta-HSD-like_SDR_c, 17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	1.1889e-101
NZ_CP025257.1|WP_036256628.1|324370_324952_+|lipoprotein	gnl|CDD|275340	TIGR04547, putative_liporotein, MOLPALP family lipoprotein. Members of this family are surface lipoproteins, about 900 amino acids long on average, found only in the Mollicutes (Mycoplasma, Entomoplasma, Acholeplasma, Mesoplasma, Spiroplasma). Paralogs occur, such as MCAP_0360, MCAP_0361, and MCAP_0362 in Mycoplasma capricolum. This family shares significant N-terminal sequence similarity with STREFT (Secreted Thousand Residue Frequently Tandem), described by model TIGR04512; several members of the STREFT family have been misannotated as GnsA/GnsB family proteins. For proteins in this family, we suggest the name MOLPALP (Mollicutes Paralogous Lipoprotein) family lipoprotein [Cell envelope, Surface structures].	0.000683905
NZ_CP025257.1|WP_051591909.1|303208_303583_-|MerR-family-transcriptional-regulator	gnl|CDD|133384	cd01109, HTH_YyaN, Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB. Putative helix-turn-helix (HTH) MerR-like transcription regulators of Bacillus subtilis, YyaN and YraB, and related proteins; N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.	3.18067e-35
NZ_CP025257.1|WP_027048631.1|302149_303136_+|aldo/keto-reductase	gnl|CDD|381304	cd19078, AKR_AKR13C1_2, AKR13C family of aldo-keto reductase (AKR). The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.	3.85769e-177
NZ_CP025257.1|WP_027048617.1|320328_321744_+|NADP-dependent-glyceraldehyde-3-phosphate-dehydrogenase	gnl|CDD|143401	cd07082, ALDH_F11_NP-GAPDH, NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11. NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.	0
NZ_CP025257.1|WP_101305122.1|321895_324250_+|lipoprotein	gnl|CDD|224117	COG1196, Smc, Chromosome segregation ATPases [Cell division and chromosome partitioning].	4.24866e-17
NZ_CP025257.1|WP_051591905.1|318376_318799_+|MerR-family-transcriptional-regulator	gnl|CDD|133384	cd01109, HTH_YyaN, Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB. Putative helix-turn-helix (HTH) MerR-like transcription regulators of Bacillus subtilis, YyaN and YraB, and related proteins; N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.	1.10512e-38
NZ_CP025257.1|WP_027048635.1|308321_311384_-|HsdR-family-type-I-site-specific-deoxyribonuclease	gnl|CDD|273028	TIGR00348, R_protein, type I site-specific deoxyribonuclease, HsdR family. This gene is part of the type I restriction and modification system which is composed of three polypeptides R (restriction endonuclease), M (modification) and S (specificity). This group of enzymes recognize specific short DNA sequences and have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine. They also catalyse the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.(J. Mol. Biol. 271 (3), 342-348 (1997)). Members of this family are assumed to differ from each other in DNA site specificity. [DNA metabolism, Restriction/modification].	6.73772e-113
NZ_CP025257.1|WP_101305119.1|305025_305748_+|tyrosine-type-recombinase/integrase	gnl|CDD|274042	TIGR02224, Tyrosine_recombinase_XerC, tyrosine recombinase XerC. The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerC, one of two closely related chromosomal proteins along with XerD (TIGR02225). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and homologs of XerC on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerC, as some apparent XerC examples score in the gray zone between trusted (450) and noise (410) cutoffs, along with some XerD examples. XerC and XerD interact with cell division protein FtsK. [DNA metabolism, DNA replication, recombination, and repair].	1.79877e-16
NZ_CP025257.1|WP_027048634.1|306802_308320_-|N-6-DNA-methylase	gnl|CDD|280533	pfam02384, N6_Mtase, N-6 DNA Methylase. Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.	1.03405e-98
NZ_CP025257.1|WP_101305118.1|303736_304945_-|restriction-endonuclease-subunit-S	gnl|CDD|341141	cd17252, RMtype1_S_EcoKI-TRD1-CR1_like, Type I restriction-modification system specificity (S) subunit Target Recognition Domain-ConseRved domain (TRD-CR), similar to S.EcoKI TRD1-CR1, S.StySPI TRD1-CR1, S.Ara36733II TRD1-CR1, and S.Eco3722I TRD1-CR1. Escherichia coli str. K-12 substr. MG1655 S subunit (S.EcoKI) and Escherichia coli NCM3722 S subunit (S.Eco3722I) recognize 5'... AACNNNNNNGTGC ... 3', Salmonella enterica subsp. enterica serovar Potsdam S subunit (S.StySPI) recognizes 5'... AACNNNNNNGTRC ... 3', and Actinomyces radicidentis S subunit (S.Ara36733II) recognizes 5'... CATCNNNNNNCTC ... 3'. The restriction-modification (RM) system S subunit consists of two variable target recognition domains (TRD1 and 2) and two conserved regions (CR1 and CR2) which separate the TRDs. The TRDs each bind to different specific sequences in the DNA. For example, S.EcoKI-TRD1 and S.StySPI-TRD1 recognize AAC/GTT, S.EcoKI-TRD2 recognizes GCAC/GTGC, and S.StySPI-TRD2 recognizes GYAC/GTRC. RM systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one enzyme complex composed of one DNA specificity (S) subunit (this family), two modification (M) subunits and two restriction (R) subunits. This model contains both TRD1-CR1 and TRD2-CR2. It also includes TRD-CR-like sequence-recognition domains of various type II restriction enzymes and methyltransferases such as Treponema pedis T A4 putative Type IIG restriction enzyme/N6-adenine DNA methyltransferase RM.TpeTA4ORF2695P. It may also include type I DNA methyltransferases.	6.31234e-15
NZ_CP025257.1|WP_027048186.1|335957_336920_+|GMP-reductase	gnl|CDD|235479	PRK05458, PRK05458, guanosine 5'-monophosphate oxidoreductase; Provisional.	0
NZ_CP025257.1|WP_084497562.1|337598_338858_+|ABC-transporter-ATP-binding-protein	gnl|CDD|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	4.72832e-51
NZ_CP025257.1|WP_027048637.1|313777_314542_+|RNA-methyltransferase	gnl|CDD|223640	COG0566, SpoU, rRNA methylases [Translation, ribosomal structure and biogenesis].	4.72669e-58

Protein sequences

>NZ_CP025257.1|WP_027048638.1|314551_315076_+|hypothetical-protein
MNTFTLVFLLIMIACILASLVTFLISLYLRFVKITETSFSKQVIKRKKHAERRIGCEIASTILLIAAMFIFLPIFILFLDNVSLESFIGIVITCLTFAITSIIAVFLYFTKLINRDEKKYTFEAWKKLEIDNQWYKNFCDNSDDEIKVKYFSKKIKMNNRRIQEIIDYFEEFNK
>NZ_CP025257.1|WP_027048637.1|313777_314542_+|RNA-methyltransferase
MEKITSVANSKIKEILKLKDTKYRNQSQRFIVEGFHLVMEALNKGTVLTILGTGHGIESLTSNIKNADQIIEISDSIAHKLSDTVKTQAVFAVCEMPKPSIDFQNNILLLDKVQDPGNIGTLIRSGASFNFKTIITAPNSVSFYNDKVLRSTQGTFFDVNLINDDLISVIKLLKTNGYTIIGTELHSSYKKLADLECQKYSKVALLIGNEAQGISQTLLDYIDLNVVIEMRAGIESLNAGVAGSIIMYQLYNKK
>NZ_CP025257.1|WP_027048636.1|311518_313684_+|glycosyl-hydrolase-53-family-protein
MKNIKLKPLMISIFILLTSFLATFASSCTPSSLREDFPANGKIITNEKFIKGVDVSSYAEIIEQSTLDNGEVKSYSNLTDDEQKIYYNFAGEKENLFKILADNGANSIRLRVWNDPYENGQTYGGGHNDIDTNIWIANQAKKNGINDVLLNFHYSDFWADPSRQWLPKKWVDITNEKELENGIYQYTLDSLIKFEKETGIIPSKVQIGNEITNGSFWNWKRSNTQYKNYQYTSRLLKKGLEAVEDFALSKKAKISKSIHIDGSITLKRWKQLLHIYLIEGDLINLVDGIAITHHPDWNGNSKTLYDVMSLIKREYNLPSFVSETAAVSTFDETNLAGDITTSQHNPNSYYNIPDAATQMILINSMMEASSQALPDNETGIYWWEPAWILSNNSGWATRKGIIYSEPLDEQKQKDFKTGNSWWNSGIFTNQAKPLPVLKVIKNYERINQSKDNLNWHQITNKSIFKNFNKDPVLEFSKIAGFKNKLDINDWIDDHNLLIYDYSTEADIYKAFLKLNPRILEKHITYENIVWDQNKEAGKLKIKNAKTNTVYKPFELSIDFKILDYEENTYRITEPIEIGRNDTNWLSKIVEAVPNKKETIKQGETEIDSFIYESIRPEFYKNEYYSWAGKSNNALVFYDDKNGENRFLDTKILKNNNTKIFKNKKVDYSYLAKNSQAWQNVLSIGEYEISLVFTKRIEFENFGLENWKELGGFAIKAKVKVI
>NZ_CP025257.1|WP_027048635.1|308321_311384_-|HsdR-family-type-I-site-specific-deoxyribonuclease
MIINEKLFEDNVEEELQNLGWEKLTYKNFKRKDYSEVINFDILKNSIQRINNIDEQKADKVIYEIIKNVDSFEKLNFKGMQFLFDGIKIYDENEERNLTIKLISEDSNLNKFGYFRQFEITNGVDKKRIPDIVLFINGLPIAVLELKQPLGSEGLNEAFLQNESLKFFKPELWYFNIINFVSNRISTKYGSTTAGFRHFYGWNKWEISNKMNPIKMLFSQKNIIDIIFNFSFYSDDQSPIKYLAAPHQIRAVNKTIEHLKNIKDNRGGIIWHTQGSGKSVTMVFLTKAIIKQFGTSTILLVTDRRDLDQQLYKRFLNAETFLRNKSKNISSRNDLIQELNDKKHFGIYFSTVQKFAEQTGILTNRSDIFILVDEAHRTQNNINGERKLSREQEEFIIKFGYARYMREAFPNAKITGFTGTPLMGNEKDTRNIFGDYIDTYPMNQAVEDGATVPIYYEMWKPNITLDKKYLEEMDKIQSEYKNTLDPNDIASEQKMEALLKAVNKSIIFEDKKIIAAKADKMIEHLNKRKRILNGKAMIVANSRNSAYEYYLNITTKYPEYKDKTILVMTTDSNKDSKEMANAIVPKSDMNKVASEFRKSDSKYKIAIVVDMWLTGFDVPDLDVMYMDKIVKWHNLMQAIARVNRTFEDKKTNKTKESGLIVDYIGIWKYISDALIQYANGSDTKLDIEIEDIEKAKEKLNELFEIIDNNYIENILKFPNLNLKEQYQFVMGAYDKLLDVNKFNTDEKNKFIKLARKAKRFYKISYTNISERETLIAKCIETINSLITSSTIGNDSKLTWTIESVKEAIRKAVMTADTSIKIDESTMTKDINKVANILESEAEKLVKSRPRVAAQLYANSIQMQIDEIAKIKPYFAKLASEKLKELILELENSRDIEEFIEFLIKLSKEMKEEKDKPLEFDNIELQVFFDILSNDKFLQYNKSSETLRAIAQDLWEAIRENNTDQFLFNPMVQSNITTTLKKLLTTKYQYPPEGLYTLSENLIKEITNTIKTNKNAFRKDD
>NZ_CP025257.1|WP_027048634.1|306802_308320_-|N-6-DNA-methylase
MAKKIKDIESKLWEASNVLRGNTSAEEYMHTILGILTLKYISDRNKVALQKISDEGMKIEMFSPNELYYSYKTFIVHEESKWEYLMNFSNTEKIGEKLDEAFMKLELQNEILRGIFNKNFNREGLDQIKLGNVIKIFSDEDLSEEDNEDMIGRVYEYFLGKFFKDRGQKGGEFYTPTSIVKLMVNLIKPLKGTIYDPACGTGGILVQAKRYIQEHKGKIEDITVYGQEYNNVTWKLAKLNLVLNGFSLFDTDDNGVLGQTNADTFTNDQHKNKKFDFVMANPPFNMKNWGRDALEEDMRFKWGLPPSGNANYAWLSHMLSKLSNQGKMAIVLANGSLSSSQKEEKAIRENFVKENKVDAIIELPDKLFYTTGIPACIWVFNNKKVNKNILMVSGSNIEGNMISKKLRELTDENISIIQTLYDKHLAGEEINEQGLAKTIKFTNLVENDFSFVPGRYVESKEEKIDKEQTQKDIMQLSLELSDLLKEFDELKPKLHEAIKKTLESK
>NZ_CP025257.1|WP_101305120.1|305763_306780_+|restriction-endonuclease-subunit-S
MAIYKLGDISIIQNGSTPSTKNESLWKKEIPFLGPSDIEANRASRYVTKNKAKRPGTILISTTATIGNIGILEVESWFNQQITSIEANPNFVKDKFLFYYFLTQKNKIKKISDGGSVFSIIHVNTFRNWIIDLSSLEEQQKIIDIIEPIEKMKNKFMTLNKTVLELIKKIELSDEKIRIIDFFYEVREKPKNIKQISAKVLSENKGLILKAESPNTYKTNTFYCNEGTFIFCSIRTYLQKWGITPFDADVNGTLFQFEIKKNLTPLINYLKNESSWSTFNLLSKGTKMPVLSKKDFLNIEINKTKFEIKKIDLILKNINKIIIDMESLIEKSVSLLVK
>NZ_CP025257.1|WP_101305119.1|305025_305748_+|tyrosine-type-recombinase/integrase
MKKNEYLKFLKKNNYSANTISTYKSILSIYQNDFVNIARIKKHMLKYFSSPNTVWTHYNVICSYMKWSKDKRLGNFKEMKLPKIPKTYMKVFKKDFLIKKTNINDEDSELLKQKKIVIRFLFETGIRAAELNSILEINSKTIKVVGKGNKVREIFHRNDTTKQLKEFIYTTKTLRFWVKEILGENFTPHSIRRSYATHMLLGGANPKMVMMQLGHEKIETTFRYLNLSLEENWKIYSKFL
>NZ_CP025257.1|WP_101305118.1|303736_304945_-|restriction-endonuclease-subunit-S
MAIYKLNEICKTERGNGSFKKNDLSHDKNLEYLALHYGKTYKLEIIDNDFSFFVDKSFLKTNSLMSKNDVFLISTSETVKELGKVIFYNADKEGILGGEQIKIIPDNTKVLNRWLFYWLKMNQNIFAKFATGIKVYRFKRADFSHIDISLPSLEEQQKIIDIIEPIENLFLKYSNCIRIDTFKNCEDDVKKIIDIIEPIEIVIAKNKEILNSSIKLIAQIGQKLITKKAIGKKLNIYQQREEKIEKGIYSQTADIGNFSNKIKKQEYYSKLPSRARLKVQLNTLYICKLLGERKFLFSNSDKNLIISNGMWGIKSDSDFKFSNLSFFMSDYFYNKKKLFSTGTTMVGLNDQGLKKIISEVEIIHDLESETLLEKLFETLSISSKIDNELDKLINATIKMLVR
>NZ_CP025257.1|WP_051591909.1|303208_303583_-|MerR-family-transcriptional-regulator
MPKRYYIKEIANKFNIPEYLLRYYDEKGVITKFKRDENDYRYMFEDDLIFVKTVLCLKKTNMPLKEIIKYIELVDQGEITLESRQAMILKQEKVVLKKQHDLEEQIAFINYKKDFYEQAIKNKK
>NZ_CP025257.1|WP_027048631.1|302149_303136_+|aldo/keto-reductase
MKTRILGNKLQVNEIGLGCMGLSMSFPPFPTEDEAVAFLRKAYKQGVNFFDTAEIYGPFENEKLVGKAFKDIRSEVIIATKFGFKYEGNKAVGLDSSRENILRALEGSLKRLQTNYIDLFYQHRVDPQVPIEEVAQVMKELIAAGKIKYWGLSEASAATIRRAHKICPVTVVQSEYSMFWREPEQKIFPTLKELQIGFVPFSPLGKGFLTGHVKPGQIFGEGDFRNTIPRFNNPEYLAANMKLVEFVRELANAKQTTPAAIAIGWVLAQGEWIVPIPGTKKINRLIENISASQLVFSSSEIEMIDQKLSEIEIIGFRYSEQSESQIDK
>NZ_CP025257.1|WP_036256623.1|317098_317935_-|SDR-family-oxidoreductase
MKNKTWFITGASQGFGLGITKRLLEQGYQVAATTRNPEKLISQLGNHANLLVLKVDLSNQKEIDNAVEKAVEKFEGIDILLNNAGYGQLWTFEESSDAEIRECFEVNLFGTMNVTRAVLPVMRSQKSGHIFTTSSVWGYVGVPYNSTYAAVKFATDGWTESLAHELKPLGITVSSIKPGGFRTNFLSSTSLVFGSELIEDYKRERNQWFDSLKTWDKNQDGDPDKYCDFIIKITKLNEQLPVHIFAGRDAYQHAEEKINSIRNDMDKLKIPATDLHVK
>NZ_CP025257.1|WP_051591905.1|318376_318799_+|MerR-family-transcriptional-regulator
MDKVGIKELSKLFNVSEQTVRFYDSKGLFPFFYRESNNYRFTYEKDLQWFRMVFLLRKSGMEIKNIQRYINLCMEGDQTLIERLEIIQSQKISLQSKIDDLQDEMRVLTSKEQHYQMVIETGTVDDWNPVNFKELLQKTN
>NZ_CP025257.1|WP_027048616.1|318975_320085_+|hypothetical-protein
MIKLLVLISGTGVIAAPIAPMVSLNTIQKLDSTSASDTSFSLNPQVQLFTRETIAKSSRFVGSGVETSTSVKDEPTSINLNWLIGNKSVTVGTYDAIIIMDQETISQSAQSVLLTRVDIENNSEVKWVGSIKNKNEDGKLISAFDLNLKFYFAENGRAMLRTELTHTAVDAKDNYNASTKEHGINLFFKGKAINFFKEQNNNSVDQSFGETIIREWNIDASNSLVVVDKSLKSSSRVSGLSGTLLSIPKNIEKVTRVSYEGNLKSAVVANPVNWSIIYSSFNLFKNETASTATHMVFDSEFRSAYNTPESGEVSSLLKMQLIIDLDYSKNYTKFTPLAIIELDNSKTNPASNSWLETTYVFDKVKLWVN
>NZ_CP025257.1|WP_027048617.1|320328_321744_+|NADP-dependent-glyceraldehyde-3-phosphate-dehydrogenase
MYKFKAMINNKFIDTAAQLEIINPDGLEICGSVSALSKEQINHAFLAARQAQKKWEKISLDKRIEYLNGWKELLVANKNELATIIMSEVGKGYKDALVEVERTVEYMTETFAQATKLEPLKLDGSKYGAPNKQATFSRVAKGVGVAISPFNYPINLAISKIAPALVMGNTLVFKPATQGSLIGARLGELAVEAGIPEGIFNVVTGRGRDIGDVIVTNSEIDFISFTGSVGIGKHLLEIASSKDIVLELGGKDPAIVIDADNLEKYANEIVSGAFSYSGQRCTAIKRVLTTNEIADKLVPLLVSKINTLSVGKPIDNADITPLIDLKSADFVWDLINDAKAKGATALTGDSRIANLITPTLVDNVTTEMRLAWEEPFGPVLPILRLNSIEEMIKVANASNFGLQASIYGTNLEQALEIAYQIEAGTVNINGKSQRGPDQFPFLGIKDSGFGTQGIGETILSVTRYKGIVINH
>NZ_CP025257.1|WP_101305122.1|321895_324250_+|lipoprotein
MKKLMTMLATISLVATTTTTVISCRTKSDDAIIDLKKQLEDLKKQKEDLIEDHDKELKERQKDLNKLNQKITLRDKEISELNTLIFNKEKQIVDFKRKVNEMTEAIEDKEKTLNEKQQEYENLSQKYQKKNEELKNLNQDFETKEKEVSFHKQNIEKLQKQIESQNIAIQQKQKNINILIRQNNLNESRIGKLSNLLEEAKLKKHNLETEITSLNGKLYKNANEIANLEIRVQNLETEKQKLAKLLADAQQKISNFEKESQNKVWSEIDDLILSHNALIQFKQKVLEFETELKNKNVSLQEKNDQLENKRIENENLQNTITRLEQENLKIEKQSIEIKNELKKVNQIVAEKIAEIANLKSENEQLSKSKSEIESALRESRNQNSQLSKLKCQLDEQLKQINKTLQAKNTENAMLQKDKQALEKEIENLNIQLAKAINSKRTMQQEIDTLRQEKQSFESHYNLLKQEYEQISKSFRFKQVFKKELEPAFWSLLDTEQSDLKIRQNADDYNQKQNKYTDKNFYVINNNYHLKKQDYFYNGIREFLLEFMTNYDIERDQKYWKKLTKTESNIKKYEKFRTSDNVYLTGLANPDNLKLVQNQMQLWLNDLKTNSNYHQKYFGRAKYWINLLNPVVKVYHLTKEHSNVRNLVSYRLKDGREYTHSKSTRFEISLQPQIKSTDSPEDKLIKKIVYGNKKFFDLARIDFTNDWYENGMYAFNEEGPTRLSFDPKDYNRGLYEEGYYSNGYSIRIRKFEKKLDEQTKNDRLSLLGQKSQKYAKWFFSIKFNE
>NZ_CP025257.1|WP_036256628.1|324370_324952_+|lipoprotein
MKKLLTLLGAVGLTATASSAVVACGNKDKSVDTKEFEAAAKIEANAKYATIKEAAAAIEKLAKPKGVSKITVTGNEETKKITIKFTVEKGYKAINDMVLDFKAAGEEKTPVIKGAEAKSVEVGKEVTLNITIDNAIEGEKLTVKSSDATIATVAVNDTNVVTVKGLKAGKATITLSYKGAADVTFEATVTTAE
>NZ_CP025257.1|WP_027048188.1|330691_330919_+|hypothetical-protein
MHLEDRTQYEDIWISGQYQNLVLFYDVVATNSNVKHFSVEIKITKYQLTKSTLRVSSKGNTILRNAHYLQGRQTH
>NZ_CP025257.1|WP_027048187.1|331448_335840_+|hypothetical-protein
MKVLLGLLSALTVGEQATTMLMSTNLSHSTKTNEQDIIKDYEIVDRAVVYLGAKVEQSFFDKKSGATFWRGLFRKEKRNRLAYTKMKADYSGFETYKAIDSTTNENGWDGPGNRAKKAMGIDLKDQTIFYAANDEVFYFSEKGITKFEWNIQKSNENQSDGLVEGIAGGVNGLLAGFGGLLTPAKPTPIDSTGEEIILLKPEQETVKNAVFSEVNNAIYYTTVSSIENIWRINRLDYETLKSTVIDSGPMIGENNYPALATSNDSDTGFVYSVLSGNISLINGENIQVIHQYSDSNQAIKVIAEKDGMWIVNASKKNGVVNLENTISYFVDIVSKETKKVAETGTWIEDVVWINDLTKYTIFNNQVRIKSTNNASSEYLYKQTPLPSTNEFSVKTVEGYSGIFDYAVSFQTDEMFRRKGGILGGGKWDGMYVNRTISDKFQEALRFTNLGNQEGQLEYSLGEKDEVYVWADPEKHAIKITGNSYISKVTLLDEDSEEEIDVVLEYNDNDKFWSVPIVKPGSAKGTDILIQFYDEENPEFKKEARLKLRDRQNVQIDLSLPENSIENNLKVSNETKEPEIFAAIREKFGLNLTNNDINIFFEKATYSTPGKIKIEAKPESHLVIKSQEIKIPTLVLDIETFRFENLTSLTDEGEIRNAVTKQLKAATDMNLDVGSNYDLDYEPATQTENGYIDIKAKMNSTLFINSQRIVLSASGAIDLATLLVHENIQLSNDITNEKILEMINKAIKKEFPNSDEISLSDLIIEKSEAKIGVKGSLYIAADPDTALIKNSVTLDIPWLKFDLDKLSVQFDSNEANQENFLNQINAIQGLKKVANKDFDFTINKATIQSEGKIVLTANKNSEYLVGKKVISIQKIYDLSTANLFDDLKVFKETNVDDIVEYLANKKGWEKVSELDLEVAISRDSSSTEEGMMLIKASSNSTRIQNQKEVAILRDRQDLNEIILEKDNFIGNITPNDVENKTEEQVFEFINKLLIKKYPNIKLDEIWLKGYDENEIEIAAKPDSEVYKNSATVTYTYKRDLEVEIPEEKRSLGIKDITPTVAAVREHFADLNFNWEQIEIDMNTKEKEKIIILKAKKDANFYKGSVEIKYAIPEDLQEVIKEKKLGKISNYKESNIKAKLQELNPNLDIEAVKIENIRNENANSSYQIVNKHYIATIESANEEIYKNSVEITFNVDEGEAEDLSTVIKNKTISVPYGKTTEIDTIKKAIKTQNPYPTIDWDLIELKFNDKNQVILHSKNVNYYYGEVVITVKELGKNLAEIITKSKIIVEHGKTQDKQIIKQIIDNKNGHINWDAAEIEFKDGKVYLVSVNQEVYVGEIEIIVGELGPELSSVIKKQEIGISFANRGNQESIKQAIIEANKELGIKWAQIKFTFNSDGTVTLSTLDQDVYMGEIVLSIFEINEEKETYTVLIISVIGVVSFATFIALLLLLLKRKDKKEEQDSQK
>NZ_CP025257.1|WP_027048186.1|335957_336920_+|GMP-reductase
MYAFDYEDIQLIPNKCIVTSRSQCDTSVELGKYKFAMPVVPANMASVINEEICVELAKQNYFYVMHRFNVDAVKFVKMMHQKNLIASISLGVQPADYQIVADLVAIEEIPEFITIDIAHGHSESVKQLIEYIRKMMGDRTFIIAGNVATPQAVRDLEYWGADATKVGVGPGKVCITKLKTGFGTGGWQLGAIKWCSKAATKPIIADGGLRVNGDIAKSIRFGATICMIGSLFAAHEESPGKNVTVDGIMFKEYYGSASEYNKGEKRYVEGKKELIKVRGKLTETYKEMHEDLQSSISYAGGSKLKAIKKVDYVILKTSNF
>NZ_CP025257.1|WP_084497562.1|337598_338858_+|ABC-transporter-ATP-binding-protein
MRNKNLDKSSLLFQKNSVVAVDFHKKFKDIDIGPFSFNIEKGKVTALLGSSGSGKSVFLNSLLGATLNYNGDIYINGKERKSSSSIENNANVGFYSQMDFSLYSISAYDFLKNMCNVMGLDMRIADSKIEYWLKKFDLWSAKDKSLNAFSWGMKNRMNLILCFIKEPEILILDEPGANLDSKWRNYVYEILKEFKEESECTIILTVHNIDEVYDIIENFVVLEKGKLVFSGTKEELNLYKKLKLSFENDISIENVEKHLNEHNILTFETNKKTSSIIVGLKKEQTFNDVQAVLNKYSTKAENIIAQTINISEIQKALKDKTLPHIPKYQPITYAENFKDNDKQIFIYEEFDEILNEPDKTYFYSLDKKTDSRETKIRKTSFELGVEINKDMNNEISKSANVDCDILKRINDIKKRLKIV

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	MH616963	CrAssphage sp. isolate ctbg_1, complete genome	22506-22534	5	0.828
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	MK779875	Lactococcus phage CHPC971, complete genome	23998-24026	5	0.828
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	MH622943	Myoviridae sp. isolate ctbc_4, complete genome	28559-28587	5	0.828
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	MT774403	CrAssphage cr113_1, complete genome	77316-77344	7	0.759
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	AP013699	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C58A-MedDCM-OCT-S31-C30, *** SEQUENCING IN PROGRESS ***	31191-31219	7	0.759
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	AP013700	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C58A-MedDCM-OCT-S42-C58, *** SEQUENCING IN PROGRESS ***	27108-27136	7	0.759
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	KT001915	Citrobacter phage Merlin, complete genome	91390-91418	7	0.759
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	AP013429	Uncultured Mediterranean phage uvMED DNA, complete genome, group G16, isolate: uvMED-CGR-C58A-MedDCM-OCT-S43-C47	32367-32395	7	0.759
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	NZ_CP026233	Citrobacter freundii complex sp. CFNIH4 plasmid pCFR-0b27, complete sequence	193637-193665	7	0.759
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	AP013842	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C15D-MedDCM-OCT-S41-C130, *** SEQUENCING IN PROGRESS ***	348-376	8	0.724
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	AP014462	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C15D-MedDCM-OCT-S43-C38, *** SEQUENCING IN PROGRESS ***, 6 ordered pieces	7794-7822	8	0.724
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	AP013833	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C15D-MedDCM-OCT-S27-C178, *** SEQUENCING IN PROGRESS ***	6095-6123	8	0.724
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	MH327491	Marine virus AG-345-A17 Ga0172217_12 genomic sequence	8162-8190	8	0.724
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	AP013561	Uncultured Mediterranean phage uvMED isolate uvMED-CGR-C15D-MedDCM-OCT-S44-C14, *** SEQUENCING IN PROGRESS ***, 10 ordered pieces	35290-35318	8	0.724
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	AP013843	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C15D-MedDCM-OCT-S42-C21, *** SEQUENCING IN PROGRESS ***	31087-31115	8	0.724
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	MN693550	Marine virus AFVG_25M93, complete genome	29021-29049	9	0.69
NZ_CP025257_1	1.1|316174|29|NZ_CP025257|PILER-CR	316174-316202	29	MN693245	Marine virus AFVG_25M69, complete genome	28840-28868	9	0.69

1. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to MH616963 (CrAssphage sp. isolate ctbg_1, complete genome) position: , mismatch: 5, identity: 0.828

aagatggaactaatggtaaagatggagcc	CRISPR spacer
gagatggaactgatggtaaagatggtgaa	Protospacer
.**********.************* *  

2. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to MK779875 (Lactococcus phage CHPC971, complete genome) position: , mismatch: 5, identity: 0.828

aagatggaactaatggtaaagatggagcc	CRISPR spacer
aagatggaacaaatggtaaggatggaata	Protospacer
********** ********.******.. 

3. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to MH622943 (Myoviridae sp. isolate ctbc_4, complete genome) position: , mismatch: 5, identity: 0.828

aagatggaactaatggtaaagatggagcc	CRISPR spacer
aagatggtacaaatggtaaagatggtgta	Protospacer
******* ** ************** *. 

4. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to MT774403 (CrAssphage cr113_1, complete genome) position: , mismatch: 7, identity: 0.759

aagatggaactaatggtaaagatggagcc	CRISPR spacer
agtggggagctaatggtaaagatggagat	Protospacer
*. . ***.****************** .

5. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to AP013699 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C58A-MedDCM-OCT-S31-C30, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 7, identity: 0.759

aagatggaactaatggtaaagatggagcc	CRISPR spacer
caaatggaactaatggtacagatgttgga	Protospacer
 *.*************** *****  *  

6. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to AP013700 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C58A-MedDCM-OCT-S42-C58, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 7, identity: 0.759

aagatggaactaatggtaaagatggagcc	CRISPR spacer
caaatggaactaatggtacagatgttgga	Protospacer
 *.*************** *****  *  

7. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to KT001915 (Citrobacter phage Merlin, complete genome) position: , mismatch: 7, identity: 0.759

aagatggaactaatggtaaagatggagcc	CRISPR spacer
cagatggaactaatggtaatgaattagtt	Protospacer
 ****************** **   **..

8. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to AP013429 (Uncultured Mediterranean phage uvMED DNA, complete genome, group G16, isolate: uvMED-CGR-C58A-MedDCM-OCT-S43-C47) position: , mismatch: 7, identity: 0.759

aagatggaactaatggtaaagatggagcc	CRISPR spacer
caaatggaactaatggtacagatgttgga	Protospacer
 *.*************** *****  *  

9. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to NZ_CP026233 (Citrobacter freundii complex sp. CFNIH4 plasmid pCFR-0b27, complete sequence) position: , mismatch: 7, identity: 0.759

aagatggaactaatggtaaagatggagcc	CRISPR spacer
aggatggaactattggtaaagttggttat	Protospacer
*.********** ******** ***   .

10. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to AP013842 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C15D-MedDCM-OCT-S41-C130, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 8, identity: 0.724

aagatggaactaatggtaaagatggagcc	CRISPR spacer
ttacaggaactactggtaaagatggaaac	Protospacer
  .  ******* *************. *

11. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to AP014462 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C15D-MedDCM-OCT-S43-C38, *** SEQUENCING IN PROGRESS ***, 6 ordered pieces) position: , mismatch: 8, identity: 0.724

aagatggaactaatggtaaagatggagcc	CRISPR spacer
ttacaggaactactggtaaagatggaaac	Protospacer
  .  ******* *************. *

12. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to AP013833 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C15D-MedDCM-OCT-S27-C178, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 8, identity: 0.724

aagatggaactaatggtaaagatggagcc	CRISPR spacer
ttacaggaactactggtaaagatggaaac	Protospacer
  .  ******* *************. *

13. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to MH327491 (Marine virus AG-345-A17 Ga0172217_12 genomic sequence) position: , mismatch: 8, identity: 0.724

aagatggaactaatggtaaagatggagcc	CRISPR spacer
ttacaggaactactggtaaagatggaaac	Protospacer
  .  ******* *************. *

14. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to AP013561 (Uncultured Mediterranean phage uvMED isolate uvMED-CGR-C15D-MedDCM-OCT-S44-C14, *** SEQUENCING IN PROGRESS ***, 10 ordered pieces) position: , mismatch: 8, identity: 0.724

aagatggaactaatggtaaagatggagcc	CRISPR spacer
ttacaggaactactggtaaagatggaaac	Protospacer
  .  ******* *************. *

15. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to AP013843 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C15D-MedDCM-OCT-S42-C21, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 8, identity: 0.724

aagatggaactaatggtaaagatggagcc	CRISPR spacer
ttacaggaactactggtaaagatggaaac	Protospacer
  .  ******* *************. *

16. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to MN693550 (Marine virus AFVG_25M93, complete genome) position: , mismatch: 9, identity: 0.69

aagatggaactaatggtaaagatggagcc	CRISPR spacer
ttacaggaactactggtaaagatggaaat	Protospacer
  .  ******* *************. .

17. spacer 1.1|316174|29|NZ_CP025257|PILER-CR matches to MN693245 (Marine virus AFVG_25M69, complete genome) position: , mismatch: 9, identity: 0.69

aagatggaactaatggtaaagatggagcc	CRISPR spacer
ttacaggaactactggtaaagatggaaat	Protospacer
  .  ******* *************. .