ID U4JXX2_9VIBR Unreviewed; 280 AA.
AC U4JXX2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative ATP-dependent DNA ligase {ECO:0000313|EMBL:CCO57765.1};
GN ORFNames=VIBNI_A1655 {ECO:0000313|EMBL:CCO57765.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO57765.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO57765.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR EMBL; FO203526; CCO57765.1; -; Genomic_DNA.
DR RefSeq; WP_022550665.1; NC_022528.1.
DR AlphaFoldDB; U4JXX2; -.
DR STRING; 28173.VIBNI_A1655; -.
DR KEGG; vni:VIBNI_A1655; -.
DR PATRIC; fig|1260221.3.peg.1577; -.
DR eggNOG; COG1793; Bacteria.
DR OrthoDB; 9782700at2; -.
DR Proteomes; UP000016895; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR CDD; cd08041; OBF_kDNA_ligase_like; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR029319; DNA_ligase_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF14743; DNA_ligase_OB_2; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000313|EMBL:CCO57765.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..280
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004649957"
FT DOMAIN 132..231
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 280 AA; 32226 MW; BD2F9F661A84FF96 CRC64;
MKKRILACVI IAALSGTSAI AERPTEHSLL LANEYKSEVN LDEYWVSEKL DGIRVVWDGE
TLYSRKGTKI HAPVWFIENL PPVMMEGELW AGRGKFHVVQ QTVMDKTPSD RAWQDIQFMV
FDLPHSAGDY AKRYYDIQNW VQVINQHHVR YIEHHPAGNH SQLMHMLDTI DGNYGEGVML
RKVNQRYRPG RSDDLLKLKK YQDAEATIIG YKPGEGKYHG MLGSYFVRCA DGKEFYIGSG
LKDSMRKDPL PVGARITYRF NGKTSTGKPR FARFVRERIE
//
