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Database: UniProt
Entry: A0A0Q0GG30_9GAMM
LinkDB: A0A0Q0GG30_9GAMM
Original site: A0A0Q0GG30_9GAMM 
ID   A0A0Q0GG30_9GAMM        Unreviewed;       279 AA.
AC   A0A0Q0GG30;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=DNA ligase {ECO:0000313|EMBL:KPZ70870.1};
DE            EC=6.5.1.1 {ECO:0000313|EMBL:KPZ70870.1};
GN   Name=ligA_1 {ECO:0000313|EMBL:KPZ70870.1};
GN   ORFNames=AN944_01968 {ECO:0000313|EMBL:KPZ70870.1};
OS   Shewanella sp. P1-14-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ70870.1, ECO:0000313|Proteomes:UP000050414};
RN   [1] {ECO:0000313|EMBL:KPZ70870.1, ECO:0000313|Proteomes:UP000050414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ70870.1,
RC   ECO:0000313|Proteomes:UP000050414};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPZ70870.1}.
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DR   EMBL; LKTL01000011; KPZ70870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q0GG30; -.
DR   PATRIC; fig|1723761.3.peg.2014; -.
DR   Proteomes; UP000050414; Unassembled WGS sequence.
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.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:KPZ70870.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050414};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..279
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006179736"
FT   DOMAIN          75..197
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          211..276
FT                   /note="DNA ligase OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF14743"
SQ   SEQUENCE   279 AA;  31660 MW;  5F1A3F9F9FDC1D38 CRC64;
     MFRFILSVLI VFMALLISDA VDANNKPALQ LAMRYQTDTD VTQYLISEKL DGVRGYWDGN
     QMLSRSGRVM ILPDWFTADF PKTALDGELW IKQGEFDAVS ALARSSHSHH AEWKLVKYMI
     FDLPEHGGMF VERVKAMQQI ALESRYIEAI EQQELVSTAQ LMAQLDYVIE NNGEGLMLHL
     KSGYYQIGRS QNIVKLKPKY DAEARVIGFN EGKGKFEGLM GSLKVEMPNG KQFNLGSGFS
     NELRRNPPPL GAIITYQYLG LTKNGIPRFA HFLRVRESQ
//
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