ID   B4X1K0_9GAMM            Unreviewed;       283 AA.
AC   B4X1K0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=ATP-dependent DNA ligase domain protein {ECO:0000313|EMBL:EDX88628.1};
DE            EC=6.5.1.1 {ECO:0000313|EMBL:EDX88628.1};
GN   ORFNames=ADG881_730 {ECO:0000313|EMBL:EDX88628.1};
OS   Alcanivorax sp. DG881.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=236097 {ECO:0000313|EMBL:EDX88628.1, ECO:0000313|Proteomes:UP000003954};
RN   [1] {ECO:0000313|EMBL:EDX88628.1, ECO:0000313|Proteomes:UP000003954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG881 {ECO:0000313|EMBL:EDX88628.1,
RC   ECO:0000313|Proteomes:UP000003954};
RA   Bolch C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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};
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DR   EMBL; DS989915; EDX88628.1; -; Genomic_DNA.
DR   RefSeq; WP_007149036.1; NZ_DS989915.1.
DR   AlphaFoldDB; B4X1K0; -.
DR   STRING; 236097.ADG881_730; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_021047_0_0_6; -.
DR   Proteomes; UP000003954; 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; 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:EDX88628.1}.
FT   DOMAIN          126..228
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   283 AA;  31215 MW;  5FFF3E1C521CD298 CRC64;
     MKSRQGLAII GLWIMAGWCL AQGPALQLAQ SYKKGMALQG YWVSEKLDGV RAYWNGEQLI
     SKGGHVIKAP AWFVRGYPDT PMDGELWMGH GRFAEVSAAV RRLQPDAKEW RQIRYKVFDL
     PASGAPFSQR IQQMKALASA SNAYTFSVIE QQPASSHAAL LQRLDKVMAA GGEGLMLHHG
     DSLYQAGRSD AILKVKTYQD AEAVVVGHTE GKGKYRGMLG ALVVQRDDGR QFRLGTGFTD
     KQRKTPPPLG ATVTYKYFGK TATGLPRFAS FLRIRNDEPL AEP
//