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Database: UniProt
Entry: A0A148KLE4_9ALTE
LinkDB: A0A148KLE4_9ALTE
Original site: A0A148KLE4_9ALTE 
ID   A0A148KLE4_9ALTE        Unreviewed;       296 AA.
AC   A0A148KLE4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=ATP-dependent DNA ligase {ECO:0000313|EMBL:KXI27143.1};
GN   ORFNames=AX660_01790 {ECO:0000313|EMBL:KXI27143.1};
OS   Paraglaciecola hydrolytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI27143.1, ECO:0000313|Proteomes:UP000070299};
RN   [1] {ECO:0000313|EMBL:KXI27143.1, ECO:0000313|Proteomes:UP000070299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S66 {ECO:0000313|EMBL:KXI27143.1,
RC   ECO:0000313|Proteomes:UP000070299};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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:KXI27143.1}.
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DR   EMBL; LSNE01000015; KXI27143.1; -; Genomic_DNA.
DR   RefSeq; WP_068381541.1; NZ_LSNE01000015.1.
DR   AlphaFoldDB; A0A148KLE4; -.
DR   STRING; 1799789.AX660_01790; -.
DR   OrthoDB; 9782700at2; -.
DR   Proteomes; UP000070299; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:KXI27143.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070299};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..296
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007550114"
FT   DOMAIN          55..209
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          224..287
FT                   /note="DNA ligase OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF14743"
SQ   SEQUENCE   296 AA;  33362 MW;  7FC2F1AC887DAEF1 CRC64;
     MLLPIRPFYL LIFLCSCSVF MLCAANDPNS IQASKTVKPQ QLSSLYHDDI VVAEYWISEK
     LDGIRARWTG AELITRNGNV IKAPTWFIKE LPPQVLDGEL WLARNSFEQT ASIVLRDNPN
     QEWQNIKFML FDLPEHKGTF SERLAELQLL VDTTASPYLQ LIPQFKLATH TQLLTKLDGA
     TAQGAEGLML HHQDAYYQDG RSADLLKLKK YQDGEARVIA HILGKGKYQS MLGSLLVELD
     NGLQFKIGSG FSDLQRLAPP QVGTIITFKH YGLTARGIPR FASFLRVKPM AELDKN
//
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