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Database: UniProt
Entry: A0A1E7ZAG8_9ALTE
LinkDB: A0A1E7ZAG8_9ALTE
Original site: A0A1E7ZAG8_9ALTE 
ID   A0A1E7ZAG8_9ALTE        Unreviewed;       280 AA.
AC   A0A1E7ZAG8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=DNA ligase {ECO:0000313|EMBL:OFC70414.1};
GN   ORFNames=BFC18_14720 {ECO:0000313|EMBL:OFC70414.1};
OS   Alteromonas confluentis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1656094 {ECO:0000313|EMBL:OFC70414.1, ECO:0000313|Proteomes:UP000175691};
RN   [1] {ECO:0000313|EMBL:OFC70414.1, ECO:0000313|Proteomes:UP000175691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42603 {ECO:0000313|EMBL:OFC70414.1,
RC   ECO:0000313|Proteomes:UP000175691};
RA   Seilhamer J.J.;
RL   Submitted (AUG-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:OFC70414.1}.
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DR   EMBL; MDHN01000029; OFC70414.1; -; Genomic_DNA.
DR   RefSeq; WP_070126058.1; NZ_MDHN01000029.1.
DR   AlphaFoldDB; A0A1E7ZAG8; -.
DR   STRING; 1656094.BFC18_14720; -.
DR   OrthoDB; 9782700at2; -.
DR   Proteomes; UP000175691; 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; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:OFC70414.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000175691};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..280
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009209582"
FT   DOMAIN          113..226
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   280 AA;  31911 MW;  629F603F27000ACF CRC64;
     MLTIFFTILL ALTLPAELAA APLQLPKTYN QHDNLNISNY LISEKLDGIR ARWTGSELLT
     RNGNRIHAPV WFTQNWPAEP LDGELWTKRN DFQRIASIVL SETPDARWRD VRLMVFDSPA
     SNAPFAKRVE QMKRIINKTE SQTLQLIPQF TVSSEAEFEQ RLDEVVKAGG EGLMLHHREA
     RYQDGRSEYL LKAKRFEDDE ARVIEYLPGK GKYAGMMGSL LVEGRSGLQF KIGSGFTNAE
     RLNPPPIGSW VTYKFYGKTK KGLPRFASFM HVRPAADRPQ
//
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