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Database: UniProt
Entry: A0A0Q2R923_MYCGO
LinkDB: A0A0Q2R923_MYCGO
Original site: A0A0Q2R923_MYCGO 
ID   A0A0Q2R923_MYCGO        Unreviewed;       255 AA.
AC   A0A0Q2R923;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=AO501_07950 {ECO:0000313|EMBL:KQH80510.1};
OS   Mycobacterium gordonae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH80510.1, ECO:0000313|Proteomes:UP000051677};
RN   [1] {ECO:0000313|EMBL:KQH80510.1, ECO:0000313|Proteomes:UP000051677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH80510.1,
RC   ECO:0000313|Proteomes:UP000051677};
RA   Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA   Chernousova L.;
RT   "Mycobacterium gordonae draft genome assembly.";
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   -!- 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:KQH80510.1}.
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DR   EMBL; LKTM01000023; KQH80510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q2R923; -.
DR   Proteomes; UP000051677; 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:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051677}.
FT   DOMAIN          42..177
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   255 AA;  28207 MW;  715BF2DA5671B260 CRC64;
     MLDGEIVVVD ADGRPDFGRL QQRWPQNRRP STDLLRTAPA LFYAFDVLAV DGIDTTGEPY
     TRRRELLEDD IALGSRLRVV PRFDTRELRV VDALAVAAEH RMEGVVSKRL ESVYRPGRST
     AWLKTCCRVR SEFLIGGWLP GGANRKEIGA LIVGAYDDFG RLAYCGTVGA GLSAAHRRVL
     HKRLSPLASA VSPFATAVPP DVARFANWVR AEAAGDVEYR ELRGMLRHPS WKGLRADLDD
     VTAVRMPADA RARSA
//
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