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Database: UniProt/TrEMBL
Entry: Q2RIE2_MOOTA
LinkDB: Q2RIE2_MOOTA
Original site: Q2RIE2_MOOTA 
ID   Q2RIE2_MOOTA            Unreviewed;       320 AA.
AC   Q2RIE2;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=Moth_1488 {ECO:0000313|EMBL:ABC19797.1};
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX   NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC19797.1};
RN   [1] {ECO:0000313|EMBL:ABC19797.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC19797.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT   "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL   Submitted (DEC-2005) 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};
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DR   EMBL; CP000232; ABC19797.1; -; Genomic_DNA.
DR   RefSeq; YP_430340.1; NC_007644.1.
DR   AlphaFoldDB; Q2RIE2; -.
DR   STRING; 264732.Moth_1488; -.
DR   EnsemblBacteria; ABC19797; ABC19797; Moth_1488.
DR   KEGG; mta:Moth_1488; -.
DR   PATRIC; fig|264732.11.peg.1611; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   OrthoDB; 9802472at2; -.
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:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
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; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
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, ECO:0000313|EMBL:ABC19797.1}.
FT   DOMAIN          111..202
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   320 AA;  36367 MW;  A48D620C01FA9EA8 CRC64;
     MTTTGAGLPL FQIRPMLAVI SRPFDSPDFL YEIKWDGYRC LAYLEGQTLL QSRNLLNITP
     TFPELASLHQ RVKGQPAVLD GEIIVPGKDG KPSFSLLQGR GRLGDPLKVR QAARRMPAIF
     VAFDLLYYQG ENIMPEPLRW RKERLQEALA PGENLIVSSF IENYGMKFYE ACVGQGLEGV
     MAKELDSPYL PGKRSPRWRK FRHTRAGEFI IAGYEPGAGG RLLGSLILAE CREGQLVYRG
     KVGTGFDRQE EKKLLVELQQ LQPGPPPFKE NIPELRKPRW VQPRLVCTVE YLELTPDGRL
     RHPTYRGLRW DKAPWECTST
//
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