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Database: UniProt
Entry: A0A117I4M1_9MYCO
LinkDB: A0A117I4M1_9MYCO
Original site: A0A117I4M1_9MYCO 
ID   A0A117I4M1_9MYCO        Unreviewed;       344 AA.
AC   A0A117I4M1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=RMCB_1263 {ECO:0000313|EMBL:GAS87167.1};
OS   Mycolicibacterium brisbanense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS87167.1, ECO:0000313|Proteomes:UP000069620};
RN   [1] {ECO:0000313|EMBL:GAS87167.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM15654 {ECO:0000313|EMBL:GAS87167.1};
RA   Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT   "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT   thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT   M. brisbanense, and M. novocastrense.";
RL   Genome Announc. 4:e00322-16(2016).
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:GAS87167.1}.
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DR   EMBL; BCSX01000016; GAS87167.1; -; Genomic_DNA.
DR   RefSeq; WP_062828107.1; NZ_JACKTM010000065.1.
DR   AlphaFoldDB; A0A117I4M1; -.
DR   STRING; 146020.RMCB_1263; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000069620; 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:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 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; IPR016059; DNA_ligase_ATP-dep_CS.
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; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:GAS87167.1}.
FT   DOMAIN          132..257
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   344 AA;  39473 MW;  F5AC2C770511ACE3 CRC64;
     MASADDDGHE IDCRLDRLPS EVRKLLQSEP VPTWRAPMLA TLTDQRFSDP RWIFELKLDG
     ERCLAFRDAD RTRLLSRNRQ SLNGTYPEIV HALNAQRSTR FVLDGEVVAF QGKHTSFQRL
     QSRLGVTNVD ETQASRTPVF YYVFDLLHLD GYATTALPLI WRKRLLHSAI RWTDPLRYLP
     HRRTEGQRAY QEASERGDEG VIAKLADSTY EQGHRSPNWL KFKCVLRQEF VIGGYTAPKG
     TRVGLGALLI GYYAGDKLIY AGKVGTGFDE ATLRSLHQRL SAIEQDESPF PGHRVVRPDT
     HWTRPQLVAD IGFSEWTRDG KLRHPRYVGL RYDKRPAEVV RESL
//
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