ID I2A7M4_9MYCO Unreviewed; 356 AA.
AC I2A7M4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN Name=ligC {ECO:0000313|EMBL:AFJ33298.1};
GN ORFNames=W7S_01565 {ECO:0000313|EMBL:AFJ33298.1};
OS Mycobacterium sp. MOTT36Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1168287 {ECO:0000313|EMBL:AFJ33298.1, ECO:0000313|Proteomes:UP000002868};
RN [1] {ECO:0000313|EMBL:AFJ33298.1, ECO:0000313|Proteomes:UP000002868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOTT36Y {ECO:0000313|EMBL:AFJ33298.1,
RC ECO:0000313|Proteomes:UP000002868};
RX PubMed=22815454; DOI=10.1128/JB.00752-12;
RA Kim B.J., Choi B.S., Choi I.Y., Lee J.H., Chun J., Hong S.H., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare clinical strain
RT MOTT-36Y, belonging to the INT5 genotype.";
RL J. Bacteriol. 194:4141-4142(2012).
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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DR EMBL; CP003491; AFJ33298.1; -; Genomic_DNA.
DR RefSeq; WP_008263203.1; NC_017904.1.
DR AlphaFoldDB; I2A7M4; -.
DR GeneID; 66743298; -.
DR KEGG; mmm:W7S_01565; -.
DR PATRIC; fig|1168287.3.peg.324; -.
DR HOGENOM; CLU_008325_4_1_11; -.
DR Proteomes; UP000002868; Chromosome.
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; cd07905; Adenylation_DNA_ligase_LigC; 1.
DR CDD; cd07970; OBF_DNA_ligase_LigC; 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; IPR044119; Adenylation_LigC-like.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR044117; OBF_LigC-like.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AFJ33298.1}.
FT DOMAIN 114..248
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 356 AA; 39909 MW; B186362A7C46E100 CRC64;
MDLPVMPPVS PMLAKSVRAI PPHASYEPKW DGFRSICFRD GDDVELGSRN ERPMTRYFPE
LVAAVRAELP ERCVIDGEIV IATDHGLDFE ALQQRIHPAD SRVRMLAEAT PASFIAFDLL
ALGGDDYTRR PFSERRAALV DAVGGSGRSI HVTPATTDLG TAQRWFDEFE GAGLDGVIAK
PLDVTYQPDK RVMFKIKHER TADCVVAGYR VHKSGADAIG SLLLGLYQDD GQLASVGVIG
AFPMAERRRL FAELQPLVTD FADHPWNWAA HEAGERTPRK NEYSRWNAGK DLSFVPLRPE
RVVEVRYDHM EGRRFRHTAQ FNRWRPDRDP RSCTYEQLEQ PVTFSLGEIV PGLGPG
//
