ID A1TGK9_MYCVP Unreviewed; 359 AA.
AC A1TGK9;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN OrderedLocusNames=Mvan_5543 {ECO:0000313|EMBL:ABM16309.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM16309.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM16309.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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DR EMBL; CP000511; ABM16309.1; -; Genomic_DNA.
DR RefSeq; WP_011782662.1; NZ_JACKSD010000145.1.
DR AlphaFoldDB; A1TGK9; -.
DR STRING; 350058.Mvan_5543; -.
DR KEGG; mva:Mvan_5543; -.
DR eggNOG; COG1793; Bacteria.
DR HOGENOM; CLU_008325_4_1_11; -.
DR Proteomes; UP000009159; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABM16309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT DOMAIN 18..214
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|Pfam:PF01068"
FT DOMAIN 232..334
FT /note="DNA ligase ATP-dependent C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04679"
SQ SEQUENCE 359 AA; 40366 MW; 06D55FB8AF2F0A61 CRC64;
MEPMPLSADL PVMPPLEPML AKAQTKVPDE PGMWSYEPKW DGFRALVFRD GGPGRDNVVL
LSRSGKDLAR YFPEVLDSVR DELAPRCVLD GEIVVPREIA GRTRLDWESL SQRIHPAESR
VRMLAEQTPA HFIGFDALAV GDSSLMKEPF RTRREALVDA VNEKQWCHVT RTTEDPALGA
QWLQEFEGAG LDGVIAKRLD GPYLPGKREM VKVKHHRDAD CVAIGYRIHK SGEGIGSILL
GLHRDDGELQ MVGGAASFTA KARLKLLADL EPLRIGDDVR DGEPSRWNSA ADKRWIPVRP
ERVCEVAYDQ MEGNSANGRR FRHAVKFLRW RPDRDPASCT FDQLDVPLNY DLNDVLERS
//
