ID L0J729_9MYCO Unreviewed; 330 AA.
AC L0J729;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=Mycsm_07191 {ECO:0000313|EMBL:AGB27285.1};
OS Mycobacterium sp. JS623.
OG Plasmid pMYCSM03 {ECO:0000313|EMBL:AGB27285.1,
OG ECO:0000313|Proteomes:UP000010844}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB27285.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|EMBL:AGB27285.1, ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|EMBL:AGB27285.1,
RC ECO:0000313|Proteomes:UP000010844};
RC PLASMID=pMYCSM03 {ECO:0000313|EMBL:AGB27285.1,
RC ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of plasmid 3 of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003081; AGB27285.1; -; Genomic_DNA.
DR RefSeq; WP_015298181.1; NC_019959.1.
DR AlphaFoldDB; L0J729; -.
DR KEGG; msa:Mycsm_07191; -.
DR HOGENOM; CLU_008325_4_0_11; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000010844; Plasmid pMYCSM03.
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; 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; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AGB27285.1};
KW Plasmid {ECO:0000313|EMBL:AGB27285.1}.
FT DOMAIN 113..205
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 330 AA; 35975 MW; 715EDC2123A443A8 CRC64;
MSTSRKLAVR DPAFAPMLAT LGTPPPASDD QAVEVKFDGQ RATLLLANGR VTVFSRNGLD
VSSCFPELSR VAAAVGDRPM VLDGEIVAVD AHGRPSFTRL QRRWPQQRRP SAQLLREVPV
RMLAFDIIQL DGRDLTNAPY GQRRELLDTV MVVDKSPVLT VPRAMLGVAP ADALQACAAH
GMEGIVTKRL DSPYTPGERS PHWRKTPYRA SAELLVAGYW CASGPGGRSC VGSLLVAGHD
AAGDLVACGQ VGTGFSDSTR RRLYAQLHPT RRATSPVSNP IEVPGVRWVE PRLVVEVAYR
EYVEGRWLRH PSFKGERAVE PAEVRLPVCT
//
