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Database: UniProt
Entry: A0A1A1Y769_9MYCO
LinkDB: A0A1A1Y769_9MYCO
Original site: A0A1A1Y769_9MYCO 
ID   A0A1A1Y769_9MYCO        Unreviewed;       314 AA.
AC   A0A1A1Y769;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=A5724_03755 {ECO:0000313|EMBL:OBF27167.1};
OS   Mycobacterium sp. ACS1612.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF27167.1, ECO:0000313|Proteomes:UP000092025};
RN   [1] {ECO:0000313|Proteomes:UP000092025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA   Musoke P., Ssengooba W., Joloba M.;
RL   Submitted (JUN-2016) 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}.
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:OBF27167.1}.
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DR   EMBL; LZHZ01000067; OBF27167.1; -; Genomic_DNA.
DR   RefSeq; WP_067810735.1; NZ_LZHZ01000067.1.
DR   AlphaFoldDB; A0A1A1Y769; -.
DR   STRING; 1834117.A5724_03755; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000092025; 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; 3.30.1490.70; -; 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:SF4; DNA LIGASE 1; 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   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OBF27167.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092025}.
FT   DOMAIN          103..236
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   314 AA;  35315 MW;  A1629AE17788E405 CRC64;
     MVPDWQSPTL ATLTDERFSA PDWIFERKLD GVRGLVFRDH GQIRLLSRNR LSLNKTYPEI
     VEALAGQAPA QFVMDGEIVA FEGRRTSFAR LQGRSGITDP ILAEASGIPV FYYAFDLLNL
     DGQDITDRPL LSRKRLLRNS FRYDGALRFT THRVRDGESA YRAACERGDE GVIAKLAESA
     YEGGRSRHWL KFKCTRDQEF VVVGYTAPKG ARVGLGALLL GYYDGHELVY AGKVGSGFDD
     VTLRSLRDQL AGTELSTPPI TRGSVREPTV RWVRPQLVAQ VAFGEWTRDG KLRHPRYLGL
     RTDKSPDDVV RETH
//
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