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Database: UniProt/TrEMBL
Entry: A0A0H3LKL2_MYCTE
LinkDB: A0A0H3LKL2_MYCTE
Original site: A0A0H3LKL2_MYCTE 
ID   A0A0H3LKL2_MYCTE        Unreviewed;       502 AA.
AC   A0A0H3LKL2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Probable DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=ligB {ECO:0000313|EMBL:BAL67129.1};
GN   Synonyms=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=ERDMAN_3352 {ECO:0000313|EMBL:BAL67129.1};
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616 {ECO:0000313|EMBL:BAL67129.1, ECO:0000313|Proteomes:UP000007568};
RN   [1] {ECO:0000313|EMBL:BAL67129.1, ECO:0000313|Proteomes:UP000007568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman
RC   {ECO:0000313|Proteomes:UP000007568};
RX   PubMed=22535945; DOI=10.1128/JB.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis
RT   Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU000617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; AP012340; BAL67129.1; -; Genomic_DNA.
DR   EnsemblBacteria; BAL67129; BAL67129; ERDMAN_3352.
DR   KEGG; mtn:ERDMAN_3352; -.
DR   PATRIC; fig|652616.3.peg.3417; -.
DR   KO; K10747; -.
DR   Proteomes; UP000007568; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
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; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007568};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:BAL67129.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      283    407       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    206    206       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     204    204       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     211    211       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     226    226       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     255    255       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     295    295       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     367    367       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     373    373       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   502 AA;  53149 MW;  B6C9D515A5C0B5A7 CRC64;
     MAITSMDVAA TSSRLTKVAR IAALLHRAAP DTQLVTIIVS WLSGELPQRH IGVGWAALRS
     LPPPAPQPAL TVTGVDATLS KIGTLSGKGS QAQRAALVAE LFSAATEAEQ TFLLRLLGGE
     LRQGAKGGIM ADAVAQAAGL PAATVQRAAM LGGDLAAAAA AGLSGAALDT FTLRVGRPIG
     PMLAQTATSV HDALERHGGT TIFEAKLDGA RVQIHRANDQ VRIYTRSLDD VTARLPEVVE
     ATLALPVRDL VADGEAIALC PDNRPQRFQV TASRFGRSVD VAAARATQPL SVFFFDILHR
     DGTDLLEAPT TERLAALDAL VPARHRVDRL ITSDPTDAAN FLDATLAAGH EGVMAKAPAA
     RYLAGRRGAG WLKVKPVHTL DLVVLAVEWG SGRRRGKLSN IHLGARDPAT GGFVMVGKTF
     KGMTDAMLDW QTTRFHEIAV GPTDGYVVQL RPEQVVEVAL DGVQRSSRYP GGLALRFARV
     VRYRADKDPA EADTIDAVRA LY
//
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