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Database: UniProt/TrEMBL
Entry: A0A1Y0C7X3_9MYCO
LinkDB: A0A1Y0C7X3_9MYCO
Original site: A0A1Y0C7X3_9MYCO 
ID   A0A1Y0C7X3_9MYCO        Unreviewed;       507 AA.
AC   A0A1Y0C7X3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   25-OCT-2017, entry version 3.
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=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   ORFNames=BTO20_24010 {ECO:0000313|EMBL:ART71197.1};
OS   Mycobacterium dioxanotrophicus.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=482462 {ECO:0000313|EMBL:ART71197.1, ECO:0000313|Proteomes:UP000195331};
RN   [1] {ECO:0000313|EMBL:ART71197.1, ECO:0000313|Proteomes:UP000195331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-06 {ECO:0000313|EMBL:ART71197.1,
RC   ECO:0000313|Proteomes:UP000195331};
RA   He Y.;
RT   "Whole Genome Sequence of 1,4-Dioxane Degrading Bacterium
RT   Mycobacterium dioxanotrophicus PH-06.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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; CP020809; ART71197.1; -; Genomic_DNA.
DR   Proteomes; UP000195331; 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   Gene3D; 1.10.3260.10; -; 1.
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; IPR036599; DNA_ligase_N_sf.
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; PS00333; DNA_LIGASE_A2; 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:UP000195331};
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:ART71197.1};
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      286    410       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    213    213       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     211    211       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     218    218       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     233    233       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     262    262       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     298    298       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     370    370       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     376    376       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   507 AA;  53608 MW;  8D537C696B300621 CRC64;
     MLLAEVVAAS ADVAASSGRL AKTERIATLL SAIIAAGEPV AVVVAWLSGE LPQRQIGVGW
     AGLRDLPTPA ATPTLTVTDV DSRLSAIGAV TGKGSQAHRA RLVRELFGAA TAGEQTFLRR
     LLGGELRQGA LVGVMADAVA RSSGIPATEV RRAAMLAGDL PAVAAAAATG GVTAVQAFGL
     QVGRPVGPML AQTASDIDDA LEKLGGTAVL ETKLDGARVQ IHRVGSDVSI YTRSLDDVTS
     RLPEVVAATL ALPVTDLIAD AEAIALRPDG RPHRFQVTAS RFGRRNPTDE VPLSVFFFDL
     LHVDGRDLLD LPTLERRAAL DAIVPASRRV DHIVTADPEQ AREFVATTLA AGHEGVMAKA
     PGAPYEAGRR GAGWLKVKPV HTLDLVVLAV EWGSGRRTGK LSNIHLGARD PETGGFVMLG
     KTFKGMTDAM LAWQTERFTE LADGPIDGYV VKLRPEQVVE IAFDGVQGSS RYPGGMALRF
     ARVLRYRDDK SPEEADTVET VRALYER
//
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