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Database: UniProt/TrEMBL
Entry: A0A0A1FN99_9MYCO
LinkDB: A0A0A1FN99_9MYCO
Original site: A0A0A1FN99_9MYCO 
ID   A0A0A1FN99_9MYCO        Unreviewed;       507 AA.
AC   A0A0A1FN99;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
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=G155_10930 {ECO:0000313|EMBL:AIY45996.1};
OS   Mycobacterium sp. VKM Ac-1817D.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1273687 {ECO:0000313|EMBL:AIY45996.1, ECO:0000313|Proteomes:UP000030340};
RN   [1] {ECO:0000313|EMBL:AIY45996.1, ECO:0000313|Proteomes:UP000030340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1817D {ECO:0000313|EMBL:AIY45996.1,
RC   ECO:0000313|Proteomes:UP000030340};
RX   PubMed=23474435; DOI=10.1016/j.jsbmb.2013.02.016;
RA   Bragin E.Y., Shtratnikova V.Y., Dovbnya D.V., Schelkunov M.I.,
RA   Pekov Y.A., Malakho S.G., Egorova O.V., Ivashina T.V., Sokolov S.L.,
RA   Ashapkin V.V., Donova M.V.;
RT   "Comparative analysis of genes encoding key steroid core oxidation
RT   enzymes in fast-growing Mycobacterium spp. strains.";
RL   J. Steroid Biochem. Mol. Biol. 138:41-53(2013).
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; CP009914; AIY45996.1; -; Genomic_DNA.
DR   RefSeq; WP_038563874.1; NZ_CP009914.1.
DR   EnsemblBacteria; AIY45996; AIY45996; G155_10930.
DR   KEGG; myv:G155_10930; -.
DR   KO; K10747; -.
DR   Proteomes; UP000030340; 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:UP000030340};
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:AIY45996.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030340}.
FT   DOMAIN      288    412       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    215    215       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     213    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     220    220       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     235    235       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     264    264       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     300    300       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     372    372       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     378    378       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   507 AA;  53686 MW;  F5F6DD77222B0CD4 CRC64;
     MLLAEVAAAS ADIAGAAARL AKIDRIASLL SVAAAEGDAR AVAVTVSWLS GELPQRQIGV
     GWAALRSLPA PAENPTLTVA GVDTAFTEIK AIAGKGSQAL RADSVRALFG TATETEQTFL
     RRLLGGELRQ GALAGVMADA VARASAIPAA EVRRAAMLAG DLPAVAAAAL TGGRTALAEF
     ALQVGRPVGP MLAQTATDLA DALERLGGTA VLEAKLDGAR VQIHRTGAEV AVYTRSLDDV
     THRLPEVVAA TLALPATDLI ADAEAIALRP DNRPHPFQVT AARFGRKIAN DLEPLSVFFF
     DLLHVDGQDL LDLPTEQRLA ALDALVPHDR RVDRIVTDDV DAARQFLDRT LAAGHEGVMA
     KSPTAPYEAG RRGAGWLKVK PVHTLDLVVL AVERGSGRRT GKLSNIHLGA RDPDTGGFVM
     LGKTFKGMTD AMLAWQTERF RELEVSDDGW AVTVRPEQVV EIAFDGVQRS SRYPGGVALR
     FARVLRYRDD KPAAEADTID TVRAFLT
//
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