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Database: UniProt/TrEMBL
Entry: S4ZJ86_9MYCO
LinkDB: S4ZJ86_9MYCO
Original site: S4ZJ86_9MYCO 
ID   S4ZJ86_9MYCO            Unreviewed;       509 AA.
AC   S4ZJ86;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 25.
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=OEM_38270 {ECO:0000313|EMBL:AGP65362.1};
OS   Mycobacterium yongonense 05-1390.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1138871 {ECO:0000313|EMBL:AGP65362.1, ECO:0000313|Proteomes:UP000014801};
RN   [1] {ECO:0000313|EMBL:AGP65362.1, ECO:0000313|Proteomes:UP000014801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05-1390 {ECO:0000313|EMBL:AGP65362.1};
RX   PubMed=23929490;
RA   Kim B.J., Kim B.R., Lee S.Y., Seok S.H., Kook Y.H., Kim B.J.;
RT   "Whole-Genome Sequence of a Novel Species, Mycobacterium yongonense
RT   DSM 45126T.";
RL   Genome Announc. 1:e00604-13(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; CP003347; AGP65362.1; -; Genomic_DNA.
DR   RefSeq; WP_020823283.1; NC_021715.1.
DR   EnsemblBacteria; AGP65362; AGP65362; OEM_38270.
DR   KEGG; myo:OEM_38270; -.
DR   PATRIC; fig|1138871.3.peg.3809; -.
DR   KO; K10747; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000014801; 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:UP000014801};
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:AGP65362.1};
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      290    414       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     302    302       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     374    374       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     380    380       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   509 AA;  53465 MW;  83F485AA79CC7408 CRC64;
     MLLLDVATAS TDVGSTSSRL RKVAHIADLL ARAAPDPALV MIVVSWLSGE LRQRQIGVGW
     AALRSRPPPA SHATLTVSAV DATFSEIGAV SGKGAQARRA ALLATLFAAA TETEQTFLLR
     LLGGELRQGA LAGIMADAVA KAAGIAGAAV QRAAMLGGDL PAVAAAALSG EPAALQAFTL
     RVGRPVGPML ARTAPSVADA IERHGGRAIF EAKLDGARVQ IHRAGDQVTV YTRSLDDVTA
     RLPEVVEATL ALPVNDLIAD GEAIALRPDN RPQRFQVTAS RFGRSVDIAA AVAAQPLSVF
     FFDILHRDGV DLLDAPTTDR LAALDALVPP AQRVDRLLTS DPAEAGAFLD ATLAAGHEGV
     MAKAPDAPYQ AGRRGAGWLK VKPVHTLDLV VLAVEWGSGR RRGKLSNIHL GARDPDSGEF
     VMVGKTFKGM TDAMLDWQTA RFSDLAIGGT DGYVVHVRPE QVVEVALDGV QKSSRYPGGL
     ALRFARVVRY RDDKGPAEAD TIDAVRALY
//
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