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Database: UniProt
Entry: A5UKX2
LinkDB: A5UKX2
Original site: A5UKX2 
ID   DNLI_METS3              Reviewed;         551 AA.
AC   A5UKX2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-OCT-2017, entry version 69.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=Msm_0645;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 /
OS   PS).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M.,
RA   Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K.,
RA   Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to
RT   the human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|HAMAP-Rule:MF_00407}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
DR   EMBL; CP000678; ABQ86850.1; -; Genomic_DNA.
DR   RefSeq; WP_004036507.1; NC_009515.1.
DR   ProteinModelPortal; A5UKX2; -.
DR   SMR; A5UKX2; -.
DR   STRING; 420247.Msm_0645; -.
DR   EnsemblBacteria; ABQ86850; ABQ86850; Msm_0645.
DR   GeneID; 5216232; -.
DR   KEGG; msi:Msm_0645; -.
DR   PATRIC; fig|420247.28.peg.642; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001992; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
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-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    551       DNA ligase.
FT                                /FTId=PRO_1000049872.
FT   ACT_SITE    248    248       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     246    246       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     253    253       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     268    268       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     298    298       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     337    337       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     414    414       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     420    420       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   551 AA;  61948 MW;  5CB10B16F770ACFB CRC64;
     MKYQELVDVY SALENTTKRL EKTQIISNFL LKLDSTTLEQ VGLLILGSIF PAWSDKEIGI
     GNKLVMQAVG EAVGVTPDKV EDAVRDQGDI GLACISLYAK KSQTTFFSQP LTIDFVFKSL
     RKLSEKSGAR STKRKIDIIL EMLSQASASE AKYLTRTILE ELRIGVGEGV VRDAIAQAFN
     IDKSVVERAM MLTNDLGLIA VVAKEKGEGG LKELNLTPGT PVKPMLAQLA PPIPEIINEM
     GVAICETKYD GIRLQVHRHS DEIKIFTRRL ENITHALPEI VDLFNEYLPH EDYIVEGEVI
     ATRDGNPLSF QNILHRVRRK HNIDEAMEQV PLKVFLFDLL YYIVPMIDEP LLKRRKKLEE
     IVNTTPDEIN LSNMVYGTPD TIKEVEDLFE LSIAQHHEGI MIKDAGEPYI PGLRGKKMLK
     YKAEPETLDM VVVGGTYGIG KRGDFVGSYL VSLRDEDNNL KTVAYVATGL DDATLEYLTK
     KMKEYELSTK GREIVVEPKI VLEVAFSEIV ESPEYETGYS LRFPVVKNIR KDKGVDDIDT
     VERLISMYET Q
//
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