GenomeNet

Database: UniProt
Entry: Q74M64
LinkDB: Q74M64
Original site: Q74M64 
ID   DNLI_NANEQ              Reviewed;         567 AA.
AC   Q74M64;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-OCT-2017, entry version 79.
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}; OrderedLocusNames=NEQ509;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Nanoarchaeales; Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X.,
RA   Mathur E., Ni J., Podar M., Richardson T., Sutton G.G., Simon M.,
RA   Soell D., Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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; AE017199; AAR39350.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q74M64; -.
DR   SMR; Q74M64; -.
DR   STRING; 228908.NEQ509; -.
DR   EnsemblBacteria; AAR39350; AAR39350; NEQ509.
DR   KEGG; neq:NEQ509; -.
DR   PATRIC; fig|228908.8.peg.527; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   Proteomes; UP000000578; 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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; 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; 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; 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    567       DNA ligase.
FT                                /FTId=PRO_0000365262.
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     339    339       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     415    415       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     421    421       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   567 AA;  65701 MW;  F23605248ACD6A51 CRC64;
     MEFEKLANLF SKLETISDKT RKVQYIARFL KELKDQYKET LLLLQGTVFY PWEQKNLGIA
     EKGVIRAISI AYGIEKQKVE ELFIKYGDLG IVAEKACEMR KQKPLLLKPL TVKDVYQTLR
     KIADIEGEGS QDKKIITFAK LLVNAKPKEA KYIVRLALEE LRIGVGEGII RDAIAIAFSV
     TPEAVEYAYS ILLDFGEVVR IAKEQGEQGL WQVKLQVGRP FRVMLAIRAR NVQEAFDIVG
     RPAMIEAKYD GFRLQIHKKG DQVWLWTRRL EDVTRQFPDV VNIVRNRVKA NEIIFEAEAV
     GYDKKTNKFL PFQKISQRVK RKYDIEKMAK EIPVELHAFD IVYLEGEQLM KKPFKERRAL
     LEKVIDEKEH EIQLSIGIIE KDDKKAYQFY QDCLNKGLEG VMFKNLNAPY QPGRRVGYMV
     KLKPTLETLD LVIVAAEWGE GKRSGWLTSF TVAALDKDTG NYLEVGEVGT GIKEKKERAE
     DITFEELTEL LKPYIYKQEG KKVYVKPKIV VEVAYEEIQE SPRYKSGFAL RFPRIVRIRF
     DRSPKEIDTI DRIKQIYEMQ RGGIHKQ
//
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