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Database: UniProt/SWISS-PROT
Entry: DNLI_PYRCJ
LinkDB: DNLI_PYRCJ
Original site: DNLI_PYRCJ 
ID   DNLI_PYRCJ              Reviewed;         583 AA.
AC   A3MS62;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   05-DEC-2018, entry version 72.
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=Pcal_0039;
OS   Pyrobaculum calidifontis (strain JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C.,
RA   Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) 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:0000255|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|HAMAP-
CC         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; CP000561; ABO07479.1; -; Genomic_DNA.
DR   ProteinModelPortal; A3MS62; -.
DR   SMR; A3MS62; -.
DR   STRING; 410359.Pcal_0039; -.
DR   EnsemblBacteria; ABO07479; ABO07479; Pcal_0039.
DR   KEGG; pcl:Pcal_0039; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001431; 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; 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.
FT   CHAIN         1    583       DNA ligase.
FT                                /FTId=PRO_1000049876.
FT   ACT_SITE    251    251       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     249    249       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     256    256       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     271    271       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     301    301       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     341    341       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     416    416       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     422    422       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   583 AA;  64840 MW;  3B3B4E318FC2C215 CRC64;
     MQFGELAKVL AAVESTTQRT TMVKLLTSLF KKAKPEEIDK IVYFILGDLR PPWEGVELGV
     AEKLCIRAIS KATGLSAAEL EGWYKKSGDV GEVARRALAA GKRPTLLAFA QQKPLEVAEV
     YDTLLKVAKA AGEGAQDLKV SLLSSLFSRA SPEEAKYIAR FVVGKLRLGV ADMTLIEALS
     EAFGVSKEGL ERAYHVYPDL GRLARHVAEG RPLEEIKITP GVPVLPMLAQ RLSSASEILA
     KLGGTAICEY KYDGERAQIH LREGSVKIFS RRLEDITHAY PDVAKAVKEA VKAREAILEG
     EIVAVDPDTG EMLPFQELMH RKRKHDVAEA MEAYPAVLYL FDLLYVDGED LTTQPLIYRR
     LRLSEVVEEG GDVYIAKWGM FDGAEDVDLF FHEAVSLGTE GLICKSPTST YEMGARGWNW
     IKYKRDYRSE MIDTVDLVVV GAFHGRGKRA GLYGAFLLAA YDPSTDMFYT VCKVGSGFTD
     ADLRRMYDML QPLKIPHRHP RVVSKMQPDV WFVPQVVIEV IGAEITLSPL HTCCIGAVKP
     GVGLAIRFPR FTGRYRTDKR PEDATTTKEL VEMYQRQKKV PTT
//
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