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Database: UniProt/SWISS-PROT
Entry: DNLI_PYRNV
LinkDB: DNLI_PYRNV
Original site: DNLI_PYRNV 
ID   DNLI_PYRNV              Reviewed;         584 AA.
AC   B1YA52;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   28-MAR-2018, entry version 66.
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=Tneu_0068;
OS   Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta)
OS   (Thermoproteus neutrophilus).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=444157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2338 / JCM 9278 / V24Sta;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Biddle J.F., Zhang Z.,
RA   Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL   Submitted (MAR-2008) 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: 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; CP001014; ACB39026.1; -; Genomic_DNA.
DR   ProteinModelPortal; B1YA52; -.
DR   SMR; B1YA52; -.
DR   STRING; 444157.Tneu_0068; -.
DR   EnsemblBacteria; ACB39026; ACB39026; Tneu_0068.
DR   KEGG; tne:Tneu_0068; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001694; 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; 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    584       DNA ligase.
FT                                /FTId=PRO_0000365267.
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   584 AA;  64534 MW;  01180CAA003A28EA CRC64;
     MQFGELVKTL AAVESTTQRT TMVKLLTSLL KRARPDEVDK IVYFVLGDLK PPWEGVELGV
     AEKLCLRAVS KAAGTPLSEL EAVYKRTGDV GEAARRALSA AKRPGLLAFG QQKPLEVSEV
     YDTLLKVAKA AGEGAQDMKI SLLASLFARA TPEEAKYIAR FVVGKLRLGV ADMTLLEALS
     EAFGVGKEAL ERAYHVWPDM GKLARHVAEG RPLEEVKITP GVPVLPMLAQ RLSSASEILA
     KLGGAAVCEY KYDGERAQIH ISGGSVKIFS RRLEDITHAY PDVVKAVKES VAAGEAILEG
     EIVAVDPDTG DMLPFQELMH RKRKHEVAAA VESYPAVLNL FDVLYLDGED LTGEPLIYRR
     LRLSEVVHET EKVSIARWRL FDDPGEVDVF FHEAVSLGME GLVCKSPTSI YEMGARGWNW
     IKYKRDYKSE MIDTVDLVVV GAFYGRGKRA GLYGAFLLAA YDPQTDMFYT VCKVGSGFTD
     ADLKKMYEVL QPYKIPHRHP RVVSKMTPDV WFTPQVVIEV IGAEITLSPL HTCCLGAVRP
     GVGLAIRFPR FTGRYRTDKS PEQATTPAEM VELYKRQKKV AQPE
//
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