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Database: UniProt/SWISS-PROT
Entry: DNLI_PYRIL
LinkDB: DNLI_PYRIL
Original site: DNLI_PYRIL 
ID   DNLI_PYRIL              Reviewed;         584 AA.
AC   A1RTK4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   28-MAR-2018, entry version 71.
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=Pisl_1115;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Lowe T.,
RA   Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) 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; CP000504; ABL88286.1; -; Genomic_DNA.
DR   RefSeq; WP_011762861.1; NC_008701.1.
DR   ProteinModelPortal; A1RTK4; -.
DR   SMR; A1RTK4; -.
DR   STRING; 384616.Pisl_1115; -.
DR   EnsemblBacteria; ABL88286; ABL88286; Pisl_1115.
DR   GeneID; 4616742; -.
DR   KEGG; pis:Pisl_1115; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; PISL384616:G1G7P-1223-MONOMER; -.
DR   Proteomes; UP000002595; 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_1000049877.
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;  65093 MW;  D050BF645449D34A CRC64;
     MQFGELVKTL AAVESTTQRT TMVKLLTSLF KKARPEEIDK IIYFVLGDLR PPWEGVELGV
     AEKLCLRAVS KATGVSISEL EALYKKTGDV GEAARKALST AKRPGLLAFG QQKPLEVSEV
     YDTLLKVAQA SGEGAQDMKI SLLASLFAKA SPEEAKYIAR FVVGKLRLGV ADMTLIEALS
     DAFGVDKEAL ERAYHIYPDL GKLARHVAEG RPLEEIKITP GVPVLPMLAQ RLSSSSEILA
     KLGGSAICEY KYDGERAQIH LKEGVVKIFS RRLEDITHAY PDVVKAVREA VSAREAILEG
     EIVAIDPDTG DMLPFQELMH RKRKHEVAVA VEMYPVVLNL FDLLYIDGED LTNEPLIYRR
     VRLSEVVQET EKVSIAKWRV FDDAEEIDVF FHEAVSLGME GLVCKSPTSV YEMGARGWNW
     IKYKRDYKSE MIDTVDLVVV GAFYGRGKRA GLYGAFLLAA YDPATDMFYT VCKVGSGFTD
     ADLKKMYEML QPYKIPHRHP RVVSKMEPDV WFTPQVVIEV IGAEITLSPL HTCCLGAVKP
     GVGLAIRFPR FTGRYRTDKS PEQATTVSEM IELYKRQKKV AQPE
//
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