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Database: UniProt/SWISS-PROT
Entry: DNLI_PYRHO
LinkDB: DNLI_PYRHO
Original site: DNLI_PYRHO 
ID   DNLI_PYRHO              Reviewed;         559 AA.
AC   O59288;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   20-JUN-2018, entry version 121.
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=PH1622;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 /
OS   NBRC 100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA30734.1; -; Genomic_DNA.
DR   PIR; F71041; F71041.
DR   RefSeq; WP_010885696.1; NC_000961.1.
DR   ProteinModelPortal; O59288; -.
DR   SMR; O59288; -.
DR   STRING; 70601.PH1622; -.
DR   PRIDE; O59288; -.
DR   EnsemblBacteria; BAA30734; BAA30734; BAA30734.
DR   GeneID; 1442475; -.
DR   KEGG; pho:PH1622; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; PHOR70601:G1G39-1575-MONOMER; -.
DR   Proteomes; UP000000752; 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; 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.
FT   CHAIN         1    559       DNA ligase.
FT                                /FTId=PRO_0000059614.
FT   ACT_SITE    249    249       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     247    247       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     254    254       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     269    269       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     339    339       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   559 AA;  63623 MW;  D1E85172B1D72188 CRC64;
     MKYIELAQLY QKLEKTTMKL IKTRLVADFL KRVPEDHLDF IPYLILGDVF PEWDERELGV
     GEKLLIKAVS MATGVDPKEI ENSVKDTGDL GESIALAIKR RKQKSFFSQP LTIKRVYQTL
     VKIAETTGEG SQEKKMKYLA NLFMDAEPLE AKYLARTVLG TMRTGVAEGL LRDAIALAFH
     VKVELVERAY MLTSDFGFVA KIAKAEGNEG LEKVTIQLGK PIKPMLAQQA ANIKEALLEM
     GGEAEFEIKY DGARVQVHKD GEKVIIYSRR LENVTRAIPE IVEAIKEAIE PEKVIVEGEL
     VAIGEEGRPL PFQYVLRRFR RKHNIEEMMK KIPLELNLFD VLYVDGKSFV DTKFIERRKK
     LEEIVKPNGK IKVAENLITK NAEEAEKFYK RALEMGHEGL MAKRLDAVYE PGNRGKKWLK
     IKPTMENLDL VIIGAEWGEG RRAHLFGSFI LGAYDPETGE FLEVGKVGSG FTDDDLVEFT
     KMLKPLIVKE EGKRVVIQPK IVIEVTYQEI QKSPKYRSGF ALRFPRYVAL RDDKGPEDAD
     TIERIAQLYE LQERIKGKV
//
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