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Database: UniProt/SWISS-PROT
Entry: DNLI_SULTO
LinkDB: DNLI_SULTO
Original site: DNLI_SULTO 
ID   DNLI_SULTO              Reviewed;         600 AA.
AC   Q976G4;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   28-MAR-2018, entry version 108.
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=STK_02230;
OS   Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M.,
RA   Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S.,
RA   Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y.,
RA   Yoshizawa T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T.,
RA   Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic
RT   Crenarchaeon, Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
RN   [2]
RP   ENZYME REGULATION.
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=18782564; DOI=10.1016/j.bbrc.2008.08.150;
RA   Lu S., Li Z., Wang Z., Ma X., Sheng D., Ni J., Shen Y.;
RT   "Spatial subunit distribution and in vitro functions of the novel
RT   trimeric PCNA complex from Sulfolobus tokodaii.";
RL   Biochem. Biophys. Res. Commun. 376:369-374(2008).
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   -!- ENZYME REGULATION: Inhibited by PCNA123 and PCNA323.
CC       {ECO:0000269|PubMed:18782564}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
DR   EMBL; BA000023; BAB65183.1; -; Genomic_DNA.
DR   RefSeq; WP_010978165.1; NC_003106.2.
DR   ProteinModelPortal; Q976G4; -.
DR   SMR; Q976G4; -.
DR   STRING; 273063.ST0223; -.
DR   EnsemblBacteria; BAB65183; BAB65183; STK_02230.
DR   GeneID; 1458113; -.
DR   KEGG; sto:STK_02230; -.
DR   PATRIC; fig|273063.9.peg.271; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; STOK273063:G1G3D-262-MONOMER; -.
DR   BRENDA; 6.5.1.1; 6166.
DR   Proteomes; UP000001015; 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; Reference proteome.
FT   CHAIN         1    600       DNA ligase.
FT                                /FTId=PRO_0000059619.
FT   ACT_SITE    260    260       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     258    258       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     265    265       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     280    280       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     310    310       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     350    350       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     427    427       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     433    433       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   600 AA;  68025 MW;  9D85DA4458000539 CRC64;
     MEFKLIAEYF DKLEKISSRL QLTALLTDLF KKADKNVIDK VVYLIQGKLW PDFLGYPELG
     VGEKLLIKAI SIAVNVKEEV VEEQLKVVGD LGEVAMRLKK TPQSASILSF LGAQSNEGLT
     VEETYESLTK IALASGEGSR DIKIRSLAGL LKKASPLEAK YIVRFVDGRL RVGIGDATIM
     DALSTAFTGS TSFRPLIERA YNLRADLGNI AKIIAQQGVE ALKDIKPQVG IPIRPMLAER
     MSDPAEILAK VGGEALVDYK YDGERAQIHK KDKEVYIFSR RLENITRMYP DVVEYVREYI
     NANEVIIEGE IVAVDPESNE IRPFQELMHR KRKNDINEAI KEYPVNVYLF DLMLYEDADY
     TMKPLPERRK KLEEVIKPND KLHIAHHIYT NNVDKLMEFF YDAISNGAEG VMVKSVAKDS
     IYQAGSRGFL WIKLKRDYQS EMADSVDLVV VGAFYGRGKR GGKLSSLLMA AYDPETDTFK
     TVCKVASGFS DAELDELQKK LMEIKLDKKD PRVDSQLEPD IWVEPKYVAE IIGAEITLSP
     EHTCCKDMVS KGAGLSVRFP RFIRWRDDKS IEDATTPKEI YEMYKMKLRK KEEEQHTDEA
//
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