GenomeNet

Database: UniProt/SWISS-PROT
Entry: DNLI_THEVO
LinkDB: DNLI_THEVO
Original site: DNLI_THEVO 
ID   DNLI_THEVO              Reviewed;         588 AA.
AC   Q979A1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   05-DEC-2018, entry version 105.
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=TV1261;
GN   ORFNames=TVG1298537;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Euryarchaeota; Diaforarchaea group; Thermoplasmata;
OC   Thermoplasmatales; Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S.,
RA   Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T.,
RA   Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic
RT   sequence of Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB60403.1; -; Genomic_DNA.
DR   RefSeq; WP_010917495.1; NC_002689.2.
DR   ProteinModelPortal; Q979A1; -.
DR   SMR; Q979A1; -.
DR   STRING; 273116.TVN1237; -.
DR   EnsemblBacteria; BAB60403; BAB60403; BAB60403.
DR   GeneID; 1441377; -.
DR   KEGG; tvo:TVG1298537; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; TVOL273116:G1G3C-1346-MONOMER; -.
DR   Proteomes; UP000001017; 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; 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    588       DNA ligase.
FT                                /FTId=PRO_0000059622.
FT   ACT_SITE    250    250       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     248    248       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     255    255       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     270    270       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     300    300       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     341    341       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     418    418       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     424    424       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   588 AA;  66218 MW;  7FC5FC2549F3CD3D CRC64;
     MKFSLVTDAF EKMSKTTKRT ELTEILVELL KSADEDLQSL VYLIEGKLAP DYQGIETQMS
     DKLIIKALSI VSNIPEEAVS ETYSKLGDIG SVAREIAAKK NMRSLVNEDL TVKYVHDTLM
     RMAKTSGSGS TKARIDAYVD LALSGTPADL MYITRIITGK LRIGVSDATI LDAIILAFSD
     EKYSEEIENA YNFHPDLGYI AVQLRLGNLE SVINMGPTPM VPFKVMLAER LRSVDEIVQK
     MNGKCAFEYK YDGMRTEIHI VDEKVRLFSR GNEETTGQFP DIVKSAKETF HVSSVILDGE
     AVPYNPETGE LYPFQVISQR RGRKYDLDKV SNEIPITVFL FDIVYINGKD LSKTPYAERR
     RILEGLFKEN DNFKLAKRIV SSDTGTITKF FNQAIEDGCE GLVAKSMADD SYYKAGARGW
     LWIKLKRDYQ AQLWDTIDLT VVGAFMGHGR RSGTYGALLL ATYNEKNDTF ETVCKLGSGF
     TDDVLFSLPK RFAEFVSKEK PARVVSTIEP DVWIYPSIVM EIIGAEITIS PVHTCAFGII
     EKDAGLSIRF PRFTGKWRDD KKPEDSTTTQ EIIEMYKEQK KTLTEEKS
//
DBGET integrated database retrieval system