GenomeNet

Database: UniProt
Entry: Q9HJ26
LinkDB: Q9HJ26
Original site: Q9HJ26 
ID   DNLI_THEAC              Reviewed;         588 AA.
AC   Q9HJ26;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   07-JUN-2017, entry version 96.
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=Ta1148;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 /
OS   NBRC 15155 / AMRC-C165).
OC   Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(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: 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; AL445066; CAC12273.1; -; Genomic_DNA.
DR   RefSeq; WP_010901556.1; NC_002578.1.
DR   ProteinModelPortal; Q9HJ26; -.
DR   SMR; Q9HJ26; -.
DR   STRING; 273075.Ta1148; -.
DR   PRIDE; Q9HJ26; -.
DR   EnsemblBacteria; CAC12273; CAC12273; CAC12273.
DR   GeneID; 1456651; -.
DR   KEGG; tac:Ta1148; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001024; 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; 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_0000059620.
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;  66538 MW;  FFD61667871BE291 CRC64;
     MLFSVVADAF EKMESTTKRL ELTDLLVNLL KEADDDLPLL IYLLEGKLGP DYLGIETQMS
     DKLIIKALSV ASNISEDEIA KEYAKAGDIG TIAKEIAEKR SLRSLVQEEM TVKYIHDTLM
     KMARTTGSGS TKARVDAYMD LFLNSTPKEI MYITRIITGK LRIGISDATI LDAIVKAFAD
     EKYSEDIENA FNFHPDLGYI ASELRKGNID AILKLGPTPM IPFKVMLAER LRSVEEILEK
     MGGRCAFEYK YDGMRTETHI ERGKVRLFSR GNEETTNQFP DITKAASETF KVDSAILDGE
     AVPYDPDTGE LYPFQVISHR RGRKYDLDKV SSEIPITVFL FDIVYLNGRD LSKTPYTERR
     KILESIFTES DSFRLAKRIE SGDPAEVHRF FNSAIEDGCE GLVAKSTSPD SFYKAGARGW
     LWIKLKRDYQ AQLWDTLDLT VVGAFYGHGR RKGTYGALLL ATYNDKNDTF ETVCKLGSGF
     SDDVLFSLPK KFEQYVSKEK PARVISNLEP DVWFYPAVVM EVIGAEITVS PIHTCAYGEI
     EKDSGLSVRF PRFTGKWRED KKPEDSTTSR EILEMYKEQK KTITEEKS
//
DBGET integrated database retrieval system