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Database: UniProt/TrEMBL
Entry: G2RBC7_THITE
LinkDB: G2RBC7_THITE
Original site: G2RBC7_THITE 
ID   G2RBC7_THITE            Unreviewed;      1040 AA.
AC   G2RBC7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   07-JUN-2017, entry version 32.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=THITE_2080045 {ECO:0000313|EMBL:AEO69098.1};
OS   Thielavia terrestris (strain ATCC 38088 / NRRL 8126) (Acremonium
OS   alabamense).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Thielavia.
OX   NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO69098.1, ECO:0000313|Proteomes:UP000008181};
RN   [1] {ECO:0000313|EMBL:AEO69098.1, ECO:0000313|Proteomes:UP000008181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J.,
RA   Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B.,
RA   Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J.,
RA   Lucas S., Harris P., Powlowski J., Bellemare A., Taylor D., Butler G.,
RA   de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R.,
RA   Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J.,
RA   LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M.,
RA   de Leon A.L., Rey M.W., Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading
RT   fungi Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP003012; AEO69098.1; -; Genomic_DNA.
DR   RefSeq; XP_003655434.1; XM_003655386.1.
DR   STRING; 578455.XP_003655434.1; -.
DR   EnsemblFungi; AEO69098; AEO69098; THITE_2080045.
DR   GeneID; 11520347; -.
DR   KEGG; ttt:THITE_2080045; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000008181; Chromosome 4.
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: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   CDD; cd00027; BRCT; 1.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 1.
DR   Pfam; PF16589; BRCT_2; 1.
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   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
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 {ECO:0000256|RuleBase:RU000617};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008181};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008181}.
FT   DOMAIN      464    587       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      770    853       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      934   1039       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   1040 AA;  116374 MW;  F35809FF60A6B6F0 CRC64;
     MSSRTKRAKS PDVDAIEEDE KQYGSGPLTL EELDEQFPNR PRNHSKTPPF SDLFQSLFNP
     LIDCKPSTAG AASAPARARA RARAGPSFSS SSSSTKLSYH EQRRHIIERF MARWRADVGP
     DFYPAMRLIL PDKDRDRGVY GLKENTIGKL LVKVMKIDRN SEDGYALMHW KLPGHAGGGG
     GRFGGGAGGG GGGGSRGSAG DFAGRCFEIV SKRQMRTEPG NFTIGEVNVM LDRLAGASGE
     AEQLPIFEEF YQGMNAEELM WLVRIILKDM KVGATERTFL GLWHPDAEAL FSVSSSLRRV
     CWELYDPEFR LEQQETGVTL MSCFQPQLAQ FQMTTTFAKL VANLGVTEEN PEFWIEEKLD
     GERMQMHMQE DDSVPGGYRF AFWSRKAKDY TYLYGSGLED DNSALTRHLK NAFHSGVRNL
     ILDGEMITWD PEVDKIVPFG TLKTAALEQQ KNPFQNGPRP LYRVFDILLL NDKSLTEYTL
     ADRHRALERA VKGEPRRLEI HPYETATSAD AIEPLLRKVV AEASEGLVLK NPRSRYQLNS
     RNNDWIKVKP EYMSEFGESL DCVVIGGYYG SGRRGGTLSS FLCGVRVSEN FVKSGAAASR
     EKCLSFCKVG GGFKAEDYGE IRHHTEGKWR DWDAANPPSE FIELGGGERL QYERPDVWIR
     PSESVVLSVK AASFAPSDQF ATGWTLRFPR FRKLRLDKAW DAAMDVDECE ALRTKVKQEE
     KERKAMEMES RKRRPTKRQK RELVIAGAAD PAATAATATA TAEFLDVKTP RSELFRGLDF
     CVLSEMLRPR KMTKPELEKL LKENGGRIHQ TVDKGSGMIL LADKNVVKVA SLKKAGDADI
     VRPKWVLDCL EQGGGEGYLL PFEEGHLLFA TEEMRRVAEE NTDQYGDSYA RDVGIDELRA
     ILDAMDMPDG GGAEFDVSQF LDQLEEHGNG LEDLKSFMFR RCRMYFALGD GVPETTALRL
     GNYVKFGSGE VADGVEDEKI THVVVVGGEQ DTAASEKVLA ADVRYRVSSR RAVPRIVSSR
     WVEDCWKEGT LVDEEAYAPN
//
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