TERT_YEAST
ID TERT_YEAST Reviewed; 884 AA.
AC Q06163; D6VYW1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Telomerase reverse transcriptase;
DE EC=2.7.7.49;
DE AltName: Full=Telomerase catalytic subunit;
GN Name=EST2; OrderedLocusNames=YLR318W; ORFNames=L8543.12;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 162.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9110970; DOI=10.1126/science.276.5312.561;
RA Lingner J., Hughes T.R., Shevchenko A., Mann M., Lundblad V., Cech T.R.;
RT "Reverse transcriptase motifs in the catalytic subunit of telomerase.";
RL Science 276:561-567(1997).
CC -!- FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the
CC replication of chromosome termini in most eukaryotes. It elongates
CC telomeres. It is a reverse transcriptase that adds simple sequence
CC repeats to chromosome ends by copying a template sequence within the
CC RNA component of the enzyme.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- SUBUNIT: Catalytic subunit of the telomerase holoenzyme complex
CC composed minimally of EST2 and the telomerase RNA template component.
CC {ECO:0000250|UniProtKB:O13339}.
CC -!- INTERACTION:
CC Q06163; P17214: EST1; NbExp=4; IntAct=EBI-3764464, EBI-6684;
CC Q06163; Q03096: EST3; NbExp=3; IntAct=EBI-3764464, EBI-6691;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere.
CC -!- MISCELLANEOUS: Deletion causes telomere shortening and senescence.
CC -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC subfamily. {ECO:0000305}.
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DR EMBL; U20618; AAB64520.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09627.2; -; Genomic_DNA.
DR PIR; S53396; S53396.
DR RefSeq; NP_013422.2; NM_001182207.2.
DR AlphaFoldDB; Q06163; -.
DR SMR; Q06163; -.
DR BioGRID; 31582; 81.
DR ComplexPortal; CPX-3298; Telomerase holoenzyme complex.
DR DIP; DIP-7548N; -.
DR IntAct; Q06163; 7.
DR MINT; Q06163; -.
DR STRING; 4932.YLR318W; -.
DR CarbonylDB; Q06163; -.
DR iPTMnet; Q06163; -.
DR PaxDb; Q06163; -.
DR PRIDE; Q06163; -.
DR EnsemblFungi; YLR318W_mRNA; YLR318W; YLR318W.
DR GeneID; 851028; -.
DR KEGG; sce:YLR318W; -.
DR SGD; S000004310; EST2.
DR VEuPathDB; FungiDB:YLR318W; -.
DR eggNOG; KOG1005; Eukaryota.
DR GeneTree; ENSGT00390000018531; -.
DR HOGENOM; CLU_012565_0_0_1; -.
DR InParanoid; Q06163; -.
DR OMA; CRNHNSY; -.
DR BioCyc; YEAST:G3O-32402-MON; -.
DR PRO; PR:Q06163; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06163; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000333; C:telomerase catalytic core complex; IDA:SGD.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IMP:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:SGD.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR021891; Telomerase_RBD.
DR InterPro; IPR003545; Telomerase_RT.
DR PANTHER; PTHR12066; PTHR12066; 2.
DR Pfam; PF12009; Telomerase_RBD; 1.
DR PRINTS; PR01365; TELOMERASERT.
DR SMART; SM00975; Telomerase_RBD; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Reference proteome; RNA-directed DNA polymerase; Telomere;
KW Transferase.
FT CHAIN 1..884
FT /note="Telomerase reverse transcriptase"
FT /id="PRO_0000054932"
FT DOMAIN 422..725
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 670
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 671
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT CONFLICT 162
FT /note="A -> V (in Ref. 1; AAB64520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 884 AA; 102635 MW; 84540735E3CD40F5 CRC64;
MKILFEFIQD KLDIDLQTNS TYKENLKCGH FNGLDEILTT CFALPNSRKI ALPCLPGDLS
HKAVIDHCII YLLTGELYNN VLTFGYKIAR NEDVNNSLFC HSANVNVTLL KGAAWKMFHS
LVGTYAFVDL LINYTVIQFN GQFFTQIVGN RCNEPHLPPK WAQRSSSSSA TAAQIKQLTE
PVTNKQFLHK LNINSSSFFP YSKILPSSSS IKKLTDLREA IFPTNLVKIP QRLKVRINLT
LQKLLKRHKR LNYVSILNSI CPPLEGTVLD LSHLSRQSPK ERVLKFIIVI LQKLLPQEMF
GSKKNKGKII KNLNLLLSLP LNGYLPFDSL LKKLRLKDFR WLFISDIWFT KHNFENLNQL
AICFISWLFR QLIPKIIQTF FYCTEISSTV TIVYFRHDTW NKLITPFIVE YFKTYLVENN
VCRNHNSYTL SNFNHSKMRI IPKKSNNEFR IIAIPCRGAD EEEFTIYKEN HKNAIQPTQK
ILEYLRNKRP TSFTKIYSPT QIADRIKEFK QRLLKKFNNV LPELYFMKFD VKSCYDSIPR
MECMRILKDA LKNENGFFVR SQYFFNTNTG VLKLFNVVNA SRVPKPYELY IDNVRTVHLS
NQDVINVVEM EIFKTALWVE DKCYIREDGL FQGSSLSAPI VDLVYDDLLE FYSEFKASPS
QDTLILKLAD DFLIISTDQQ QVINIKKLAM GGFQKYNAKA NRDKILAVSS QSDDDTVIQF
CAMHIFVKEL EVWKHSSTMN NFHIRSKSSK GIFRSLIALF NTRISYKTID TNLNSTNTVL
MQIDHVVKNI SECYKSAFKD LSINVTQNMQ FHSFLQRIIE MTVSGCPITK CDPLIEYEVR
FTILNGFLES LSSNTSKFKD NIILLRKEIQ HLQAYIYIYI HIVN
