TERT_SCHPO
ID TERT_SCHPO Reviewed; 988 AA.
AC O13339; O13338;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Telomerase reverse transcriptase {ECO:0000312|PomBase:SPBC29A3.14c};
DE EC=2.7.7.49 {ECO:0000269|PubMed:24793650};
DE AltName: Full=Telomerase catalytic subunit {ECO:0000303|PubMed:9252327};
GN Name=trt1 {ECO:0000312|PomBase:SPBC29A3.14c};
GN ORFNames=SPBC29A3.14c {ECO:0000312|PomBase:SPBC29A3.14c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9252327; DOI=10.1126/science.277.5328.955;
RA Nakamura T.M., Morin G.B., Chapman K.B., Weinrich S.L., Andrews W.H.,
RA Lingner J., Harley C.B., Cech T.R.;
RT "Telomerase catalytic subunit homologs from fission yeast and human.";
RL Science 277:955-959(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP INTERACTION WITH EST1, AND SUBCELLULAR LOCATION.
RX PubMed=12676088; DOI=10.1016/s0960-9822(03)00169-6;
RA Beernink H.T.H., Miller K., Deshpande A., Bucher P., Cooper J.P.;
RT "Telomere maintenance in fission yeast requires an Est1 ortholog.";
RL Curr. Biol. 13:575-580(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND RECONSTITUTION OF THE TELOMERASE
RP HOLOENZYME COMPLEX.
RX PubMed=24793650; DOI=10.1038/nsmb.2819;
RA Huang J., Brown A.F., Wu J., Xue J., Bley C.J., Rand D.P., Wu L., Zhang R.,
RA Chen J.J., Lei M.;
RT "Structural basis for protein-RNA recognition in telomerase.";
RL Nat. Struct. Mol. Biol. 21:507-512(2014).
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. {ECO:0000269|PubMed:24793650,
CC ECO:0000269|PubMed:9252327}.
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, ECO:0000269|PubMed:24793650};
CC -!- SUBUNIT: Catalytic subunit of the telomerase holoenzyme complex
CC composed minimally of trt1 and the telomerase RNA template component
CC (PubMed:24793650). Interacts with est1 (PubMed:12676088).
CC {ECO:0000269|PubMed:12676088, ECO:0000269|PubMed:24793650}.
CC -!- INTERACTION:
CC O13339; O74804: est1; NbExp=3; IntAct=EBI-1556874, EBI-1556899;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O13339-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O13339-2; Sequence=VSP_006395;
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; AF015783; AAC49802.1; -; Genomic_DNA.
DR EMBL; AF015783; AAC49803.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA18391.1; -; Genomic_DNA.
DR PIR; T03838; T03838.
DR RefSeq; NP_595842.1; NM_001021746.2.
DR AlphaFoldDB; O13339; -.
DR SMR; O13339; -.
DR BioGRID; 277127; 77.
DR DIP; DIP-38463N; -.
DR IntAct; O13339; 1.
DR STRING; 4896.SPBC29A3.14c.1; -.
DR PaxDb; O13339; -.
DR PRIDE; O13339; -.
DR EnsemblFungi; SPBC29A3.14c.1; SPBC29A3.14c.1:pep; SPBC29A3.14c. [O13339-1]
DR GeneID; 2540601; -.
DR KEGG; spo:SPBC29A3.14c; -.
DR PomBase; SPBC29A3.14c; trt1.
DR VEuPathDB; FungiDB:SPBC29A3.14c; -.
DR eggNOG; KOG1005; Eukaryota.
DR HOGENOM; CLU_001996_0_0_1; -.
DR InParanoid; O13339; -.
DR OMA; FYVTESN; -.
DR PhylomeDB; O13339; -.
DR PRO; PR:O13339; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000333; C:telomerase catalytic core complex; IDA:UniProtKB.
DR GO; GO:0000782; C:telomere cap complex; IDA:PomBase.
DR GO; GO:0008047; F:enzyme activator activity; EXP:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IPI:PomBase.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:PomBase.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IDA:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:PomBase.
DR GO; GO:0022616; P:DNA strand elongation; IDA:UniProtKB.
DR GO; GO:0032208; P:negative regulation of telomere maintenance via recombination; IGI:PomBase.
DR GO; GO:1904868; P:telomerase catalytic core complex assembly; EXP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:PomBase.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR021891; Telomerase_RBD.
DR InterPro; IPR003545; Telomerase_RT.
DR PANTHER; PTHR12066; PTHR12066; 2.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF12009; Telomerase_RBD; 1.
DR PRINTS; PR01365; TELOMERASERT.
DR SMART; SM00975; Telomerase_RBD; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA-binding; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome;
KW RNA-directed DNA polymerase; Telomere; Transferase.
FT CHAIN 1..988
FT /note="Telomerase reverse transcriptase"
FT /id="PRO_0000054931"
FT DOMAIN 486..807
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 590
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 742
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 743
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT VAR_SEQ 524
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006395"
SQ SEQUENCE 988 AA; 116329 MW; AB2DC7030228F443 CRC64;
MTEHHTPKSR ILRFLENQYV YLCTLNDYVQ LVLRGSPASS YSNICERLRS DVQTSFSIFL
HSTVVGFDSK PDEGVQFSSP KCSQSELIAN VVKQMFDESF ERRRNLLMKG FSMNHEDFRA
MHVNGVQNDL VSTFPNYLIS ILESKNWQLL LEIIGSDAMH YLLSKGSIFE ALPNDNYLQI
SGIPLFKNNV FEETVSKKRK RTIETSITQN KSARKEVSWN SISISRFSIF YRSSYKKFKQ
DLYFNLHSIC DRNTVHMWLQ WIFPRQFGLI NAFQVKQLHK VIPLVSQSTV VPKRLLKVYP
LIEQTAKRLH RISLSKVYNH YCPYIDTHDD EKILSYSLKP NQVFAFLRSI LVRVFPKLIW
GNQRIFEIIL KDLETFLKLS RYESFSLHYL MSNIKISEIE WLVLGKRSNA KMCLSDFEKR
KQIFAEFIYW LYNSFIIPIL QSFFYITESS DLRNRTVYFR KDIWKLLCRP FITSMKMEAF
EKINENNVRM DTQKTTLPPA VIRLLPKKNT FRLITNLRKR FLIKMGSNKK MLVSTNQTLR
PVASILKHLI NEESSGIPFN LEVYMKLLTF KKDLLKHRMF GRKKYFVRID IKSCYDRIKQ
DLMFRIVKKK LKDPEFVIRK YATIHATSDR ATKNFVSEAF SYFDMVPFEK VVQLLSMKTS
DTLFVDFVDY WTKSSSEIFK MLKEHLSGHI VKIGNSQYLQ KVGIPQGSIL SSFLCHFYME
DLIDEYLSFT KKKGSVLLRV VDDFLFITVN KKDAKKFLNL SLRGFEKHNF STSLEKTVIN
FENSNGIINN TFFNESKKRM PFFGFSVNMR SLDTLLACPK IDEALFNSTS VELTKHMGKS
FFYKILRSSL ASFAQVFIDI THNSKFNSCC NIYRLGYSMC MRAQAYLKRM KDIFIPQRMF
ITDLLNVIGR KIWKKLAEIL GYTSRRFLSS AEVKWLFCLG MRDGLKPSFK YHPCFEQLIY
QFQSLTDLIK PLRPVLRQVL FLHRRIAD
