ID   TERT_OXYTR              Reviewed;        1132 AA.
AC   O76332;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Telomerase reverse transcriptase;
DE            EC=2.7.7.49;
DE   AltName: Full=Telomerase catalytic subunit;
DE   AltName: Full=Telomerase subunit P133;
GN   Name=TERT;
OS   Oxytricha trifallax (Sterkiella histriomuscorum).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Sterkiella.
OX   NCBI_TaxID=94289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9671703; DOI=10.1073/pnas.95.15.8479;
RA   Bryan T.M., Sperger J.M., Chapman K.B., Cech T.R.;
RT   "Telomerase reverse transcriptase genes identified in Tetrahymena
RT   thermophila and Oxytricha trifallax.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8479-8484(1998).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere.
CC   -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF060230; AAC39163.1; -; Genomic_DNA.
DR   PIR; T31107; T31107.
DR   AlphaFoldDB; O76332; -.
DR   SMR; O76332; -.
DR   PRIDE; O76332; -.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Chromosome; DNA-binding; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Nucleus; RNA-directed DNA polymerase; Telomere; Transferase.
FT   CHAIN           1..1132
FT                   /note="Telomerase reverse transcriptase"
FT                   /id="PRO_0000054928"
FT   DOMAIN          602..956
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         708
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         886
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         887
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ   SEQUENCE   1132 AA;  134125 MW;  81E145F5F24392DC CRC64;
     MSAKKPVQSK LNIGNPTIPV TSNRSTAPKP VPGQPQFVNQ EKKQQSQNTT TGAFRSNQNN
     ANSGGNGNFE LDDLHLALKS CNEIGSAKTL FCFFMELQKI NDKIPSKKNT ELIKNDPQFQ
     YFCHNTILCT EQSYDEKTIE KLAKLEYKLE YKNSYIDMIS KVIKELLIEN KLNKLQTFGY
     KLVNNEFGNQ NHLGMMQQNQ DSSHNSNFMV KCDYINLNKQ CMITKNWEKV YFYLGDHLFM
     HIYKEYMIFL KTRDESLVQI SGTNIFCYLN EKLGRLQAAF YEGPNKNAAN SAAQGSNPEA
     NDLISAEQRK INTAIVMKKT HKYNIKAADE SYLTNQEKGF WDDQIKRNRL FYCAHQNRFF
     QKHILNSKTL SQQQIRDNIY KEVFGFNRVR AELKGKVMSI IEQVIVNQKK FDFKYYLSKN
     CPLPENWKNL KKSFLEDAAV SGELRGQVFR QLFEYQQDQR QISNFLTEFV ANVFPKNFLE
     GKNKKIFNKK MLQFVKFNRF ESFTKISLLN KFRVNEVSWL SFKCKDENKK FFMNENEHVF
     FKVLKWVFED LAITLMRCYF YSTEKAKEYQ RIFYYRKNIW NMIMRLSIDD LLKQNLKQVE
     KKEMRIFCES QNFAPGKLRL IPKGDTFRPI MTFNRKIPNQ VGKFQSRMTT NNKLQTAHMM
     LKNLKSKMFK HSFGFAVFNY DDIMKRYENF VQKWKQINSP KLYFVAMDIE KCYDNVDCER
     VVNFLQKSDL MDKEYFILNT FVLKRKNNII VERSNFRKLP IKQYFRYKFQ KIGIDGSSYP
     TLFEILEDEF NDLNMKRTII VEQEQRKKFP KNDLLQPVLK ICQNNYVTFN KKQYKQMKGI
     PQGLCVSYIL SSFYYANLEE NALQFLRKES MDPEKPEINL LMRLTDDYLL MTTEKNNAML
     FIEKLYQLSL GNFFKFHMKK LKTNFALNLQ KIGCTNTTQD IDSINDDLFH WIGISIDIKT
     LNIIQNINIK KEGILCTLNV NMQTNESILW LKKKLKSFLM NNISFYFKST INTKQFANIT
     LSKLYIAAAE KYVACCQEFK RFHENTSLGG QNIDIKIIHI IYVVIRSFFK YLVCNVKSPV
     FERDDYQQFF IYSLKFFITR FKQQKNEFAG VYKILKAKEK KLEVAKIEFQ IQ