ID   TERT_EUPAE              Reviewed;        1031 AA.
AC   O00939;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Telomerase reverse transcriptase;
DE            EC=2.7.7.49;
DE   AltName: Full=Telomerase catalytic subunit;
DE   AltName: Full=Telomerase subunit P123;
OS   Euplotes aediculatus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX   NCBI_TaxID=5940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN   [2]
RP   FUNCTION, AND IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
RX   PubMed=11080168; DOI=10.1093/emboj/19.22.6230;
RA   Aigner S., Lingner J., Goodrich K.J., Grosshans C.A., Shevchenko A.,
RA   Mann M., Cech T.R.;
RT   "Euplotes telomerase contains an La motif protein produced by apparent
RT   translational frameshifting.";
RL   EMBO J. 19:6230-6239(2000).
RN   [3]
RP   FUNCTION, AND IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
RX   PubMed=12665556; DOI=10.1242/jcs.00351;
RA   Moellenbeck M., Postberg J., Paeschke K., Rossbach M., Joensson F.,
RA   Lipps H.J.;
RT   "The telomerase-associated protein p43 is involved in anchoring telomerase
RT   in the nucleus.";
RL   J. Cell Sci. 116:1757-1761(2003).
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:0000305|PubMed:11080168,
CC       ECO:0000305|PubMed:12665556}.
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: Component of the telomerase holoenzyme complex composed
CC       minimally of the catalytic subunit p123 and the telomerase RNA template
CC       component. {ECO:0000269|PubMed:11080168, ECO:0000269|PubMed:12665556}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U95964; AAC47515.1; -; Genomic_DNA.
DR   AlphaFoldDB; O00939; -.
DR   SMR; O00939; -.
DR   PRIDE; O00939; -.
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; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR021891; Telomerase_RBD.
DR   InterPro; IPR003545; Telomerase_RT.
DR   PANTHER; PTHR12066; PTHR12066; 1.
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   Chromosome; DNA-binding; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Nucleus; RNA-directed DNA polymerase; Telomere; Transferase.
FT   CHAIN           1..1031
FT                   /note="Telomerase reverse transcriptase"
FT                   /id="PRO_0000054927"
FT   DOMAIN          498..852
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         603
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         781
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         782
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ   SEQUENCE   1031 AA;  122563 MW;  57B87A63A1FED60F CRC64;
     MEVDVDNQAD NHGIHSALKT CEEIKEAKTL YSWIQKVIRC RNQSQSHYKD LEDIKIFAQT
     NIVATPRDYN EEDFKVIARK EVFSTGLMIE LIDKCLVELL SSSDVSDRQK LQCFGFQLKG
     NQLAKTHLLT ALSTQKQYFF QDEWNQVRAM IGNELFRHLY TKYLIFQRTS EGTLVQFCGN
     NVFDHLKVND KFDKKQKGGA ADMNEPRCCS TCKYNVKNEK DHFLNNINVP NWNNMKSRTR
     IFYCTHFNRN NQFFKKHEFV SNKNNISAMD RAQTIFTNIF RFNRIRKKLK DKVIEKIAYM
     LEKVKDFNFN YYLTKSCPLP ENWRERKQKI ENLINKTREE KSKYYEELFS YTTDNKCVTQ
     FINEFFYNIL PKDFLTGRNR KNFQKKVKKY VELNKHELIH KNLLLEKINT REISWMQVET
     SAKHFYYFDH ENIYVLWKLL RWIFEDLVVS LIRCFFYVTE QQKSYSKTYY YRKNIWDVIM
     KMSIADLKKE TLAEVQEKEV EEWKKSLGFA PGKLRLIPKK TTFRPIMTFN KKIVNSDRKT
     TKLTTNTKLL NSHLMLKTLK NRMFKDPFGF AVFNYDDVMK KYEEFVCKWK QVGQPKLFFA
     TMDIEKCYDS VNREKLSTFL KTTKLLSSDF WIMTAQILKR KNNIVIDSKN FRKKEMKDYF
     RQKFQKIALE GGQYPTLFSV LENEQNDLNA KKTLIVEAKQ RNYFKKDNLL QPVINICQYN
     YINFNGKFYK QTKGIPQGLC VSSILSSFYY ATLEESSLGF LRDESMNPEN PNVNLLMRLT
     DDYLLITTQE NNAVLFIEKL INVSRENGFK FNMKKLQTSF PLSPSKFAKY GMDSVEEQNI
     VQDYCDWIGI SIDMKTLALM PNINLRIEGI LCTLNLNMQT KKASMWLKKK LKSFLMNNIT
     HYFRKTITTE DFANKTLNKL FISGGYKYMQ CAKEYKDHFK KNLAMSSMID LEVSKIIYSV
     TRAFFKYLVC NIKDTIFGEE HYPDFFLSTL KHFIEIFSTK KYIFNRVCMI LKAKEAKLKS
     DQCQSLIQYD A