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Database: UniProt
Entry: C5MCQ7_CANTT
LinkDB: C5MCQ7_CANTT
Original site: C5MCQ7_CANTT 
ID   C5MCQ7_CANTT            Unreviewed;       879 AA.
AC   C5MCQ7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Telomerase reverse transcriptase {ECO:0000256|ARBA:ARBA00016182, ECO:0000256|RuleBase:RU365061};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493, ECO:0000256|RuleBase:RU365061};
DE   AltName: Full=Telomerase catalytic subunit {ECO:0000256|RuleBase:RU365061};
GN   ORFNames=CTRG_04008 {ECO:0000313|EMBL:EER32337.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER32337.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER32337.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0007829|PDB:6ZD1, ECO:0007829|PDB:6ZD2}
RP   X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 177-879.
RX   PubMed=33856462; DOI=10.1093/nar/gkab261;
RA   Zhai L.T., Rety S., Chen W.F., Song Z.Y., Auguin D., Sun B., Dou S.X.,
RA   Xi X.G.;
RT   "Crystal structures of N-terminally truncated telomerase reverse
RT   transcriptase from fungi.";
RL   Nucleic Acids Res. 49:4768-4781(2021).
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:0000256|RuleBase:RU365061}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00024557,
CC         ECO:0000256|RuleBase:RU365061};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365061}.
CC       Chromosome, telomere {ECO:0000256|RuleBase:RU365061}.
CC   -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC       subfamily. {ECO:0000256|ARBA:ARBA00008001,
CC       ECO:0000256|RuleBase:RU365061}.
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DR   EMBL; GG692399; EER32337.1; -; Genomic_DNA.
DR   RefSeq; XP_002549711.1; XM_002549665.1.
DR   PDB; 6ZD1; X-ray; 2.47 A; A=177-879.
DR   PDB; 6ZD2; X-ray; 2.84 A; A=158-745.
DR   PDB; 6ZD6; X-ray; 2.64 A; A=177-879.
DR   PDB; 6ZDP; X-ray; 2.85 A; A=158-879.
DR   AlphaFoldDB; C5MCQ7; -.
DR   SMR; C5MCQ7; -.
DR   STRING; 294747.C5MCQ7; -.
DR   EnsemblFungi; CTRG_04008-t43_1; CTRG_04008-t43_1-p1; CTRG_04008.
DR   GeneID; 8296986; -.
DR   KEGG; ctp:CTRG_04008; -.
DR   VEuPathDB; FungiDB:CTRG_04008; -.
DR   eggNOG; KOG1005; Eukaryota.
DR   HOGENOM; CLU_012565_0_0_1; -.
DR   OrthoDB; 55913at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IEA:InterPro.
DR   CDD; cd01648; TERT; 1.
DR   Gene3D; 1.10.132.70; -; 1.
DR   Gene3D; 3.30.70.2630; -; 1.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR021891; Telomerase_RBD.
DR   InterPro; IPR003545; Telomerase_RT.
DR   PANTHER; PTHR12066; TELOMERASE REVERSE TRANSCRIPTASE; 1.
DR   PANTHER; PTHR12066:SF0; TELOMERASE REVERSE TRANSCRIPTASE; 1.
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   3D-structure {ECO:0007829|PDB:6ZD1, ECO:0007829|PDB:6ZD2};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU365061};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU365061};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365061};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU365061};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365061};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   RNA-directed DNA polymerase {ECO:0000256|RuleBase:RU365061};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365061};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
FT   DOMAIN          394..734
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
SQ   SEQUENCE   879 AA;  101660 MW;  BB9505D19FD2FB2B CRC64;
     MQTISLLQYV KDNSSDQSVQ LPSFINYLKS VNLIEITKPN KLPRITSDTS YQDFINNLIT
     ELVLRKSQNV LVSGYKSTIE DSKVALPCVN LDGNFLPTNL NDSNWHRVFT LLGSEKFLNL
     LINHKGFLKH KNGQQIQIFG DITSYAKPAA KAVLPIPKWI YKFDVLYQSR NPRYRNYEII
     RTNVQEVLAE IVSPSTKNPN SENPAVKKRF RGIKNVVSRI ISNDKKCRYD LIYNKYLSSS
     DTRKLKTMID YSTKFNRVVE VVLIIMGKLL PLDAWGGTEN KKVIQDRIVD FLRLGANERL
     HLDDVLSGIK LSKFKWLGVG NNISSQQDFQ IRKRLLEGYI NWVFISLVKN IVRAFWYVTE
     SSNMDRSKLF YFTHSIWNEL SSNWITKYAK GNLVQVVSPE SKGQFTNGKI KLIPKRGGFR
     VICVPLKQSL YSFNNKRNFA LKQKEKWDYI FYQKYTLSPV RQVLQLKLNA LRKSDMGHRS
     SVNSTNEVAD RILTFRNDLL KKNKTLPVLY MIKFDMKECY DRLNQNALKE SIAGIFKEDN
     ENTTYHVREY GTLDEFLKLK RVRTLIETEV QNFNIIMNSK DEAEAGSRSY GTKVDKVKTL
     SISKNKIIEV CHSQIEDATC LVKNKEGQYD LFKRKQGVFQ GFSLSGIFCD ILYSTMVSKE
     FKFLWEATED NLLLRLVDDF IFITSNKDTL KKVKDKISSN ELQKYGAFVN HEKTVEINGE
     AGSSNKMTFV GLDINCLTLD VKKDSSQFSR PTCKFRSFKA LFSNLKQFYC SNLSEFLLDF
     SSNSLETIRE NVDAILKLTF EAIQTSFATI SKQDSFERYR FMKFLHVIIE TTIEKFARVN
     GSMEGVEYLL TCIKITITKS LAFMATKQEI IEWLYTLTI
//
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