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Database: UniProt
Entry: G3JHR0_CORMM
LinkDB: G3JHR0_CORMM
Original site: G3JHR0_CORMM 
ID   G3JHR0_CORMM            Unreviewed;      1156 AA.
AC   G3JHR0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=CCM_05923 {ECO:0000313|EMBL:EGX91766.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX91766.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX91766.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX91766.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126402; EGX91766.1; -; Genomic_DNA.
DR   RefSeq; XP_006671130.1; XM_006671067.1.
DR   AlphaFoldDB; G3JHR0; -.
DR   STRING; 983644.G3JHR0; -.
DR   GeneID; 18167941; -.
DR   KEGG; cmt:CCM_05923; -.
DR   VEuPathDB; FungiDB:CCM_05923; -.
DR   eggNOG; KOG1005; Eukaryota.
DR   HOGENOM; CLU_001996_0_1_1; -.
DR   InParanoid; G3JHR0; -.
DR   OMA; FYVTESN; -.
DR   OrthoDB; 55913at2759; -.
DR   Proteomes; UP000001610; 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; 1.10.357.90; -; 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; PF00078; RVT_1; 1.
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 {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:UP000001610};
KW   RNA-directed DNA polymerase {ECO:0000256|RuleBase:RU365061,
KW   ECO:0000313|EMBL:EGX91766.1};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365061};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
FT   DOMAIN          631..994
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..795
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..817
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        818..836
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1156 AA;  131538 MW;  907D29277C7D33D5 CRC64;
     MTKRKRAQKD ASSGKNAKGQ PAPHPLHRDL LNFFYPHCIS LREYALASLP QTSRLRRRKI
     KSLGTIPERF ELEKDLCCLL DSTLVCYHQL TPDVADNRWE QWLSFSQRGE DSSVSLTGGS
     PIYSQSEIVD FVIWLIFSRD NNGFFGPKHL LCDGYRRRAT EKAEPERIPG VFSRYPNDQV
     ASLKAGPWPQ LLNLLGRSGE RIMINMLVDC SIFVAMESGL NNFYQISELE HGLEMKKGPE
     KGICARKLSE ISLVRSRVFY ARPPMTSRGH IEAGYRHIRE YQHLGSWSAH QILTTLDALN
     RYNYIPEHES TESIVTQKNT LNTAKVMMYV FPRQFGLHNV FTSTVDSKTT VQKLQDYTVR
     DDEIAQHMRS DKNFLTQGVP KIPKRLRGAA RDLVRRLQIL HRRCSYIALI RHYCASPLDP
     LRERTQKNNE PTSTSKTAPS QAADGKSSKQ ATPSQTQRRT QDSRVFQLDP SVPIVDLATP
     VSHVSVFLQA VLSKILPGAF LGEGDDLRHN QALLAKKAHH FVTLRRFESM SLHELSQGFK
     ISSLAWLQLP GRGDQKPSQN ETFKQLELFH ELLYYIFDSL LIPLMRNTFY VTESNTHRYQ
     VFYFRHDVWK LVSERALRAM KDGMLEELKV GDVQRAVESR RLGFSQIRLL PKGTTLRPIM
     NLRRRYPLKQ NKKMLGPSIN TVLAPIHNVL KLEKRLNPSK LGATLFSVGD IYNRLKEFRR
     KLPDPLPRLY FVKADVQSAF DTIPQEAVLK LMAAIPSHEH YKIFKHAEVK PGERPPTNTC
     TTAPDGASTS HAQAPSRPIR RWHSTAHPGD ESGRFHQRLD GQSSTSGIAA QQPQRKNTVF
     VNSAVQSDHD TRGLLRLLAE HVADNRIRVG KKTYRQRRGI PQGSVLSSYL CNYFYADLEA
     RHLRFLDDSG SHRSVLLRLV DDFLLVTTDR ARARRFAAVL HRGVPEYGVH VSPHKSLANF
     ALSVPPAGGG DDGPPVPIAT VHSTADFPYC GVRISCRTLE IKKDCQREQQ TDVANTLTVE
     HSRVPGQNFQ RKVLRDAIPS ISPKKNTTWS PVPSFAYRPG AATDAFKIQS HLMFYDTSHN
     SPATVLDTLR AAFRQTALKM WAYMRALHRT ARPRPGLVKL TITRTVEASY LIITSRFRKL
     KYQGYECSVR KTQVTR
//
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