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Database: UniProt
Entry: F0XKQ7_GROCL
LinkDB: F0XKQ7_GROCL
Original site: F0XKQ7_GROCL 
ID   F0XKQ7_GROCL            Unreviewed;      1100 AA.
AC   F0XKQ7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=CMQ_8096 {ECO:0000313|EMBL:EFX01630.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX01630.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(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; GL629788; EFX01630.1; -; Genomic_DNA.
DR   RefSeq; XP_014171112.1; XM_014315637.1.
DR   AlphaFoldDB; F0XKQ7; -.
DR   STRING; 655863.F0XKQ7; -.
DR   GeneID; 25981713; -.
DR   eggNOG; KOG1005; Eukaryota.
DR   HOGENOM; CLU_001996_0_1_1; -.
DR   InParanoid; F0XKQ7; -.
DR   OrthoDB; 55913at2759; -.
DR   Proteomes; UP000007796; 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   Gene3D; 3.30.70.2630; -; 1.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR021891; Telomerase_RBD.
DR   InterPro; IPR003545; Telomerase_RT.
DR   InterPro; IPR049139; TERT_C.
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   Pfam; PF21399; TERT_C; 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:UP000007796};
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          581..928
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1100 AA;  124623 MW;  898406092588EB8A CRC64;
     MVDQADMSAL IRRKRKRADA DDSRNIGEAP PSRTKQPRRE ASSEQHPAAH RQLDPVVKHA
     LLTRCFPQVL TLRAYLLSRL PASSRIRRKK LREVGLAADP SPVEQRLRRL LDNALVACSH
     HDGSGQGDKP LDSLPSLQDD RQQQRLAYIE HKRAEESHVI ISNAQEGVFS PQSEPLCNLE
     PLTKFQATEQ TARDTRDEKS LSDISFVRNR MFYAKPSMAQ SGAVHFGLKH IHVLNRFSYR
     SCPTKKVGLQ ELAAANNHGT VHMMMYMFPR QFGLHNVFTS VVDRATTAQR FQDYTLREAE
     ISAKFGKIGW KDRSASVRIP KRLRGMAVHL VERLRKLHNR CSYYELLQHY CPDIAYQETR
     HEVTSAEPGS HKEEAHTLVS LGHPNQESAS KDVATTGQDP APQRQQCVPY SSKSGPELKS
     TTPLVELATP LQRVSTFCQA VILNVVPNDF WGNGEAQAKN RQAVLKKVDL FLRLRRFETL
     NLHDLMQGIK ISDILWLAPP GLRKGKISQT DVQKRRQIFA EFLYYLFDSF LIPLVRSNFY
     VTESSSHRNK LFFFRHDVWR RITEPALVGL KARMFEDIKH GEALQILGSR DLGYGQIRLL
     PKQATVRPIM NLRRRTAVKG GTRLGSSANT ILAPVQAMLK FEILMFSLLK KQHPERLGSG
     MFSVGTLFKK LKEFKKRMAS ESQHTFYLAK VDVKSAFDTM PQEAVVELVH KLSSHRAYYM
     DKHVEMAAPE NRGLGGVFNA AVKGDFVPMR RWKTIASAST DASGFHDVVE SSLATYQRNA
     IFADTAYRKP RDSASLVGLA ASHILQNLVK IGKKFYRQKT GIPQGSVLSA LLCNCFYAEL
     EAEELGFLDA DGSKGCLLLR LIDDFLLITT DQSKAARFVE VMHRGLPQYG VAVSSDKSLV
     NFDLQGPDGK SVSRVANGAW FPYCGLVVNC LTLDIAKDWE TKKQEHARSP GHNFKRKIFN
     GFKVLSHVMF FDTAHNSLRT TLCNAHKVFS DTAVKVWAYT RCLPRDKRPS TRLVISTIEE
     LSELAYTVLN GRARRMPEYQ FSVFKPQLRW LLLHAFSGVL GKKQAGYSDV LTWIRSEMHY
     LRSQQDLRLP KIFIETSVQA
//
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