ID F6HBF5_VITVI Unreviewed; 895 AA.
AC F6HBF5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 OrderedLocusNames=VIT_13s0064g00980 {ECO:0000313|EMBL:CCB49507.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB49507.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN595509; CCB49507.1; -; Genomic_DNA.
DR AlphaFoldDB; F6HBF5; -.
DR STRING; 29760.F6HBF5; -.
DR PaxDb; 29760-VIT_13s0064g00980-t01; -.
DR eggNOG; KOG1005; Eukaryota.
DR HOGENOM; CLU_001996_0_1_1; -.
DR InParanoid; F6HBF5; -.
DR Proteomes; UP000009183; Chromosome 13.
DR ExpressionAtlas; F6HBF5; baseline.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000333; C:telomerase catalytic core complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
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 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:UP000009183};
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 317..701
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
SQ SEQUENCE 895 AA; 103367 MW; 5D0B821A4B2807FB CRC64;
MGEEGGWTPR FLRPFNDWEV EEVERFLSTI QGKRLNADVE DRMVWKETKN EIFTVKSLYN
SLDHSCAVPF PWSIIWSPYV PTKVGFFCLG SFMGEGSYLR STQKEGYHSL VSLLTLLIRK
TQSCRHLRLL DKHCAIPSLG RNANENALFM SEVSKSHVHE SKHLKKTLNV LSHQFELNRS
YCSKSQVISF ISAVCKRIVP SRLLGTPSNW RILRKKISKF VWLRRFEKLS LKQCMHKLKI
SRFPLLSNKH SSCHLKRWIF WFFSSLVVPL VQANFYVTES EHGKNDLFYY QKSVWEKLTN
SATTCLKEQS YRSLDDVSVG QILSDRSFGF SRLRFRPKEN GVRALANLNG SSKFRVQDSP
LKDQSLGMQR KAQLHLERVK FDHFKSVNFV LRDLHAVLKG LQMKEPERLG SSIFDYNDVY
RKLCPFLISV KNGSTTMPSV FIVVSDVSKA FDSVNQDKLL KVMKDVIVKG KYLLKQSCQV
VCTRKALWAY ENQILVDQNI GTGLTEFTSS VLSHSLHSVL VNQVRRRTIG SKELYFNLNE
HVKRNVLQLG NKFYLQNSGI PQGSVLSSLL CSFYYGHMDR NVIFPFLEKT CGPATDYVSG
KDNCQDVSDA PSSSENNVIT SSPKYMLLRF IDDFLFLSTS KQQAASFFSR LQRGFRDYNC
YMNEGKFGMN FDIGHISRLS SNRIYVGEDG ISFLRWSGLL INCCSLEVQA DYTRYANSHL
SSTLTVCWQG RPGRQLKARL FNYMQLRCHP LFYDSNINSA ATVRLNIYQA FLLSAMKFHC
YTRNLSNICK LQSGYHMEII EKALRRMHTF IKRRMRSMDL DSSFHPILQL KKGEVLWLGL
KAFIQVLKRK QSRHKELLSL LKSKLLAHPL PETASPELKY AVDDSHSSLL WKIKY
//