ID   A0A0E0J9B2_ORYNI        Unreviewed;       875 AA.
AC   A0A0E0J9B2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Telomerase reverse transcriptase {ECO:0000256|RuleBase:RU365061};
DE            EC=2.7.7.49 {ECO:0000256|RuleBase:RU365061};
DE   AltName: Full=Telomerase catalytic subunit {ECO:0000256|RuleBase:RU365061};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA12G09220.3};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA12G09220.3}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA12G09220.3};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA12G09220.3}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA12G09220.3};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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|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|RuleBase:RU365061}.
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DR   AlphaFoldDB; A0A0E0J9B2; -.
DR   EnsemblPlants; ONIVA12G09220.3; ONIVA12G09220.3; ONIVA12G09220.
DR   Gramene; ONIVA12G09220.3; ONIVA12G09220.3; ONIVA12G09220.
DR   Proteomes; UP000006591; 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; -; 2.
DR   Gene3D; 3.30.70.2630; -; 1.
DR   InterPro; IPR000477; RT_dom.
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   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   Chromosome {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}; Nucleus {ECO:0000256|RuleBase:RU365061};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW   RNA-directed DNA polymerase {ECO:0000256|RuleBase:RU365061};
KW   Telomere {ECO:0000256|RuleBase:RU365061};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
FT   DOMAIN          499..772
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
SQ   SEQUENCE   875 AA;  100192 MW;  E82A976C532AD915 CRC64;
     MPRRRRRRRA APGGQVPPEL RLAYGARALT LGRAVFSLLP SPRHCESPCP ACRGRVASGC
     LACRRWEHLL RDGDPIAYRR LITRAVCAIA ADDLSAPPPP RYTPGNSGHS QARLVREMMK
     SIVADQSHGT KNVLCNGLHE GGQSICISDL VSSSSWSILL HRIGDLLMCY LLRSLVFHSM
     WFCEILYLQV LLRENINPKL QKQNVIHTCK IVTQQSCETC GSIRRAESKD PSEGCNCPKF
     PSDGRSGECC NCYTHNTRKR KRLYSWQRRS KKKQVCSVDE SSAEWSKLNG SNFNMSNGPS
     ENLAGKMNDQ AQSVELTVDN TSLARSNDDS SSEIKVINAT ILSSEKSPCS VFDIRGSQGL
     SCHYSLSEVQ YQSTCPQVGP SSYLHLNVAP DVTKNDGKAH YPPGGKAAYY DRSFSRLEAY
     STHQQVASFV WAVLKRIVPK PLLGNSFGKR SLRTNIWKFI KLQRESKRYD VFYYPKSVWR
     DLTSNAIASL NKKNFRILRG EPRKAVRHLN CSSRVRFLPK AKDMRPLVDL RAKSKDANLN
     KCHLIMKKLR DEKPEMFGSS VFDYNNVHQN LSQFISSKRS QLMKKLKAFD CVSHDMVLKM
     IDDAFKCDEY TVRKCSKGTI CRILKEQFHH LLYEQIKCNI LKIGQKYYLQ QVGIAQGSKL
     SPNLCSLYYG HLENSVLSKF LHDSKLNAGE AFSEPEYLLM RFIDDFIFIS FSLEHAQKFL
     NRMRRGFVFY NCYMNDSKYG FNFCAGNSEP SSNRLYRGDD GVSFMPWSGL LINCETLEIQ
     ADYTRYMHSL IVRRMQDVEL HYNVRPVLKL RRKETIWLGL TAYIRVLQQK QSRYKDMLTL
     LTAELGRYCH LGHECDTLRY AVDDSHSSMF WKFKF
//