ID   K7WDE6_MAIZE            Unreviewed;      1166 AA.
AC   K7WDE6;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=ZEAMMB73_Zm00001d047451 {ECO:0000313|EMBL:AQL06526.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQL06526.1};
RN   [1] {ECO:0000313|EMBL:AQL06526.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQL06526.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; CM000785; AQL06526.1; -; Genomic_DNA.
DR   AlphaFoldDB; K7WDE6; -.
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   Gene3D; 1.10.10.1970; TERT catalytic subunit-like; 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; 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   RNA-directed DNA polymerase {ECO:0000256|RuleBase:RU365061,
KW   ECO:0000313|EMBL:AQL06526.1};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365061};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
SQ   SEQUENCE   1166 AA;  133605 MW;  3476B74E5482C033 CRC64;
     MARRRRRVFR GRVPPDLHRA YGALARTLGH AVLSLIPPPT QAGTPCSACR GRGGAGCLAC
     RRWEYLLRDG DPVAYRSLIT RAVCAVAPSG SATPPPLYTP GNGGHSQAKL VGVAIKLMMM
     DRACTTTNVL SSGCRAIGDL LMCYILRHSS IFLPVKKNVF FQVTGLPLND FLQKPMFASA
     AKNQQPQSTK GKYLCYLCQN PERSQIIYGG YANNSKVACS ELPLTNGPIK CSNLDNQNSR
     KRKRLYKWQR LKKQKQIFPS SEDKSLTSQS EISTNGFGVH DVLLEDLCAT VKDKSQFLEP
     TVDNDSLAMN IRTSQCNSTS RIQSTSPQVG LPNFMHLNNG LICFNCLMLN SSKRVSVDLL
     ISRHTIFYNR KTSYNVFHGN HILNKRKIPD ALSLIIHIFG FKGCCAKLLK CNCHVSTTTN
     SNCMCLSLPK LMNKLIRNSK RCQYRKLFLK HCPVNSKCAA DVAKNHNNKA HFLIGGKSAY
     YDQSYVQLEA YSTHQQVVSF IWAVLTRIIP EPLLGNSSSK RSLRINIWKF IKLRRFESFC
     LSDCIGELKV SHYSWLSNIG FSDCFCSALM EKEIWSSNGS EEEKLQNLLR CWISWMFSDI
     VIPLVQSYFY VTERESRRYD VLYYPKTVWR NLTSTAIASL NRQNFRILRG TSRKEAIQSC
     YFSTVRFIPK AKDMRPLVNL RAQSKNALLN NCHLIINKVK DENPDKFGSS VFDYNNVHQN
     IWHFISSVRS HLKEKIKIYI VVADVSKAFD CITHDMLLKV VDDALKCDDY VLRKCKKVVC
     NWSKNAIYRF DSNVSISNGD NVCDFLIQLS SRGGILVDQG KSCKIRKKEI QCFLSKQVKC
     NILKIGQNFY SQRVGIIQGN KLSPNLCSLY FGHLENSELL KSLHDNKIDS EKDVLTPRSL
     LMRFIDDFIF ISFSKEQALN FFNRMRRGFV NYNCYMNDSK YGFNFEVANS EHCSNRIYKG
     DDGFSFIPWS GLLINCETLE IQADYTRYLD IHISSTITAK MHSSAKYLES KLCHYMRPKC
     HPIFFDSVIN SPGTVRLNIY QNFLLCAMKF HCYFRSMPDP GIMKPELLHI IKRTFRYMHS
     LVAKRMHEAE LQYDVRPVLK LRRKETMWLG LSAYLRVLQK KQSRYSELLA SLREEIGRCG
     HLDRHNDALR YAVDDSHSSV FWKFKF
//