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Database: UniProt
Entry: A4ID03_LEIIN
LinkDB: A4ID03_LEIIN
Original site: A4ID03_LEIIN 
ID   A4ID03_LEIIN            Unreviewed;      1451 AA.
AC   A4ID03; A0A2K4Z8H6; A0A381MX16;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=LINJ_36_4120 {ECO:0000313|EMBL:CAM72732.1};
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM72732.1, ECO:0000313|Proteomes:UP000008153};
RN   [1] {ECO:0000313|EMBL:CAM72732.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM72732.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM72732.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM72732.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(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; FR796468; CAM72732.1; -; Genomic_DNA.
DR   RefSeq; XP_001469622.1; XM_001469585.1.
DR   AlphaFoldDB; A4ID03; -.
DR   STRING; 5671.A4ID03; -.
DR   GeneID; 5073724; -.
DR   KEGG; lif:LINJ_36_4120; -.
DR   VEuPathDB; TriTrypDB:LINF_360048200; -.
DR   eggNOG; KOG1005; Eukaryota.
DR   InParanoid; A4ID03; -.
DR   OMA; NLSHQDE; -.
DR   OrthoDB; 127986at2759; -.
DR   Proteomes; UP000008153; Chromosome 36.
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   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; PF12009; Telomerase_RBD; 1.
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:UP000008153};
KW   RNA-directed DNA polymerase {ECO:0000256|RuleBase:RU365061,
KW   ECO:0000313|EMBL:CAM72732.1};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365061};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
SQ   SEQUENCE   1451 AA;  157577 MW;  42F91AAC815EB340 CRC64;
     MSASFPSIPG FAGPLSLKAF LEEYFGLHLT FAVETASPSP RAAAAAEAPS AAGFRALRDV
     VLPPNQSFLV VVYVALHASS SPPPTTAHAS PTPPTPAPGC AASATGFGRL RQPLTHQTAA
     STAHDTYVAR CSPADRPNSS CSSSSSTGKN GNARGLWRSS AFWLLYTNTS HRPLTDALLR
     HPWWASFAAC LGPAAMGFIE MYCPIVLQLE AMAGGVQVLG PALKHAALET SFSATAPSSE
     MKGPPPQGSG YVSSRGVKRA VDTGECSGFL PLQKQRRVEA PPKAKAGRRL QRGVVPCSRP
     RRDDPFASPV NRAAMPVTWA AALTRTDVPR TRLYSVRVSD SDGAGDGSGG ALPLPAGFLE
     AQWLRRHPHS LHRVLQAALP KRVAYGASAR RYSVGASERV TGCTSVEDIP MWHVAHVFRW
     LVLQPPQSGA DASPTTPPKF DLPSYLRRLL STVVDQCSRL DLRGAALKHT GYLEEAFRRQ
     QQGVEPWDVQ RLSTPVDVVV SYLRTLLSTL RWAPLKEAKN RSFWGRDAAG SERVLDALMG
     AVRNWLIAGR HAIVPVSRFL DGVPVAQVPW LNGFYTTTPS LPFSAATSSA ARHARRERSH
     VQQRVWLQFV LFLTQDILPF LLRASFTITW SSKNTHKLLF FPAFVWRRLI RREVRRTRSC
     GAPRSQMPLA GESARSVGAE RVALSSAPCA CEGAATAALP TPHSAASKAS AAISAPRDVW
     RAVRTDGVLA HRGARATLAT RGGGASCLYA SVRFRPDRRK LRPIAVVRSA SLRSLKEMAR
     GSPSPYSHAS AIVRLLCRLG CSDTDGQLPA ATATLLRRVQ ARSRHNHHTG VHRFPHPLPP
     HLPHKAALRD ALRCLVSGVE EQRVRDGLPR LSNLSHQDEY AELRSFCEEV RRRPALPCEG
     PAGTAPVVSS ASPPSAAACC FAPYVTLVRS DASRCYDNLP QERVLAAVAS LVKHDAYRVL
     RFTAIHALDG EAACKGGCLL RRTFTTRTIA CAEAECGVLA RIPRGHIYWE EEEEGRTLSG
     PHTTAAVSRT TKASSRCGAN LISGAAVRAL LSEHLRHHLV VVSGGNLLEQ RVGILQGSPV
     AMLLCDRLFS DVVDTALSGI LSEHAERSLL LRRVDDVLVA TTSPAAAERC LQAMQRGWPS
     VGYLSNPSKL TLSTACGSLV PWCGLLLHDT TLEVSVEWRR IGVLLASLRV GDPHYVHRGD
     HEPLYLTQRF LAVLQLRVAP TVLCGRMNSK TRQLQTFYEV GLLWSRVVLE KVQEALPAAR
     NRCVAVLLLH PLAVCVGRLC RLLNRHQRFL AARKSACDVS AAEVRACVLT ALHRTVQAKL
     RVLQARTVRV MTAQRGRTPR GTSLKGRQKP PCTNKASSAG CKYCERRRKG RNRRCSTRVC
     LRSFWWLAAA EVELQWRRSL GALHRAAPHP GEARGSTAPS LSPSASASLL MEDGPLSMHA
     RALSATRLSQ T
//
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