ID K8EYH3_9CHLO Unreviewed; 1541 AA.
AC K8EYH3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-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=Bathy08g02850 {ECO:0000313|EMBL:CCO17545.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO17545.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO17545.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO17545.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO082271; CCO17545.1; -; Genomic_DNA.
DR RefSeq; XP_007511424.1; XM_007511362.1.
DR STRING; 41875.K8EYH3; -.
DR GeneID; 19014264; -.
DR KEGG; bpg:Bathy08g02850; -.
DR eggNOG; KOG1005; Eukaryota.
DR OrthoDB; 55913at2759; -.
DR Proteomes; UP000198341; Chromosome_8.
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; IPR043502; DNA/RNA_pol_sf.
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; PF00078; RVT_1; 1.
DR Pfam; PF12009; Telomerase_RBD; 1.
DR SMART; SM00975; Telomerase_RBD; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU365061};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000198341};
KW RNA-directed DNA polymerase {ECO:0000256|RuleBase:RU365061,
KW ECO:0000313|EMBL:CCO17545.1};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365061};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
FT DOMAIN 905..1336
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 546..577
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 373..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1541 AA; 175787 MW; 2163B3972B7F8879 CRC64;
METRPPPPPP SEEKDERSRR RGRRRRKTEK KRRQGGGEKN KKKQNEIPIL LRAVYGRHVY
TVREAIRKVC EQFRGAPKSV MKNLEDKERD SRAYARGVLD ESFIALPERL PPLVMKSSAE
EEAEEEEEED LGARGYPTMS SPPAIGRPTA KERVATVQMK FFSARQKPNN ALCFGLTRFA
KGRDERNCVN SAEAFATSTH WGTLWDRVGD EIAEWLMLYA SGFASLTSTS TVTTTANAEK
IVRQLFETSG APTVIAKAKK KSKKRSRGRR LSSEKEERLV QILGKPITSE HVVFKASMDR
ANCTYKKSTA SALASGVSHH ESMANYSSVF SQGAKKMKKK LTPKQIKKVK RRKAKRKEYA
DMKKKAKEGN GKVENGQPQQ LSSKEDVTMK QTTVNANFVV VGNEENSVPE ATPEEDTQTT
KEDTPILSTQ ELEDDDWCIP ETPSQSNGDA DDDDDDDDDD AGVQGTAEDD MNDSPVKNKK
RGRETRKPRP PSWVRRKLAK ERAEAEAKAK ETADEAKREE TNTTSFIATE SMGEDEKWAM
LARYAEQSKQ RKLERLAKEK QEQIQQAELK AKASRVIGKQ TKRKNAKKTV DANHPRNIVL
DRSPALYCST FSKRPGFPAK HILRCNGSSI NASRKLYADI FGAKKRKVKT PLMHQQRIND
PRMVMSQAPS SYMSSEHQEI IPTQLSQKSP RMTIRISKSH RKNVLPLLRR TLRRAKKCNF
AKLLDLHCPV KRSDWRTADT EQLVKLNSSH KDVSSFIWAI LRGVLPKQFL GSKTTTKRRL
REFVSRIVSL RRIERCTLHE AMIGVKTSDY AFLDNVDYRR REKKKIQKKK TVAEFEARKR
RVEKIILWII KSIVFPVIRS HFFVTDTDHE RQKMYYYRKG VWSRIVRAKN REFVTSGRYE
KLSKNDTENT LSHHSLGFSR IRWKPKKTGV RPIAMLGQPA SMRLTSKKRD GSGFRKKMKF
EFEPVNDRLY TISDILDHEI RADETLMGNF VSDYDETMKI YAPFAERWRR KQGLLNTDEV
DEVVDSEDSP EDINKTKATV KDKKKLPKLY FVCADIKAAF DSIPTEKLET VISSLFKKQE
YAMLKYRTQS VLGNRYATRK VAFATENVED TGMDIVHKNS SGSAITSSQN DANTATADEN
IKNSKKKLPG PIFSPNESDV GRRALVKTLP PGSVSIDLGK TRTAYRHQAL NTLREHLGNT
LVKSHGSLFR QKIGIPQGSI LSTKLCALFY AHMEQTQSMA AFETEIYKGT PKKKVLNEGY
GDGVFMRWTD DLLFVTDNFS RAKHFLNSLL DGIAEYGVEI NPTKTKINFD HLERKLEKNV
ECKDGCEFIP WCGLLFDTQT LEVRADYSKY LNVWLRETIN LPSSHLAWKY LSNKTRSYLN
HKLCALLYDP RVNSRETIAT NMYQALLLCA AKTTSYVRAV EAVPGVTPCG HALLKRAIES
AISYARTGAR KRLLDRYLDP NLVPSEKVSR ALGLLAFQKY FSWYSLVGRR RKKKNKTKHE
ETAAWLRAQL SLSRSMSETV AEVSKTITPA CKNEFFESIR A
//
