ID A0A3B4B6X2_9GOBI Unreviewed; 1062 AA.
AC A0A3B4B6X2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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|ARBA:ARBA00032044, ECO:0000256|RuleBase:RU365061};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000024294.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000024294.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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|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 AlphaFoldDB; A0A3B4B6X2; -.
DR STRING; 409849.ENSPMGP00000024294; -.
DR Ensembl; ENSPMGT00000025885.1; ENSPMGP00000024294.1; ENSPMGG00000019650.1.
DR Proteomes; UP000261520; Unplaced.
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 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 Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365061};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
FT DOMAIN 549..865
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 208..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 120575 MW; 8936E077C607DC30 CRC64;
MTSTDLSSVL NILHSLYRKV EPLVEFADGV VFKEGQKARV LDQSDTARFS SFARSVYVCS
DKELQQVPSS TEICSLPELL AFVLNNLKRK KRKNVLIHGY NLLPHNEQQR NADLFKFQGD
VTQSAAYIHG SDLWKKATKR LGTDITRYLL ESCSVFVAVP PSCFFQVCGL PIYDRVSMTS
TTTGITLRPQ NKTRKTRKSK FAIKTCKKLR KSKRDRGSRK RKRETNKCDD EDVETPAKRR
LVDDQNGTDD QAVLLAPTQF TKSLENSSGP GLKEEGVPSW RSGTYPPLPS SQCFFRTLGL
LYGGRGMRGF LLNRKKKDAE GVKRLQGKDL IRVIFFEGIG YLNGAQRKPK KLPQRFFNMV
PMFNQLLRRH RRFLYGRVLQ KLCPSLQQAD PGEGELTLLL SQHCAAHRVY LFVRECLVAV
IPQQAWGSDQ NRVHFLARVR GFLSGGKFDK VSLAELLWKM KVNDCDWIKM SKNGRVPPSE
LAYRTRVLGQ FLAWLLDGYV VGLVRACFYV TESVGLKNAL RFYRQEIWTK LQDLAFRCHL
SKGQMTELTP AQVAHLPKST VISRLRFIPK NDGMRPITRV VGADVKTRLY RGRSRDLLYM
LQACVRTAPS TLGSTVWGMT DIHKAIRSMA SQQKEKTQPL YFVKVDVSGA YESLPHDKLT
EVVTEALTPF LDEIFTLRRF AKVWCDSHEG LKKAFVRQAD LLEDNMGSSN MKSFVSSLQM
SGKIHHSILV EQHFSSDLHG KDALQFFTQM LTGNVVQFGK KTYRQCRGIP QGSVVSSLLC
CLCYGHMENM LFGNKGKTKG YKQNHNCNTL LPTAEVLLPG VPEYGLTINP QKVAVNFKVS
ETATVCPEIR VLPPRCLFPW CGLLLDTHSL DVYKDYSSYA GLSLRYSLTL GSLRSAGQDM
KRKLMAILRL QCHALFLDLK TNSVEAVYKN IYKLVLLHAC RFHVCAQSLP FGQTVAKNPN
YFLQMIWDMA KYANQLIRKN NKGLTLGSKA QTGIIQYEAV ELIFCLCFVL VLSQHRCVYK
TLLPPLQKRK RSLQQRLGDL RLARVRQAFG CKIPDDFLVI QS
//
