ID A0A2D0SD37_ICTPU Unreviewed; 1062 AA.
AC A0A2D0SD37;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
GN Name=tert {ECO:0000313|RefSeq:XP_017340637.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017340637.1};
RN [1] {ECO:0000313|RefSeq:XP_017340637.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017340637.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_017340637.1; XM_017485148.3.
DR AlphaFoldDB; A0A2D0SD37; -.
DR STRING; 7998.ENSIPUP00000033980; -.
DR Ensembl; ENSIPUT00000035320; ENSIPUP00000033984; ENSIPUG00000022566.
DR GeneID; 108274792; -.
DR KEGG; ipu:108274792; -.
DR CTD; 7015; -.
DR OMA; SEREHDW; -.
DR OrthoDB; 55913at2759; -.
DR Proteomes; UP000221080; Chromosome 14.
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 InterPro; IPR049139; TERT_C.
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 Pfam; PF21399; TERT_C; 1.
DR PRINTS; PR01365; TELOMERASERT.
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 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|RefSeq:XP_017340637.1};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365061};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365061}.
FT DOMAIN 556..870
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 203..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 121393 MW; 5C522391B6E3C7DE CRC64;
MSDYSLTRVL EILRGLYGRV QTLEEFSDGV EFSDGRKPVL MEECDSERFK TLIRGLIVCT
ESPLTHTPSS AQLGTLPEVL AFVLNRMKMK KKRNVLRFGY RSSSGGADSD PFKFHGSISQ
SAAFICGNEA WAKINQRLGS DLTQYLLTRC AMFTTAPPTC LVQICGVPVY DLVPVHTWSG
FFLNSSNKAG MLNRNQRIDI KKQNGVRKEA KNRRRRQMNS KNAKNTVNAK KRKREEGKED
VEDIRESHEE LPAKQRCIEI VGKSCIIENI CPVQSELSHI SPAPKHGLSS WKPSDQPPHR
PSHCFISVLS MLYGGRGMKG FLLNRKLQGH MGRARNIQGA DVVRMVFCLK DKAQLSGSNS
QNRKLPKRFF AMVPIFTLLL RRHRKCDYIH FLSQKCATSE GEGDMASLLP SHCSSYRVYL
FVRECVRFVI PDELWGSQHN LLQFLSRVKH FLRLGKFEKL SLTQVMWKIK VSDCHWLGHK
KGHCPSEHRY REWIFGQFLL WMLKDFVIGL VKSLFYVTES VGQKHALRFY RRHIWTRLQD
QAFREHLSKG QWEELSPAEV ASLPKNTVTS RIRFIPKTNG MRPITRLIGT GAAMQFQSSA
RDLQNILSVC VRERPTLLGS TVWGRQDIHR VLRSITHSHT PWYFVKVDIS GAYDSLPHCK
LLDVVQDVLK PLEENCFSLR HYAKVCTDSE QEIRKHFCTR AEAVESLNMK GFVMEEQNNG
KLHNAILVEM LSVEVKGADV FQFFKQMLSS CIIQYNKKVF RQVCGIPQGS AVSTMLCNLC
YGHMENCVLK KATEKGGYLM RLVDDFLLIT PRLSKAVDFL KTLMAGVPDY GCVINPQKVA
VNFPLRDELE SVEMTEFPAH CMFPWCGLLI DTRSLHVYND YSGYAGQSLR YSLTLGSAHS
PATFMRKKLL MILRLKCDSI LLDVHLNSIE VVYKNIYKLL LLQAMRFHVC VKSLPLGQGV
WTNPSFFLKM IWRMVKITNK SITHSNSGVC VDDVLQYEAV ELLCCLAFDV VLTLHRSSYR
ALLPHIHKRK RCLMSVLRGV RLARVFQAAT PRIPPDFTSI RA
//
