TERT_TETTS
ID TERT_TETTS Reviewed; 1117 AA.
AC O77448; Q22ZB5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Telomerase reverse transcriptase;
DE EC=2.7.7.49 {ECO:0000269|PubMed:10944124, ECO:0000269|PubMed:15696174, ECO:0000269|PubMed:16462747, ECO:0000269|PubMed:20713447};
DE AltName: Full=Telomerase catalytic subunit;
DE AltName: Full=Telomerase subunit P133 {ECO:0000303|PubMed:9671704};
GN Name=TERT {ECO:0000303|PubMed:9671703};
GN ORFNames=TTHERM_00112560 {ECO:0000312|EMBL:EAR90406.3};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9671703; DOI=10.1073/pnas.95.15.8479;
RA Bryan T.M., Sperger J.M., Chapman K.B., Cech T.R.;
RT "Telomerase reverse transcriptase genes identified in Tetrahymena
RT thermophila and Oxytricha trifallax.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8479-8484(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9671704; DOI=10.1073/pnas.95.15.8485;
RA Collins K., Gandhi L.;
RT "The reverse transcriptase component of the Tetrahymena telomerase
RT ribonucleoprotein complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8485-8490(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210;
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-158; GLN-168; ARG-226;
RP PHE-230; TYR-231; CYS-232; HIS-234; ARG-237; CYS-331; PHE-379; ARG-381;
RP PRO-389; TRP-433; PHE-462; ARG-473; TYR-477; THR-479; GLU-480; ARG-492;
RP LYS-493; LYS-532; ARG-534; LYS-538; LYS-539; PHE-542; ARG-543; TYR-623;
RP ASP-624; GLN-767; GLN-773; SER-778; ARG-812; LYS-849; PHE-854; TRP-876;
RP GLY-878; SER-880; ASP-882; ASN-884; THR-885; LYS-910 AND LYS-1077.
RX PubMed=10944124; DOI=10.1093/emboj/19.16.4412;
RA Miller M.C., Liu J.K., Collins K.;
RT "Template definition by Tetrahymena telomerase reverse transcriptase.";
RL EMBO J. 19:4412-4422(2000).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE TELOMERASE
RP HOLOENZYME COMPLEX.
RX PubMed=15696174; DOI=10.1038/nsmb900;
RA Prathapam R., Witkin K.L., O'Connor C.M., Collins K.;
RT "A telomerase holoenzyme protein enhances telomerase RNA assembly with
RT telomerase reverse transcriptase.";
RL Nat. Struct. Mol. Biol. 12:252-257(2005).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
RX PubMed=17322903; DOI=10.1038/nature05600;
RA Stone M.D., Mihalusova M., O'connor C.M., Prathapam R., Collins K.,
RA Zhuang X.;
RT "Stepwise protein-mediated RNA folding directs assembly of telomerase
RT ribonucleoprotein.";
RL Nature 446:458-461(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE TELOMERASE HOLOENZYME
RP COMPLEX, AND MUTAGENESIS OF LEU-327; PRO-334 AND ASP-618.
RX PubMed=20713447; DOI=10.1128/mcb.00827-10;
RA Berman A.J., Gooding A.R., Cech T.R.;
RT "Tetrahymena telomerase protein p65 induces conformational changes
RT throughout telomerase RNA (TER) and rescues telomerase reverse
RT transcriptase and TER assembly mutants.";
RL Mol. Cell. Biol. 30:4965-4976(2010).
RN [8]
RP IDENTIFICATION IN THE TELOMERASE HOLOENZYME.
RX PubMed=19941821; DOI=10.1016/j.molcel.2009.09.041;
RA Min B., Collins K.;
RT "An RPA-related sequence-specific DNA-binding subunit of telomerase
RT holoenzyme is required for elongation processivity and telomere
RT maintenance.";
RL Mol. Cell 36:609-619(2009).
RN [9] {ECO:0007744|PDB:2B2A}
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 2-191, FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-94; LYS-103;
RP 145-GLU-GLU-146; GLN-168; LEU-174; PHE-178; 183-LYS--LYS-186;
RP 183-LYS--LYS-189; 185-LYS-LYS-186; LYS-185; TRP-187; TYR-188 AND LYS-189.
RX PubMed=16462747; DOI=10.1038/nsmb1054;
RA Jacobs S.A., Podell E.R., Cech T.R.;
RT "Crystal structure of the essential N-terminal domain of telomerase reverse
RT transcriptase.";
RL Nat. Struct. Mol. Biol. 13:218-225(2006).
RN [10] {ECO:0007744|PDB:2R4G}
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 254-519.
RX PubMed=17997966; DOI=10.1016/j.str.2007.09.007;
RA Rouda S., Skordalakes E.;
RT "Structure of the RNA-binding domain of telomerase: implications for RNA
RT recognition and binding.";
RL Structure 15:1403-1412(2007).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE TELOMERASE HOLOENZYME.
RX PubMed=23552895; DOI=10.1038/nature12062;
RA Jiang J., Miracco E.J., Hong K., Eckert B., Chan H., Cash D.D., Min B.,
RA Zhou Z.H., Collins K., Feigon J.;
RT "The architecture of Tetrahymena telomerase holoenzyme.";
RL Nature 496:187-192(2013).
RN [12] {ECO:0007744|PDB:5C9H}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 217-516 IN COMPLEX WITH TER RNA.
RX PubMed=26436828; DOI=10.1038/nsmb.3101;
RA Jansson L.I., Akiyama B.M., Ooms A., Lu C., Rubin S.M., Stone M.D.;
RT "Structural basis of template-boundary definition in Tetrahymena
RT telomerase.";
RL Nat. Struct. Mol. Biol. 22:883-888(2015).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE TELOMERASE HOLOENZYME, AND
RP MUTAGENESIS OF LYS-90 AND ARG-137.
RX PubMed=26472759; DOI=10.1126/science.aab4070;
RA Jiang J., Chan H., Cash D.D., Miracco E.J., Ogorzalek Loo R.R., Upton H.E.,
RA Cascio D., O'Brien Johnson R., Collins K., Loo J.A., Zhou Z.H., Feigon J.;
RT "Structure of Tetrahymena telomerase reveals previously unknown subunits,
RT functions, and interactions.";
RL Science 350:AAB4070-AAB4070(2015).
RN [14] {ECO:0007744|PDB:6D6V}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS) OF THE TELOMERASE
RP HOLOENZYME IN COMPLEX WITH TELOMERIC DNA AND TER RNA.
RX PubMed=29775593; DOI=10.1016/j.cell.2018.04.038;
RA Jiang J., Wang Y., Susac L., Chan H., Basu R., Zhou Z.H., Feigon J.;
RT "Structure of telomerase with telomeric DNA.";
RL Cell 173:1179-1190(2018).
CC -!- FUNCTION: Catalytic component of telomerase, an essential
CC ribonucleoprotein enzyme that copies new telomeric repeats onto
CC chromosome ends by repetitively synthesizing the short telomere-repeat
CC sequence 5'-TTGGGG-3' using an RNA template component TER
CC (PubMed:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447,
CC PubMed:16462747). TERT is a reverse transcriptase that adds simple
CC sequence repeats to chromosome ends by copying a template sequence
CC within the RNA component of the enzyme (PubMed:10944124,
CC PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747).
CC {ECO:0000269|PubMed:10944124, ECO:0000269|PubMed:15696174,
CC ECO:0000269|PubMed:16462747, ECO:0000269|PubMed:17322903,
CC ECO:0000269|PubMed:20713447}.
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:0000269|PubMed:10944124, ECO:0000269|PubMed:15696174,
CC ECO:0000269|PubMed:16462747, ECO:0000269|PubMed:20713447};
CC -!- SUBUNIT: Component of the telomerase holoenzyme complex, composed of
CC the catalytic core (the catalytic subunit TERT, the telomerase RNA
CC template component TER and TAP65/p65), which is associated with two
CC heterotrimeric subcomplexes: (i) the replication protein A (RPA)-
CC related subcomplex, composed of TEB1, RPA2/TEB2 and RPA3/TEB3 and (ii)
CC the CST-like subcomplex, composed of TAP75/p75, TAP45/p45 and TAP19/p19
CC (PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:19941821,
CC PubMed:23552895, PubMed:26472759, PubMed:29775593). TEB1 and the CST-
CC like subcomplex are tethered to the catalytic core by TAP50/p50
CC (PubMed:19941821, PubMed:23552895, PubMed:26472759, PubMed:29775593).
CC {ECO:0000269|PubMed:15696174, ECO:0000269|PubMed:17322903,
CC ECO:0000269|PubMed:19941821, ECO:0000269|PubMed:20713447,
CC ECO:0000269|PubMed:23552895, ECO:0000269|PubMed:26472759,
CC ECO:0000269|PubMed:29775593}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU365061}.
CC Chromosome, telomere {ECO:0000255|RuleBase:RU365061,
CC ECO:0000269|PubMed:16462747}.
CC -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC subfamily. {ECO:0000255|RuleBase:RU365061}.
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DR EMBL; AF062652; AAC39135.1; -; Genomic_DNA.
DR EMBL; AF061284; AAC39140.1; -; mRNA.
DR EMBL; GG662798; EAR90406.3; -; Genomic_DNA.
DR PIR; T14891; T14891.
DR RefSeq; XP_001010651.3; XM_001010651.3.
DR PDB; 2B2A; X-ray; 2.22 A; A/B/C=2-191.
DR PDB; 2R4G; X-ray; 1.71 A; A=254-519.
DR PDB; 5C9H; X-ray; 3.00 A; A/B=217-516.
DR PDB; 6D6V; EM; 4.80 A; A=1-1117.
DR PDB; 7LMA; EM; 3.30 A; A=1-1117.
DR PDB; 7LMB; EM; 3.80 A; A=1-1117.
DR PDBsum; 2B2A; -.
DR PDBsum; 2R4G; -.
DR PDBsum; 5C9H; -.
DR PDBsum; 6D6V; -.
DR PDBsum; 7LMA; -.
DR PDBsum; 7LMB; -.
DR AlphaFoldDB; O77448; -.
DR SMR; O77448; -.
DR DIP; DIP-60200N; -.
DR DIP; DIP-61863N; -.
DR IntAct; O77448; 8.
DR STRING; 5911.EAR90406; -.
DR PRIDE; O77448; -.
DR EnsemblProtists; EAR90406; EAR90406; TTHERM_00112560.
DR GeneID; 7843517; -.
DR KEGG; tet:TTHERM_00112560; -.
DR eggNOG; KOG1005; Eukaryota.
DR HOGENOM; CLU_282497_0_0_1; -.
DR OrthoDB; 1297956at2759; -.
DR BRENDA; 2.7.7.49; 6245.
DR EvolutionaryTrace; O77448; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070034; F:telomerase RNA binding; IDA:UniProtKB.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IDA:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:UniProtKB.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR021891; Telomerase_RBD.
DR InterPro; IPR003545; Telomerase_RT.
DR PANTHER; PTHR12066; PTHR12066; 2.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF12009; Telomerase_RBD; 1.
DR PRINTS; PR01365; TELOMERASERT.
DR SMART; SM00975; Telomerase_RBD; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; RNA-binding;
KW RNA-directed DNA polymerase; Telomere; Transferase.
FT CHAIN 1..1117
FT /note="Telomerase reverse transcriptase"
FT /id="PRO_0000054929"
FT DOMAIN 517..881
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 1..191
FT /note="TEN"
FT /evidence="ECO:0000305|PubMed:29775593"
FT REGION 217..519
FT /note="RBD"
FT /evidence="ECO:0000305|PubMed:29775593"
FT REGION 520..887
FT /note="RT"
FT /evidence="ECO:0000305|PubMed:29775593"
FT REGION 638..742
FT /note="TRAP"
FT /evidence="ECO:0000305|PubMed:29775593"
FT REGION 888..1117
FT /note="CTE"
FT /evidence="ECO:0000305|PubMed:29775593"
FT BINDING 618
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 815
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405,
FT ECO:0000305|PubMed:20713447"
FT BINDING 816
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT MUTAGEN 90
FT /note="K->A: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:26472759"
FT MUTAGEN 94
FT /note="D->A: Decreased reverse transcriptase activity; does
FT not affect DNA-binding."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 103
FT /note="K->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 137
FT /note="R->A: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:26472759"
FT MUTAGEN 145..146
FT /note="EE->AA: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 158
FT /note="F->A: Abolished reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 168
FT /note="Q->A: Strongly decreased reverse transcriptase
FT activity; strongly decreased DNA-binding."
FT /evidence="ECO:0000269|PubMed:10944124,
FT ECO:0000269|PubMed:16462747"
FT MUTAGEN 168
FT /note="Q->E: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 168
FT /note="Q->N: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 174
FT /note="L->A: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 178
FT /note="F->A: Strongly decreased reverse transcriptase
FT activity; strongly decreased DNA-binding."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 183..189
FT /note="KQKKWYK->AQAAWYA: Strongly decreased reverse
FT transcriptase activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 183..186
FT /note="KQKK->AQAA: Strongly decreased reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 185..186
FT /note="KK->AA: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 185
FT /note="K->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 187
FT /note="W->A: Abolished reverse transcriptase activity;
FT strongly decreased DNA-binding."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 188
FT /note="Y->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 189
FT /note="K->A: Slightly decreased reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:16462747"
FT MUTAGEN 226
FT /note="R->A: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 230
FT /note="F->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 231
FT /note="Y->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 232
FT /note="C->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 234
FT /note="H->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 237
FT /note="R->A: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 327
FT /note="L->A: Impaired assembly of telomerase holoenzyme,
FT which can be rescued by TAP65/p65."
FT /evidence="ECO:0000269|PubMed:20713447"
FT MUTAGEN 331
FT /note="C->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 334
FT /note="P->A: Impaired assembly of telomerase holoenzyme,
FT which can be rescued by TAP65/p65."
FT /evidence="ECO:0000269|PubMed:20713447"
FT MUTAGEN 379
FT /note="F->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 381
FT /note="R->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 389
FT /note="P->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 433
FT /note="W->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 462
FT /note="F->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 473
FT /note="R->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 477
FT /note="Y->F: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 479
FT /note="T->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 480
FT /note="E->D: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 480
FT /note="E->Q: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 492
FT /note="R->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 493
FT /note="K->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 532
FT /note="K->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 532
FT /note="K->R: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 534
FT /note="R->A: Abolished reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 534
FT /note="R->K: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 538
FT /note="K->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 539
FT /note="K->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 542
FT /note="F->A: Abolished reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 543
FT /note="R->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 543
FT /note="R->K: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 618
FT /note="D->A: Abolished reverse transcriptase activity,
FT which cannot be rescued by TAP65/p65."
FT /evidence="ECO:0000269|PubMed:20713447"
FT MUTAGEN 623
FT /note="Y->A: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 624
FT /note="D->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 767
FT /note="Q->A,N: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 767
FT /note="Q->E: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 773
FT /note="Q->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 778
FT /note="S->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 812
FT /note="R->A: Abolished reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 849
FT /note="K->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 849
FT /note="K->R: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 854
FT /note="F->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 876
FT /note="W->A: Abolished reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 876
FT /note="W->F: Decreased reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 878
FT /note="G->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 880
FT /note="S->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 882
FT /note="D->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 882
FT /note="D->N: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 884
FT /note="N->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 884
FT /note="N->D: Abolished reverse transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 885
FT /note="T->A: Slightly decreased transcriptase activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 910
FT /note="K->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT MUTAGEN 1077
FT /note="K->A: Does not affect reverse transcriptase
FT activity."
FT /evidence="ECO:0000269|PubMed:10944124"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:2B2A"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2B2A"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:2B2A"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:2B2A"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2B2A"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2B2A"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:2B2A"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2B2A"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2B2A"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2B2A"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2B2A"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:2B2A"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:2B2A"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2B2A"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:2B2A"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:2B2A"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:2B2A"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2B2A"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:5C9H"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5C9H"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 301..320
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 356..366
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 373..387
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 395..410
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 419..423
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:2R4G"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 445..466
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 468..475
FT /evidence="ECO:0007829|PDB:2R4G"
FT STRAND 476..483
FT /evidence="ECO:0007829|PDB:2R4G"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 493..509
FT /evidence="ECO:0007829|PDB:2R4G"
FT TURN 510..516
FT /evidence="ECO:0007829|PDB:2R4G"
FT HELIX 522..527
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 539..547
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 561..576
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 577..581
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 590..607
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 628..636
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 643..655
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 696..708
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 714..717
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 729..733
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 738..741
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 742..754
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 763..766
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 778..793
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 796..799
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 800..802
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 808..812
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 814..822
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 824..841
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 846..848
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 849..854
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 858..862
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 865..870
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 872..874
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 883..885
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 896..900
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 909..911
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 912..925
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 926..930
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 934..936
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 939..964
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 973..979
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 981..983
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 984..1008
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 1011..1013
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 1015..1037
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 1042..1046
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 1047..1074
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 1082..1093
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 1094..1098
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 1100..1102
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 1105..1108
FT /evidence="ECO:0007829|PDB:7LMA"
SQ SEQUENCE 1117 AA; 133318 MW; E5AF15E86B0F0CD8 CRC64;
MQKINNINNN KQMLTRKEDL LTVLKQISAL KYVSNLYEFL LATEKIVQTS ELDTQFQEFL
TTTIIASEQN LVENYKQKYN QPNFSQLTIK QVIDDSIILL GNKQNYVQQI GTTTIGFYVE
YENINLSRQT LYSSNFRNLL NIFGEEDFKY FLIDFLVFTK VEQNGYLQVA GVCLNQYFSV
QVKQKKWYKN NFNMNGKATS NNNQNNANLS NEKKQENQYI YPEIQRSQIF YCNHMGREPG
VFKSSFFNYS EIKKGFQFKV IQEKLQGRQF INSDKIKPDH PQTIIKKTLL KEYQSKNFSC
QEERDLFLEF TEKIVQNFHN INFNYLLKKF CKLPENYQSL KSQVKQIVQS ENKANQQSCE
NLFNSLYDTE ISYKQITNFL RQIIQNCVPN QLLGKKNFKV FLEKLYEFVQ MKRFENQKVL
DYICFMDVFD VEWFVDLKNQ KFTQKRKYIS DKRKILGDLI VFIINKIVIP VLRYNFYITE
KHKEGSQIFY YRKPIWKLVS KLTIVKLEEE NLEKVEEKLI PEDSFQKYPQ GKLRIIPKKG
SFRPIMTFLR KDKQKNIKLN LNQILMDSQL VFRNLKDMLG QKIGYSVFDN KQISEKFAQF
IEKWKNKGRP QLYYVTLDIK KCYDSIDQMK LLNFFNQSDL IQDTYFINKY LLFQRNKRPL
LQIQQTNNLN SAMEIEEEKI NKKPFKMDNI NFPYYFNLKE RQIAYSLYDD DDQILQKGFK
EIQSDDRPFI VINQDKPRCI TKDIIHNHLK HISQYNVISF NKVKFRQKRG IPQGLNISGV
LCSFYFGKLE EEYTQFLKNA EQVNGSINLL MRLTDDYLFI SDSQQNALNL IVQLQNCANN
NGFMFNDQKI TTNFQFPQED YNLEHFKISV QNECQWIGKS IDMNTLEIKS IQKQTQQEIN
QTINVAISIK NLKSQLKNKL RSLFLNQLID YFNPNINSFE GLCRQLYHHS KATVMKFYPF
MTKLFQIDLK KSKQYSVQYG KENTNENFLK DILYYTVEDV CKILCYLQFE DEINSNIKEI
FKNLYSWIMW DIIVSYLKKK KQFKGYLNKL LQKIRKSRFF YLKEGCKSLQ LILSQQKYQL
NKKELEAIEF IDLNNLIQDI KTLIPKISAK SNQQNTN
