TFC4_YEAST
ID TFC4_YEAST Reviewed; 1025 AA.
AC P33339; D6VUI4; Q45U37;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transcription factor tau 131 kDa subunit;
DE AltName: Full=TFIIIC 131 kDa subunit;
DE AltName: Full=Transcription factor C subunit 4;
GN Name=TFC4; Synonyms=PCF1; OrderedLocusNames=YGR047C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND IDENTIFICATION IN TFIIIC.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8387209; DOI=10.1073/pnas.90.9.4027;
RA Marck C., Lefebvre O., Carles C., Riva M., Chaussivert N., Ruet A.,
RA Sentenac A.;
RT "The TFIIIB-assembling subunit of yeast transcription factor TFIIIC has
RT both tetratricopeptide repeats and basic helix-loop-helix motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4027-4031(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN TFIIIC, AND
RP MUTAGENESIS OF HIS-190.
RX PubMed=8264649; DOI=10.1128/mcb.14.1.822-830.1994;
RA Rameau G., Puglia K., Crowe A., Sethy I., Willis I.;
RT "A mutation in the second largest subunit of TFIIIC increases a rate-
RT limiting step in transcription by RNA polymerase III.";
RL Mol. Cell. Biol. 14:822-830(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 147-205, AND
RP MUTAGENESIS OF GLU-148; PHE-162; ALA-164; THR-167; TYR-171; ALA-188;
RP HIS-190; ASN-192 AND TRP-199.
RX PubMed=9372943; DOI=10.1128/mcb.17.12.7119;
RA Moir R.D., Sethy-Coraci I., Puglia K., Librizzi M.D., Willis I.M.;
RT "A tetratricopeptide repeat mutation in yeast transcription factor IIIC131
RT (TFIIIC131) facilitates recruitment of TFIIB-related factor TFIIIB70.";
RL Mol. Cell. Biol. 17:7119-7125(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF HIS-190.
RX PubMed=12167707; DOI=10.1128/mcb.22.17.6131-6141.2002;
RA Moir R.D., Puglia K.V., Willis I.M.;
RT "A gain-of-function mutation in the second tetratricopeptide repeat of
RT TFIIIC131 relieves autoinhibition of Brf1 binding.";
RL Mol. Cell. Biol. 22:6131-6141(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-280; VAL-635 AND
RP VAL-1025.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [8]
RP FUNCTION.
RX PubMed=2686985; DOI=10.1002/j.1460-2075.1989.tb08614.x;
RA Willis I., Schmidt P., Soell D.;
RT "A selection for mutants of the RNA polymerase III transcription apparatus:
RT PCF1 stimulates transcription of tRNA and 5S RNA genes.";
RL EMBO J. 8:4281-4288(1989).
RN [9]
RP IDENTIFICATION IN TFIIIC.
RX PubMed=2180956; DOI=10.1016/s0021-9258(19)34089-x;
RA Parsons M.C., Weil P.A.;
RT "Purification and characterization of Saccharomyces cerevisiae
RT transcription factor TFIIIC. Polypeptide composition defined with
RT polyclonal antibodies.";
RL J. Biol. Chem. 265:5095-5103(1990).
RN [10]
RP INTERACTION WITH TFIIIB.
RX PubMed=1922038; DOI=10.1128/mcb.11.10.5181-5189.1991;
RA Bartholomew B., Kassavetis G.A., Geiduschek E.P.;
RT "Two components of Saccharomyces cerevisiae transcription factor IIIB
RT (TFIIIB) are stereospecifically located upstream of a tRNA gene and
RT interact with the second-largest subunit of TFIIIC.";
RL Mol. Cell. Biol. 11:5181-5189(1991).
RN [11]
RP INTERACTION WITH TFC1; TFC3 AND TFC6, AND PHOSPHORYLATION.
RX PubMed=7688737; DOI=10.1016/s0021-9258(17)46809-8;
RA Conesa C., Swanson R.N., Schultz P., Oudet P., Sentenac A.;
RT "On the subunit composition, stoichiometry, and phosphorylation of the
RT yeast transcription factor TFIIIC/tau.";
RL J. Biol. Chem. 268:18047-18052(1993).
RN [12]
RP MUTAGENESIS OF HIS-190 AND ARG-728.
RX PubMed=7488859;
RA Sethy I., Willis I.M.;
RT "Recessive mutations in the second largest subunit of TFIIIC suggest a new
RT step in RNA polymerase III transcription.";
RL Gene Expr. 5:35-47(1995).
RN [13]
RP INTERACTION WITH RPC10.
RX PubMed=10559229; DOI=10.1074/jbc.274.47.33462;
RA Dumay H., Rubbi L., Sentenac A., Marck C.;
RT "Interaction between yeast RNA polymerase III and transcription factor
RT TFIIIC via ABC10alpha and tau131 subunits.";
RL J. Biol. Chem. 274:33462-33468(1999).
RN [14]
RP INTERACTION WITH BRF1 AND BDP1, AND MUTAGENESIS OF LEU-469; GLU-472;
RP VAL-504; SER-541 AND LEU-542.
RX PubMed=12930823; DOI=10.1074/jbc.m308354200;
RA Liao Y., Willis I.M., Moir R.D.;
RT "The Brf1 and Bdp1 subunits of transcription factor TFIIIB bind to
RT overlapping sites in the tetratricopeptide repeats of Tfc4.";
RL J. Biol. Chem. 278:44467-44474(2003).
RN [15]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to
CC intragenic promoter elements. Upstream of the transcription start site,
CC TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is
CC sufficient for RNA polymerase III recruitment and function. Part of the
CC tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and
CC similar genes. TFC4 is the TFIIIB-assembling subunit of TFIIIC and
CC essential for viability. {ECO:0000269|PubMed:2686985,
CC ECO:0000269|PubMed:8387209}.
CC -!- SUBUNIT: Component of the TFIIIC complex composed of TFC1, TFC3, TFC4,
CC TFC6, TFC7 and TFC8. The subunits are organized in two globular
CC domains, tauA and tauB, connected by a proteolysis-sensitive and
CC flexible linker. Interacts with TFC1, TFC3, TFC6, TFIIIB subunits BRF1
CC and BDP1, and with RNA polymerase III subunit RPC10.
CC {ECO:0000269|PubMed:10559229, ECO:0000269|PubMed:12930823,
CC ECO:0000269|PubMed:1922038, ECO:0000269|PubMed:2180956,
CC ECO:0000269|PubMed:7688737, ECO:0000269|PubMed:8264649,
CC ECO:0000269|PubMed:8387209}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:7688737}.
CC -!- MISCELLANEOUS: Present with 876 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L12722; AAA35145.1; -; Genomic_DNA.
DR EMBL; DQ115391; AAZ22462.1; -; Genomic_DNA.
DR EMBL; Z72832; CAA97046.1; -; Genomic_DNA.
DR EMBL; Z72833; CAA97048.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08145.1; -; Genomic_DNA.
DR PIR; A47453; A47453.
DR RefSeq; NP_011561.3; NM_001181176.3.
DR PDB; 5AEM; X-ray; 3.40 A; A=123-566.
DR PDB; 5AIO; X-ray; 3.15 A; A=123-566.
DR PDB; 6YJ6; EM; 3.10 A; A=1-1025.
DR PDBsum; 5AEM; -.
DR PDBsum; 5AIO; -.
DR PDBsum; 6YJ6; -.
DR AlphaFoldDB; P33339; -.
DR SMR; P33339; -.
DR BioGRID; 33294; 139.
DR ComplexPortal; CPX-1656; Transcription factor TFIIIC complex.
DR DIP; DIP-230N; -.
DR IntAct; P33339; 16.
DR MINT; P33339; -.
DR STRING; 4932.YGR047C; -.
DR iPTMnet; P33339; -.
DR MaxQB; P33339; -.
DR PaxDb; P33339; -.
DR PRIDE; P33339; -.
DR EnsemblFungi; YGR047C_mRNA; YGR047C; YGR047C.
DR GeneID; 852938; -.
DR KEGG; sce:YGR047C; -.
DR SGD; S000003279; TFC4.
DR VEuPathDB; FungiDB:YGR047C; -.
DR eggNOG; KOG2076; Eukaryota.
DR GeneTree; ENSGT00390000016929; -.
DR HOGENOM; CLU_002391_0_1_1; -.
DR InParanoid; P33339; -.
DR OMA; HEVAFNL; -.
DR BioCyc; YEAST:G3O-30765-MON; -.
DR Reactome; R-SCE-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SCE-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:P33339; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P33339; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IC:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR039340; Tfc4/TFIIIC-102/Sfc4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR23082; PTHR23082; 1.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1025
FT /note="Transcription factor tau 131 kDa subunit"
FT /id="PRO_0000106364"
FT REPEAT 128..161
FT /note="TPR 1"
FT REPEAT 162..195
FT /note="TPR 2"
FT REPEAT 196..229
FT /note="TPR 3"
FT REPEAT 230..263
FT /note="TPR 4"
FT REPEAT 264..297
FT /note="TPR 5"
FT REPEAT 432..465
FT /note="TPR 6"
FT REPEAT 467..501
FT /note="TPR 7"
FT REPEAT 502..535
FT /note="TPR 8"
FT REPEAT 536..569
FT /note="TPR 9"
FT REPEAT 875..908
FT /note="TPR 10"
FT REPEAT 959..992
FT /note="TPR 11"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..569
FT /note="Sufficient to bind BDP1"
FT REGION 309..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 280
FT /note="I -> T (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 635
FT /note="M -> V (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 1025
FT /note="I -> V (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT MUTAGEN 148
FT /note="E->K: In PCF1-17; increases RNA polymerase III gene
FT transcription."
FT /evidence="ECO:0000269|PubMed:9372943"
FT MUTAGEN 162
FT /note="F->L: In PCF1-12; increases RNA polymerase III gene
FT transcription."
FT /evidence="ECO:0000269|PubMed:9372943"
FT MUTAGEN 162
FT /note="F->S: In PCF1-139; increases RNA polymerase III gene
FT transcription."
FT /evidence="ECO:0000269|PubMed:9372943"
FT MUTAGEN 164
FT /note="A->V: In PCF1-19; increases RNA polymerase III gene
FT transcription."
FT /evidence="ECO:0000269|PubMed:9372943"
FT MUTAGEN 167
FT /note="T->I: In PCF1-2; increases RNA polymerase III gene
FT transcription due to an increase in the recruitment of BRF1
FT to TFIIIC-DNA. No effect on affinity of TFIIIC for DNA."
FT /evidence="ECO:0000269|PubMed:9372943"
FT MUTAGEN 172
FT /note="Y->C: In PCF1-11; increases RNA polymerase III gene
FT transcription."
FT MUTAGEN 188
FT /note="A->T: In PCF1-23; increases RNA polymerase III gene
FT transcription."
FT /evidence="ECO:0000269|PubMed:9372943"
FT MUTAGEN 190
FT /note="H->Y: In PCF1-1; affects the rate of recruitment of
FT TFIIIB to the template. Increases the amount of
FT transcriptionally active TFIIIB. Increases RNA polymerase
FT III gene transcription. Increases the binding affinity for
FT BRF1, but does not affect the binding affinity for BDP1 in
FT the TFIIIC-dependent assembly of TFIIIB. Overcomes
FT autoinhibition of BRF1 binding."
FT /evidence="ECO:0000269|PubMed:12167707,
FT ECO:0000269|PubMed:7488859, ECO:0000269|PubMed:8264649,
FT ECO:0000269|PubMed:9372943"
FT MUTAGEN 192
FT /note="N->L: In PCF1-138; increases RNA polymerase III gene
FT transcription."
FT /evidence="ECO:0000269|PubMed:9372943"
FT MUTAGEN 199
FT /note="W->R: In PCF1-15; increases RNA polymerase III gene
FT transcription."
FT /evidence="ECO:0000269|PubMed:9372943"
FT MUTAGEN 469
FT /note="L->K: RNA polymerase III defective. Defect in the
FT recruitment of BRF1 into TFIIIB-TFIIIC-DNA complexes and
FT diminished direct interaction between TFC4 and BRF1.
FT Decreased binding affinity for BDP1 incorporation into
FT TFIIIB-TFIIIC-DNA complexes and inhibited binary
FT interaction between BDP1 and TFC4."
FT /evidence="ECO:0000269|PubMed:12930823"
FT MUTAGEN 472
FT /note="E->K: RNA polymerase III defective."
FT /evidence="ECO:0000269|PubMed:12930823"
FT MUTAGEN 504
FT /note="V->K: RNA polymerase III defective."
FT /evidence="ECO:0000269|PubMed:12930823"
FT MUTAGEN 541
FT /note="S->I: RNA polymerase III defective."
FT /evidence="ECO:0000269|PubMed:12930823"
FT MUTAGEN 542
FT /note="L->G: RNA polymerase III defective."
FT /evidence="ECO:0000269|PubMed:12930823"
FT MUTAGEN 728
FT /note="R->E: In PCF1-8; increases RNA polymerase III
FT transcription."
FT /evidence="ECO:0000269|PubMed:7488859"
FT MUTAGEN 728
FT /note="R->G: In PCF1-7; increases RNA polymerase III
FT transcription."
FT /evidence="ECO:0000269|PubMed:7488859"
FT MUTAGEN 728
FT /note="R->H: In PCF1-4; increases RNA polymerase III
FT transcription ninefold over wild-type. Increases the amount
FT of transcriptionally active TFIIIB."
FT /evidence="ECO:0000269|PubMed:7488859"
FT MUTAGEN 728
FT /note="R->K: In PCF1-3; increases RNA polymerase III
FT transcription two- to threefold over wild-type. Increases
FT the amount of transcriptionally active TFIIIB."
FT /evidence="ECO:0000269|PubMed:7488859"
FT MUTAGEN 728
FT /note="R->M: In PCF1-5; increases RNA polymerase III
FT transcription."
FT /evidence="ECO:0000269|PubMed:7488859"
FT MUTAGEN 728
FT /note="R->V: In PCF1-6; increases RNA polymerase III
FT transcription."
FT /evidence="ECO:0000269|PubMed:7488859"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 280..303
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 374..387
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 432..444
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 448..455
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 467..479
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 483..490
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 491..495
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:5AIO"
FT HELIX 502..514
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 518..528
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 537..548
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 552..570
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 613..636
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 648..664
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 677..683
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 692..700
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 727..730
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 736..748
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 752..762
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 765..771
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 772..774
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 775..786
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 787..789
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 792..805
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 810..819
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 824..830
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 833..851
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 877..886
FT /evidence="ECO:0007829|PDB:6YJ6"
FT TURN 887..889
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 891..902
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 909..923
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 930..952
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 957..971
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 975..987
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 995..1008
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 1012..1021
FT /evidence="ECO:0007829|PDB:6YJ6"
SQ SEQUENCE 1025 AA; 120229 MW; 12DE18304AAF4862 CRC64;
MAAGKLKKEQ QNQSAERESA DTGKVNDEDE EHLYGNIDDY KHLIQDEEYD DEDVPHDLQL
SEDEYNSERD SSLLAEFSDY GEISEDDEED FMNAIREASN FKVKKKKKND KGKSYGRQRK
ERVLDPEVAQ LLSQANEAFV RNDLQVAERL FNEVIKKDAR NFAAYETLGD IYQLQGRLND
CCNSWFLAAH LNASDWEFWK IVAILSADLD HVRQAIYCFS RVISLNPMEW ESIYRRSMLY
KKTGQLARAL DGFQRLYMYN PYDANILREL AILYVDYDRI EDSIELYMKV FNANVERREA
ILAALENALD SSDEESAAEG EDADEKEPLE QDEDRQMFPD INWKKIDAKY KCIPFDWSSL
NILAELFLKL AVSEVDGIKT IKKCARWIQR RESQTFWDHV PDDSEFDNRR FKNSTFDSLL
AAEKEKSYNI PIDIRVRLGL LRLNTDNLVE ALNHFQCLYD ETFSDVADLY FEAATALTRA
EKYKEAIDFF TPLLSLEEWR TTDVFKPLAR CYKEIESYET AKEFYELAIK SEPDDLDIRV
SLAEVYYRLN DPETFKHMLV DVVEMRKHQV DETLHRISNE KSSNDTSDIS SKPLLEDSKF
RTFRKKKRTP YDAERERIER ERRITAKVVD KYEKMKKFEL NSGLNEAKQA SIWINTVSEL
VDIFSSVKNF FMKSRSRKFV GILRRTKKFN TELDFQIERL SKLAEGDSVF EGPLMEERVT
LTSATELRGL SYEQWFELFM ELSLVIAKYQ SVEDGLSVVE TAQEVNVFFQ DPERVKMMKF
VKLAIVLQMD DEEELAENLR GLLNQFQFNR KVLQVFMYSL CRGPSSLNIL SSTIQQKFFL
RQLKAFDSCR YNTEVNGQAS ITNKEVYNPN KKSSPYLYYI YAVLLYSSRG FLSALQYLTR
LEEDIPDDPM VNLLMGLSHI HRAMQRLTAQ RHFQIFHGLR YLYRYHKIRK SLYTDLEKQE
ADYNLGRAFH LIGLVSIAIE YYNRVLENYD DGKLKKHAAY NSIIIYQQSG NVELADHLME
KYLSI
