RPC1_YEAST
ID RPC1_YEAST Reviewed; 1460 AA.
AC P04051; D6W2H5;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC1;
DE Short=RNA polymerase III subunit C1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase III largest subunit;
DE AltName: Full=RNA polymerase III subunit C160;
GN Name=RPO31; Synonyms=RPC1, RPC160; OrderedLocusNames=YOR116C;
GN ORFNames=O3254, YOR3254C;
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].
RX PubMed=3896517; DOI=10.1016/0092-8674(85)90117-5;
RA Allison L.A., Moyle M., Shales M., Ingles C.J.;
RT "Extensive homology among the largest subunits of eukaryotic and
RT prokaryotic RNA polymerases.";
RL Cell 42:599-610(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP MUTAGENESIS.
RX PubMed=8164651; DOI=10.1128/mcb.14.5.2905-2913.1994;
RA Hermann-Ledenmat S., Werner M., Sentenac A., Thuriaux P.;
RT "Suppression of yeast RNA polymerase III mutations by FHL1, a gene coding
RT for a fork head protein involved in rRNA processing.";
RL Mol. Cell. Biol. 14:2905-2913(1994).
RN [7]
RP MUTAGENESIS.
RX PubMed=8599945; DOI=10.1002/j.1460-2075.1996.tb00394.x;
RA Thuillier V., Brun I., Sentenac A., Werner M.;
RT "Mutations in the alpha-amanitin conserved domain of the largest subunit of
RT yeast RNA polymerase III affect pausing, RNA cleavage and transcriptional
RT transitions.";
RL EMBO J. 15:618-629(1996).
RN [8]
RP REVIEW ON THE RNA POL III COMPLEX.
RX PubMed=10384303; DOI=10.1101/sqb.1998.63.381;
RA Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O.,
RA Werner M., Carles C., Sentenac A.;
RT "The yeast RNA polymerase III transcription machinery: a paradigm for
RT eukaryotic gene activation.";
RL Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998).
RN [9]
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 [10]
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 [11]
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).
RN [12]
RP 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
RX PubMed=16818233; DOI=10.1016/j.molcel.2006.05.013;
RA Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P.;
RT "Structural biology of RNA polymerase III: subcomplex C17/25 X-ray
RT structure and 11 subunit enzyme model.";
RL Mol. Cell 23:71-81(2006).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic core component of RNA polymerase III which
CC synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase
CC active center together with the second largest subunit. A single-
CC stranded DNA template strand of the promoter is positioned within the
CC central active site cleft of Pol III. A bridging helix emanates from
CC RPC1 and crosses the cleft near the catalytic site and is thought to
CC promote translocation of Pol III by acting as a ratchet that moves the
CC RNA-DNA hybrid through the active site by switching from straight to
CC bent conformations at each step of nucleotide addition (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits.
CC -!- INTERACTION:
CC P04051; P41910: MAF1; NbExp=4; IntAct=EBI-15810, EBI-10375;
CC P04051; P35718: RPC25; NbExp=3; IntAct=EBI-15810, EBI-15854;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 6020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; X03129; CAA26905.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62123.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64036.1; -; Genomic_DNA.
DR EMBL; Z75024; CAA99314.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10891.1; -; Genomic_DNA.
DR PIR; A00694; RNBY3L.
DR RefSeq; NP_014759.1; NM_001183535.1.
DR PDB; 5FJ8; EM; 3.90 A; A=1-1460.
DR PDB; 5FJ9; EM; 4.60 A; A=1-1460.
DR PDB; 5FJA; EM; 4.65 A; A=1-1460.
DR PDB; 6CNB; EM; 4.10 A; A=1-1460.
DR PDB; 6CNC; EM; 4.10 A; A=1-1460.
DR PDB; 6CND; EM; 4.80 A; A=1-1460.
DR PDB; 6CNF; EM; 4.50 A; A=1-1460.
DR PDB; 6EU0; EM; 4.00 A; A=1-1460.
DR PDB; 6EU1; EM; 3.40 A; A=1-1460.
DR PDB; 6EU2; EM; 3.40 A; A=1-1460.
DR PDB; 6EU3; EM; 3.30 A; A=1-1460.
DR PDB; 6F40; EM; 3.70 A; A=1-1460.
DR PDB; 6F41; EM; 4.30 A; A=1-1460.
DR PDB; 6F42; EM; 5.50 A; A=1-1460.
DR PDB; 6F44; EM; 4.20 A; A=1-1460.
DR PDB; 6TUT; EM; 3.25 A; A=1-1460.
DR PDBsum; 5FJ8; -.
DR PDBsum; 5FJ9; -.
DR PDBsum; 5FJA; -.
DR PDBsum; 6CNB; -.
DR PDBsum; 6CNC; -.
DR PDBsum; 6CND; -.
DR PDBsum; 6CNF; -.
DR PDBsum; 6EU0; -.
DR PDBsum; 6EU1; -.
DR PDBsum; 6EU2; -.
DR PDBsum; 6EU3; -.
DR PDBsum; 6F40; -.
DR PDBsum; 6F41; -.
DR PDBsum; 6F42; -.
DR PDBsum; 6F44; -.
DR PDBsum; 6TUT; -.
DR AlphaFoldDB; P04051; -.
DR SMR; P04051; -.
DR BioGRID; 34512; 279.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-612N; -.
DR IntAct; P04051; 43.
DR MINT; P04051; -.
DR STRING; 4932.YOR116C; -.
DR iPTMnet; P04051; -.
DR MaxQB; P04051; -.
DR PaxDb; P04051; -.
DR PRIDE; P04051; -.
DR EnsemblFungi; YOR116C_mRNA; YOR116C; YOR116C.
DR GeneID; 854283; -.
DR KEGG; sce:YOR116C; -.
DR SGD; S000005642; RPO31.
DR VEuPathDB; FungiDB:YOR116C; -.
DR eggNOG; KOG0261; Eukaryota.
DR GeneTree; ENSGT00930000151028; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; P04051; -.
DR OMA; AVCPPYN; -.
DR BioCyc; YEAST:G3O-33645-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:P04051; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P04051; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IDA:ComplexPortal.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:ComplexPortal.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1460
FT /note="DNA-directed RNA polymerase III subunit RPC1"
FT /id="PRO_0000073953"
FT REGION 858..870
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 506
FT /note="T->I: Temperature-sensitive."
FT MUTAGEN 509
FT /note="N->Y: Temperature-sensitive."
FT MUTAGEN 518
FT /note="N->Q: Temperature-sensitive."
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 144..150
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6EU2"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 284..305
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 309..327
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6EU1"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 368..383
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 396..401
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 485..500
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:6EU3"
FT TURN 505..509
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:6EU1"
FT TURN 537..539
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 544..546
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 556..565
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 573..582
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 583..587
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 606..614
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 637..641
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 651..657
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 677..685
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 687..700
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 705..708
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 714..717
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 723..746
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 758..770
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 773..782
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 790..796
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 797..800
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 803..810
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 818..821
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 827..832
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 842..845
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 852..854
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 858..872
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 876..893
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 911..915
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 916..918
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 923..925
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 928..930
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 931..933
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 935..945
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 949..951
FT /evidence="ECO:0007829|PDB:6EU2"
FT HELIX 956..966
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 967..973
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 979..981
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 986..990
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 992..994
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 999..1024
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1025..1027
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1037..1040
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1049..1053
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1055..1059
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1067..1080
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1089..1098
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1100..1103
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 1111..1115
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 1123..1130
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1144..1146
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1151..1161
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1164..1166
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1167..1169
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1170..1177
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1179..1181
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 1182..1188
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1191..1197
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1202..1212
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1214..1217
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 1219..1221
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1222..1225
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1226..1228
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1229..1234
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1237..1243
FT /evidence="ECO:0007829|PDB:6EU1"
FT TURN 1244..1246
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 1248..1250
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 1251..1254
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 1256..1265
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1270..1274
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1281..1285
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 1287..1289
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 1291..1295
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 1301..1305
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1311..1313
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 1315..1317
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 1319..1326
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1329..1342
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1343..1345
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1353..1361
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1362..1365
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1370..1372
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1373..1379
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1384..1389
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1391..1393
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1394..1396
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1397..1401
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1411..1417
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1424..1427
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1428..1432
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1438..1440
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 1441..1443
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 1448..1455
FT /evidence="ECO:0007829|PDB:6TUT"
SQ SEQUENCE 1460 AA; 162301 MW; D1697EB2352BCA4F CRC64;
MKEVVVSETP KRIKGLEFSA LSAADIVAQS EVEVSTRDLF DLEKDRAPKA NGALDPKMGV
SSSSLECATC HGNLASCHGH FGHLKLALPV FHIGYFKATI QILQGICKNC SAILLSETDK
RQFLHELRRP GVDNLRRMGI LKKILDQCKK QRRCLHCGAL NGVVKKAAAG AGSAALKIIH
DTFRWVGKKS APEKDIWVGE WKEVLAHNPE LERYVKRCMD DLNPLKTLNL FKQIKSADCE
LLGIDATVPS GRPETYIWRY LPAPPVCIRP SVMMQDSPAS NEDDLTVKLT EIVWTSSLIK
AGLDKGISIN NMMEHWDYLQ LTVAMYINSD SVNPAMLPGS SNGGGKVKPI RGFCQRLKGK
QGRFRGNLSG KRVDFSGRTV ISPDPNLSID EVAVPDRVAK VLTYPEKVTR YNRHKLQELI
VNGPNVHPGA NYLLKRNEDA RRNLRYGDRM KLAKNLQIGD VVERHLEDGD VVLFNRQPSL
HRLSILSHYA KIRPWRTFRL NECVCTPYNA DFDGDEMNLH VPQTEEARAE AINLMGVKNN
LLTPKSGEPI IAATQDFITG SYLISHKDSF YDRATLTQLL SMMSDGIEHF DIPPPAIMKP
YYLWTGKQVF SLLIKPNHNS PVVINLDAKN KVFVPPKSKS LPNEMSQNDG FVIIRGSQIL
SGVMDKSVLG DGKKHSVFYT ILRDYGPQEA ANAMNRMAKL CARFLGNRGF SIGINDVTPA
DDLKQKKEEL VEIAYHKCDE LITLFNKGEL ETQPGCNEEQ TLEAKIGGLL SKVREEVGDV
CINELDNWNA PLIMATCGSK GSTLNVSQMV AVVGQQIISG NRVPDGFQDR SLPHFPKNSK
TPQSKGFVRN SFFSGLSPPE FLFHAISGRE GLVDTAVKTA ETGYMSRRLM KSLEDLSCQY
DNTVRTSANG IVQFTYGGDG LDPLEMEGNA QPVNFNRSWD HAYNITFNNQ DKGLLPYAIM
ETANEILGPL EERLVRYDNS GCLVKREDLN KAEYVDQYDA ERDFYHSLRE YINGKATALA
NLRKSRGMLG LLEPPAKELQ GIDPDETVPD NVKTSVSQLY RISEKSVRKF LEIALFKYRK
ARLEPGTAIG AIGAQSIGEP GTQMTLKTFH FAGVASMNVT LGVPRIKEII NASKVISTPI
INAVLVNDND ERAARVVKGR VEKTLLSDVA FYVQDVYKDN LSFIQVRIDL GTIDKLQLEL
TIEDIAVAIT RASKLKIQAS DVNIIGKDRI AINVFPEGYK AKSISTSAKE PSENDVFYRM
QQLRRALPDV VVKGLPDISR AVINIRDDGK RELLVEGYGL RDVMCTDGVI GSRTTTNHVL
EVFSVLGIEA ARYSIIREIN YTMSNHGMSV DPRHIQLLGD VMTYKGEVLG ITRFGLSKMR
DSVLQLASFE KTTDHLFDAA FYMKKDAVEG VSECIILGQT MSIGTGSFKV VKGTNISEKD
LVPKRCLFES LSNEAALKAN
