RPC2_YEAST
ID RPC2_YEAST Reviewed; 1149 AA.
AC P22276; D6W2R3; Q12696;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC2;
DE Short=RNA polymerase III subunit C2;
DE EC=2.7.7.6;
DE AltName: Full=C128;
DE AltName: Full=DNA-directed RNA polymerase III 130 kDa polypeptide;
GN Name=RET1; Synonyms=RPC128, RPC2; OrderedLocusNames=YOR207C;
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=2005101; DOI=10.1016/s0021-9258(19)67639-8;
RA James P., Whelen S., Hall B.D.;
RT "The RET1 gene of yeast encodes the second-largest subunit of RNA
RT polymerase III. Structural analysis of the wild-type and ret1-1 mutant
RT alleles.";
RL J. Biol. Chem. 266:5616-5624(1991).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 Second largest core component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the
CC polymerase catalytic activity and forms the polymerase active center
CC together with the largest subunit. Pol III is composed of mobile
CC elements and RPC2 is part of the core element with the central large
CC cleft and probably a clamp element that moves to open and close the
CC cleft (By similarity). {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1950 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; M38723; AAB59324.1; -; Genomic_DNA.
DR EMBL; Z75115; CAA99422.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10979.1; -; Genomic_DNA.
DR PIR; S67099; S67099.
DR RefSeq; NP_014850.1; NM_001183626.1.
DR PDB; 5FJ8; EM; 3.90 A; B=1-1149.
DR PDB; 5FJ9; EM; 4.60 A; B=1-1149.
DR PDB; 5FJA; EM; 4.65 A; B=1-1149.
DR PDB; 6CNB; EM; 4.10 A; B=1-1149.
DR PDB; 6CNC; EM; 4.10 A; B=1-1149.
DR PDB; 6CND; EM; 4.80 A; B=1-1149.
DR PDB; 6CNF; EM; 4.50 A; B=1-1149.
DR PDB; 6EU0; EM; 4.00 A; B=1-1149.
DR PDB; 6EU1; EM; 3.40 A; B=1-1149.
DR PDB; 6EU2; EM; 3.40 A; B=1-1149.
DR PDB; 6EU3; EM; 3.30 A; B=1-1149.
DR PDB; 6F40; EM; 3.70 A; B=1-1149.
DR PDB; 6F41; EM; 4.30 A; B=1-1149.
DR PDB; 6F42; EM; 5.50 A; B=1-1149.
DR PDB; 6F44; EM; 4.20 A; B=1-1149.
DR PDB; 6TUT; EM; 3.25 A; B=1-1149.
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; P22276; -.
DR SMR; P22276; -.
DR BioGRID; 34602; 364.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-997N; -.
DR IntAct; P22276; 29.
DR MINT; P22276; -.
DR STRING; 4932.YOR207C; -.
DR CarbonylDB; P22276; -.
DR iPTMnet; P22276; -.
DR MaxQB; P22276; -.
DR PaxDb; P22276; -.
DR PRIDE; P22276; -.
DR EnsemblFungi; YOR207C_mRNA; YOR207C; YOR207C.
DR GeneID; 854382; -.
DR KEGG; sce:YOR207C; -.
DR SGD; S000005733; RET1.
DR VEuPathDB; FungiDB:YOR207C; -.
DR eggNOG; KOG0215; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; P22276; -.
DR OMA; LAYCSWC; -.
DR BioCyc; YEAST:G3O-33711-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:P22276; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P22276; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
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; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1149
FT /note="DNA-directed RNA polymerase III subunit RPC2"
FT /id="PRO_0000048096"
FT ZN_FING 1095..1110
FT /note="C4-type"
FT /evidence="ECO:0000250"
FT BINDING 1095
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1098
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 213
FT /note="K -> E (in Ref. 1; AAB59324)"
FT /evidence="ECO:0000305"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 69..73
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 140..152
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:6EU2"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 277..292
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 343..361
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 380..407
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 422..439
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 445..448
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 463..468
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 506..510
FT /evidence="ECO:0007829|PDB:6EU1"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 527..535
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 552..557
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 568..580
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 608..616
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 624..631
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 639..642
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 651..656
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 696..706
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 715..718
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 725..730
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 739..743
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 746..748
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 753..760
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 767..774
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 775..780
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 781..783
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 785..795
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 799..801
FT /evidence="ECO:0007829|PDB:6EU2"
FT STRAND 813..817
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 819..821
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 822..824
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 826..830
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 841..843
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 845..847
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 866..868
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 879..888
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 889..892
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 894..904
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 911..913
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 915..917
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 919..926
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 928..931
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 934..936
FT /evidence="ECO:0007829|PDB:6EU3"
FT STRAND 941..944
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 946..948
FT /evidence="ECO:0007829|PDB:6EU1"
FT TURN 950..953
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 955..970
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 984..994
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1007..1009
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1017..1028
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1031..1033
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1036..1040
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1045..1047
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1053..1057
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1060..1066
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1067..1072
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1076..1083
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1084..1087
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1089..1095
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1096..1098
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1101..1103
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1108..1111
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1112..1122
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 1123..1132
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 1133..1136
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 1138..1147
FT /evidence="ECO:0007829|PDB:6TUT"
SQ SEQUENCE 1149 AA; 129456 MW; 6AC52354F34CF090 CRC64;
MVAATKRRKT HIHKHVKDEA FDDLLKPVYK GKKLTDEINT AQDKWHLLPA FLKVKGLVKQ
HLDSFNYFVD TDLKKIIKAN QLILSDVDPE FYLKYVDIRV GKKSSSSTKD YLTPPHECRL
RDMTYSAPIY VDIEYTRGRN IIMHKDVEIG RMPIMLRSNK CILYDADESK MAKLNECPLD
PGGYFIVNGT EKVILVQEQL SKNRIIVEAD EKKGIVQASV TSSTHERKSK TYVITKNGKI
YLKHNSIAEE IPIAIVLKAC GILSDLEIMQ LVCGNDSSYQ DIFAVNLEES SKLDIYTQQQ
ALEYIGAKVK TMRRQKLTIL QEGIEAIATT VIAHLTVEAL DFREKALYIA MMTRRVVMAM
YNPKMIDDRD YVGNKRLELA GQLISLLFED LFKKFNNDFK LSIDKVLKKP NRAMEYDALL
SINVHSNNIT SGLNRAISTG NWSLKRFKME RAGVTHVLSR LSYISALGMM TRISSQFEKS
RKVSGPRALQ PSQFGMLCTA DTPEGEACGL VKNLALMTHI TTDDEEEPIK KLCYVLGVED
ITLIDSASLH LNYGVYLNGT LIGSIRFPTK FVTQFRHLRR TGKVSEFISI YSNSHQMAVH
IATDGGRICR PLIIVSDGQS RVKDIHLRKL LDGELDFDDF LKLGLVEYLD VNEENDSYIA
LYEKDIVPSM THLEIEPFTI LGAVAGLIPY PHHNQSPRNT YQCAMGKQAI GAIAYNQFKR
IDTLLYLMTY PQQPMVKTKT IELIDYDKLP AGQNATVAVM SYSGYDIEDA LVLNKSSIDR
GFGRCETRRK TTTVLKRYAN HTQDIIGGMR VDENGDPIWQ HQSLGPDGLG EVGMKVQSGQ
IYINKSVPTN SADAPNPNNV NVQTQYREAP VIYRGPEPSH IDQVMMSVSD NDQALIKVLL
RQNRRPELGD KFSSRHGQKG VCGIIVKQED MPFNDQGIVP DIIMNPHGFP SRMTVGKMIE
LISGKAGVLN GTLEYGTCFG GSKLEDMSKI LVDQGFNYSG KDMLYSGITG ECLQAYIFFG
PIYYQKLKHM VLDKMHARAR GPRAVLTRQP TEGRSRDGGL RLGEMERDCV IAYGASQLLL
ERLMISSDAF EVDVCDKCGL MGYSGWCTTC KSAENIIKMT IPYAAKLLFQ ELLSMNIAPR
LRLEDIFQQ
