RPA43_YEAST
ID RPA43_YEAST Reviewed; 326 AA.
AC P46669; D6W335; Q99187;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA43;
DE Short=A43;
DE AltName: Full=DNA-directed DNA-dependent RNA polymerase 36 kDa polypeptide;
GN Name=RPA43; Synonyms=RRN12; OrderedLocusNames=YOR340C; ORFNames=O6271;
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], AND PROTEIN SEQUENCE OF 89-95 AND
RP 265-276.
RX PubMed=7592632; DOI=10.1074/jbc.270.41.24252;
RA Thuriaux P., Mariotte S., Buhler J.-M., Sentenac A., Vu L., Lee B.-S.,
RA Nomura M.;
RT "Gene RPA43 in Saccharomyces cerevisiae encodes an essential subunit of RNA
RT polymerase I.";
RL J. Biol. Chem. 270:24252-24257(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8948102;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1475::aid-yea32>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast
RT chromosome XV reveals 18 open reading frames including a new pyruvate
RT kinase and three homologues to chromosome I genes.";
RL Yeast 12:1475-1481(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH RRN3 AND RRN6.
RX PubMed=11032814; DOI=10.1093/emboj/19.20.5473;
RA Peyroche G., Milkereit P., Bischler N., Tschochner H., Schultz P.,
RA Sentenac A., Carles C., Riva M.;
RT "The recruitment of RNA polymerase I on rDNA is mediated by the interaction
RT of the A43 subunit with Rrn3.";
RL EMBO J. 19:5473-5482(2000).
RN [6]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11717393; DOI=10.1073/pnas.231181398;
RA Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.;
RT "Differential roles of phosphorylation in the formation of transcriptional
RT active RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-251; SER-265;
RP SER-269 AND SER-285, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-285, AND
RP IDENTIFICATION BY 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 [11]
RP ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
RX PubMed=12145213; DOI=10.1093/emboj/cdf392;
RA Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V.,
RA Schultz P.;
RT "Localization of the yeast RNA polymerase I-specific subunits.";
RL EMBO J. 21:4136-4144(2002).
RN [12]
RP IDENTIFICATION IN THE RNA POL I COMPLEX, AND INTERACTION WITH RPA14 AND
RP RPO26.
RX PubMed=12407181; DOI=10.1073/pnas.232580799;
RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A.,
RA Riva M., Carles C.;
RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship
RT to Rpb4-Rpb7 pol II subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
RN [13]
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 [14]
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 [15]
RP FUNCTION.
RX PubMed=12888498; DOI=10.1093/nar/gkg652;
RA Meka H., Daoust G., Arnvig K.B., Werner F., Brick P., Onesti S.;
RT "Structural and functional homology between the RNAP(I) subunits A14/A43
RT and the archaeal RNAP subunits E/F.";
RL Nucleic Acids Res. 31:4391-4400(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-251, STRUCTURE BY ELECTRON
RP MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA
CC precursors. Besides, RNA polymerase I has intrinsic RNA cleavage
CC activity. Through its association with RRN3 is involved in recruitment
CC of Pol I to rDNA promoters. In vitro, the A13-A43 subcomplex binds
CC single-stranded RNA. {ECO:0000269|PubMed:11032814,
CC ECO:0000269|PubMed:12888498, ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8,
CC RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of
CC a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5,
CC RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and
CC RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43
CC form the stalk that mediates interactions with transcription initiation
CC factors and newly synthesized RNA. Interacts with RPO26/ABC23 and with
CC the initiation factor RRN3. {ECO:0000269|PubMed:11032814,
CC ECO:0000269|PubMed:11717393, ECO:0000269|PubMed:12407181,
CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184}.
CC -!- INTERACTION:
CC P46669; P50106: RPA14; NbExp=2; IntAct=EBI-15745, EBI-15750;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Contains an average of four phosphates per molecule.
CC -!- MISCELLANEOUS: Present with 4070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPA43 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; U22949; AAC49076.1; -; Genomic_DNA.
DR EMBL; X95720; CAA65028.1; -; Genomic_DNA.
DR EMBL; Z75248; CAA99664.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11101.1; -; Genomic_DNA.
DR PIR; S67249; S67249.
DR RefSeq; NP_014985.1; NM_001183760.1.
DR PDB; 2RF4; X-ray; 3.10 A; A/C/E=1-251.
DR PDB; 4C2M; X-ray; 2.80 A; 4/G/O/V=1-326.
DR PDB; 4C3H; X-ray; 3.27 A; G=1-326.
DR PDB; 4C3I; X-ray; 3.00 A; G=1-326.
DR PDB; 4C3J; X-ray; 3.35 A; G=1-326.
DR PDB; 4YM7; X-ray; 5.50 A; AG/AO/BG/BO/CG/CO/DG/DO/EG/EO/FG/FO=1-326.
DR PDB; 5G5L; EM; 4.80 A; G=1-326.
DR PDB; 5LMX; EM; 4.90 A; G=1-326.
DR PDB; 5M3F; EM; 3.80 A; G=1-326.
DR PDB; 5M3M; EM; 4.00 A; G=1-326.
DR PDB; 5M5W; EM; 3.80 A; G=1-326.
DR PDB; 5M5X; EM; 4.00 A; G=1-326.
DR PDB; 5M5Y; EM; 4.00 A; G=1-326.
DR PDB; 5M64; EM; 4.60 A; G=1-326.
DR PDB; 5N5Y; EM; 7.70 A; G=1-326.
DR PDB; 5N5Z; EM; 7.70 A; G=1-326.
DR PDB; 5N60; EM; 7.70 A; G=1-326.
DR PDB; 5N61; EM; 3.40 A; G=1-326.
DR PDB; 5OA1; EM; 4.40 A; G=1-326.
DR PDB; 5W5Y; EM; 3.80 A; G=1-326.
DR PDB; 5W64; EM; 4.20 A; G=1-326.
DR PDB; 5W65; EM; 4.30 A; G=1-326.
DR PDB; 5W66; EM; 3.90 A; G=1-326.
DR PDB; 6H67; EM; 3.60 A; G=1-326.
DR PDB; 6H68; EM; 4.60 A; G=1-326.
DR PDB; 6HKO; EM; 3.42 A; G=1-326.
DR PDB; 6HLQ; EM; 3.18 A; G=1-326.
DR PDB; 6HLR; EM; 3.18 A; G=1-326.
DR PDB; 6HLS; EM; 3.21 A; G=1-326.
DR PDB; 6RQH; EM; 3.70 A; G=1-326.
DR PDB; 6RQL; EM; 2.90 A; G=1-326.
DR PDB; 6RQT; EM; 4.00 A; G=1-326.
DR PDB; 6RRD; EM; 3.10 A; G=1-326.
DR PDB; 6RUI; EM; 2.70 A; G=1-326.
DR PDB; 6RUO; EM; 3.50 A; G=1-326.
DR PDB; 6RWE; EM; 3.00 A; G=1-326.
DR PDB; 6TPS; EM; 3.54 A; G=1-326.
DR PDBsum; 2RF4; -.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6HLQ; -.
DR PDBsum; 6HLR; -.
DR PDBsum; 6HLS; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR AlphaFoldDB; P46669; -.
DR SMR; P46669; -.
DR BioGRID; 34723; 161.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR DIP; DIP-5405N; -.
DR IntAct; P46669; 12.
DR MINT; P46669; -.
DR STRING; 4932.YOR340C; -.
DR iPTMnet; P46669; -.
DR MaxQB; P46669; -.
DR PaxDb; P46669; -.
DR PRIDE; P46669; -.
DR EnsemblFungi; YOR340C_mRNA; YOR340C; YOR340C.
DR GeneID; 854518; -.
DR KEGG; sce:YOR340C; -.
DR SGD; S000005867; RPA43.
DR VEuPathDB; FungiDB:YOR340C; -.
DR eggNOG; KOG4134; Eukaryota.
DR GeneTree; ENSGT00390000005553; -.
DR HOGENOM; CLU_060987_0_0_1; -.
DR InParanoid; P46669; -.
DR OMA; HLNPMVM; -.
DR BioCyc; YEAST:G3O-33815-MON; -.
DR Reactome; R-SCE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR EvolutionaryTrace; P46669; -.
DR PRO; PR:P46669; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P46669; protein.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR CDD; cd04328; RNAP_I_Rpa43_N; 1.
DR DisProt; DP01185; -.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR041901; RNAP_I_Rpa43_N.
DR InterPro; IPR041178; RPA43_OB.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR PANTHER; PTHR12709; PTHR12709; 1.
DR Pfam; PF17875; RPA43_OB; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW Transcription.
FT CHAIN 1..326
FT /note="DNA-directed RNA polymerase I subunit RPA43"
FT /id="PRO_0000073960"
FT REGION 179..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 318
FT /note="N -> D (in Ref. 1; AAC49076)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 65..71
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4C2M"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5N61"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:4C3I"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:4C3I"
FT HELIX 273..293
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4C2M"
SQ SEQUENCE 326 AA; 36224 MW; 0CC6421AC3BBC641 CRC64;
MSQVKRANEN RETARFIKKH KKQVTNPIDE KNGTSNCIVR VPIALYVSLA PMYLENPLQG
VMKQHLNPLV MKYNNKVGGV VLGYEGLKIL DADPLSKEDT SEKLIKITPD TPFGFTWCHV
NLYVWQPQVG DVLEGYIFIQ SASHIGLLIH DAFNASIKKN NIPVDWTFVH NDVEEDADVI
NTDENNGNNN NEDNKDSNGG SNSLGKFSFG NRSLGHWVDS NGEPIDGKLR FTVRNVHTTG
RVVSVDGTLI SDADEEGNGY NSSRSQAESL PIVSNKKIVF DDEVSIENKE SHKELDLPEV
KEDNGSEIVY EENTSESNDG ESSDSD
