RRP43_YEAST
ID RRP43_YEAST Reviewed; 394 AA.
AC P25359; D6VR45; Q8NKJ5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Exosome complex component RRP43;
DE AltName: Full=Ribosomal RNA-processing protein 43;
GN Name=RRP43; OrderedLocusNames=YCR035C; ORFNames=YCR35C, YCR522;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=1964349; DOI=10.1002/yea.320060609;
RA Thierry A., Fairhead C., Dujon B.;
RT "The complete sequence of the 8.2 kb segment left of MAT on chromosome III
RT reveals five ORFs, including a gene for a yeast ribokinase.";
RL Yeast 6:521-534(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION TO 102 AND 363.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 25-33, FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9390555; DOI=10.1016/s0092-8674(00)80432-8;
RA Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.;
RT "The exosome: a conserved eukaryotic RNA processing complex containing
RT multiple 3'-->5' exoribonucleases.";
RL Cell 91:457-466(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-394.
RX PubMed=1776366; DOI=10.1002/yea.320070711;
RA Wicksteed B.L., Roberts A.B., Sagliocco F.A., Brown A.J.P.;
RT "The complete sequence of a 7.5 kb region of chromosome III from
RT Saccharomyces cerevisiae that lies between CRY1 and MAT.";
RL Yeast 7:761-772(1991).
RN [7]
RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX BY MASS SPECTROMETRY.
RX PubMed=10465791; DOI=10.1101/gad.13.16.2148;
RA Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D.,
RA Mitchell P.;
RT "The yeast exosome and human PM-Scl are related complexes of 3'-->5'
RT exonucleases.";
RL Genes Dev. 13:2148-2158(1999).
RN [8]
RP FUNCTION.
RX PubMed=9973615; DOI=10.1093/nar/27.5.1283;
RA Zanchin N.I., Goldfarb D.S.;
RT "The exosome subunit Rrp43p is required for the efficient maturation of
RT 5.8S, 18S and 25S rRNA.";
RL Nucleic Acids Res. 27:1283-1288(1999).
RN [9]
RP FUNCTION, INTERACTION WITH RRP46, AND MUTAGENESIS OF SER-162; VAL-212;
RP CYS-230; ALA-246; ILE-274 AND CYS-276.
RX PubMed=12364597; DOI=10.1093/nar/gkf545;
RA Oliveira C.C., Gonzales F.A., Zanchin N.I.;
RT "Temperature-sensitive mutants of the exosome subunit Rrp43p show a
RT deficiency in mRNA degradation and no longer interact with the exosome.";
RL Nucleic Acids Res. 30:4186-4198(2002).
RN [10]
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 [11]
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 [12]
RP RECONSTITUTION OF THE RNA EXOSOME COMPLEX, AND LACK OF EXONUCLEASE
RP ACTIVITY.
RX PubMed=17174896; DOI=10.1016/j.cell.2006.10.037;
RA Liu Q., Greimann J.C., Lima C.D.;
RT "Reconstitution, activities, and structure of the eukaryotic RNA exosome.";
RL Cell 127:1223-1237(2006).
RN [13]
RP ERRATUM OF PUBMED:17174896.
RA Liu Q., Greimann J.C., Lima C.D.;
RL Cell 131:188-189(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE RNA EXOSOME COMPLEX,
RP AND SUBUNIT.
RX PubMed=17173052; DOI=10.1038/nsmb1184;
RA Dziembowski A., Lorentzen E., Conti E., Seraphin B.;
RT "A single subunit, Dis3, is essentially responsible for yeast exosome core
RT activity.";
RL Nat. Struct. Mol. Biol. 14:15-22(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Non-catalytic component of the RNA exosome complex which has
CC 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing and degradation events. In the nucleus, the RNA
CC exosome complex is involved in proper maturation of stable RNA species
CC such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC by-products and non-coding 'pervasive' transcripts, such as antisense
CC RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with
CC processing defects, thereby limiting or excluding their export to the
CC cytoplasm. In the cytoplasm, the RNA exosome complex is involved in
CC general mRNA turnover and in RNA surveillance pathways, preventing
CC translation of aberrant mRNAs. The catalytic inactive RNA exosome core
CC complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the
CC binding and presentation of RNA for ribonucleolysis, and to serve as a
CC scaffold for the association with catalytic subunits and accessory
CC proteins or complexes. RRP43 is part of the hexameric ring of RNase PH
CC domain-containing subunits proposed to form a central channel which
CC threads RNA substrates for degradation. {ECO:0000269|PubMed:12364597,
CC ECO:0000269|PubMed:17173052, ECO:0000269|PubMed:9390555,
CC ECO:0000269|PubMed:9973615}.
CC -!- SUBUNIT: Component of the RNA exosome complex. Specifically part of the
CC catalytically inactive RNA exosome core (Exo-9) complex which
CC associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and
CC nuclear-specific RNA exosome complex forms. Exo-9 is formed by a
CC hexameric ring of RNase PH domain-containing subunits and peripheral S1
CC domain-containing components CSL4, RRP4 and RRP40 located on the top of
CC the ring structure. Interacts with NIP7 and NOP8. Interacts strongly
CC with RRP46. {ECO:0000269|PubMed:10465791, ECO:0000269|PubMed:12364597,
CC ECO:0000269|PubMed:17173052, ECO:0000269|PubMed:9390555}.
CC -!- INTERACTION:
CC P25359; P53859: CSL4; NbExp=15; IntAct=EBI-1773, EBI-1731;
CC P25359; Q08962: NIP7; NbExp=5; IntAct=EBI-1773, EBI-12067;
CC P25359; P38768: PIH1; NbExp=2; IntAct=EBI-1773, EBI-24499;
CC P25359; P46948: SKI6; NbExp=4; IntAct=EBI-1773, EBI-1788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:17173052 and PubMed:17174896, only
CC DIS3/RRP44 subunit of the exosome core has exonuclease activity.
CC {ECO:0000305}.
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DR EMBL; X56909; CAA40227.1; -; Genomic_DNA.
DR EMBL; X59720; CAC42984.1; -; Genomic_DNA.
DR EMBL; S78624; AAB21261.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07514.1; -; Genomic_DNA.
DR PIR; S12917; S12917.
DR RefSeq; NP_009964.2; NM_001178749.1.
DR PDB; 4IFD; X-ray; 2.80 A; C=2-394.
DR PDB; 4OO1; X-ray; 3.30 A; C=1-394.
DR PDB; 5C0W; X-ray; 4.60 A; C=1-394.
DR PDB; 5C0X; X-ray; 3.81 A; C=1-394.
DR PDB; 5G06; EM; 4.20 A; C=1-394.
DR PDB; 5JEA; X-ray; 2.65 A; C=1-394.
DR PDB; 5K36; X-ray; 3.10 A; C=1-394.
DR PDB; 5OKZ; X-ray; 3.20 A; C/M/W/g=1-394.
DR PDB; 5VZJ; X-ray; 3.30 A; C=1-394.
DR PDB; 6FSZ; EM; 4.60 A; CC=2-394.
DR PDB; 6LQS; EM; 3.80 A; R3=1-394.
DR PDB; 7AJT; EM; 4.60 A; ED=1-394.
DR PDB; 7AJU; EM; 3.80 A; ED=1-394.
DR PDB; 7D4I; EM; 4.00 A; R3=1-394.
DR PDBsum; 4IFD; -.
DR PDBsum; 4OO1; -.
DR PDBsum; 5C0W; -.
DR PDBsum; 5C0X; -.
DR PDBsum; 5G06; -.
DR PDBsum; 5JEA; -.
DR PDBsum; 5K36; -.
DR PDBsum; 5OKZ; -.
DR PDBsum; 5VZJ; -.
DR PDBsum; 6FSZ; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR AlphaFoldDB; P25359; -.
DR SMR; P25359; -.
DR BioGRID; 31018; 224.
DR ComplexPortal; CPX-599; Nuclear/nucleolar exosome complex, DIS3-RRP6 variant.
DR ComplexPortal; CPX-603; Cytoplasmic exosome complex, DIS3 variant.
DR DIP; DIP-5485N; -.
DR IntAct; P25359; 19.
DR MINT; P25359; -.
DR STRING; 4932.YCR035C; -.
DR iPTMnet; P25359; -.
DR MaxQB; P25359; -.
DR PaxDb; P25359; -.
DR PRIDE; P25359; -.
DR EnsemblFungi; YCR035C_mRNA; YCR035C; YCR035C.
DR GeneID; 850401; -.
DR KEGG; sce:YCR035C; -.
DR SGD; S000000631; RRP43.
DR VEuPathDB; FungiDB:YCR035C; -.
DR eggNOG; KOG1613; Eukaryota.
DR GeneTree; ENSGT00950000183130; -.
DR HOGENOM; CLU_065411_0_0_1; -.
DR InParanoid; P25359; -.
DR OMA; LCWNSLI; -.
DR BioCyc; YEAST:G3O-29348-MON; -.
DR Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P25359; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25359; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:SGD.
DR GO; GO:0000178; C:exosome (RNase complex); IPI:ComplexPortal.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IMP:SGD.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IC:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IMP:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IC:SGD.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IMP:SGD.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IC:SGD.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IC:SGD.
DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0016072; P:rRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0043628; P:small regulatory ncRNA 3'-end processing; IC:SGD.
DR GO; GO:0034473; P:U1 snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 3.30.230.70; -; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR033196; Rrp43.
DR PANTHER; PTHR11097:SF9; PTHR11097:SF9; 1.
DR Pfam; PF01138; RNase_PH; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Exosome;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..394
FT /note="Exosome complex component RRP43"
FT /id="PRO_0000139970"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 162
FT /note="S->F: Interaction with RRP46 abolished; when
FT associated with T-246."
FT /evidence="ECO:0000269|PubMed:12364597"
FT MUTAGEN 212
FT /note="V->A: Interaction with RRP46 abolished."
FT /evidence="ECO:0000269|PubMed:12364597"
FT MUTAGEN 230
FT /note="C->Y: Interaction with RRP46 abolished; when
FT associated with T-274 and Y-276."
FT /evidence="ECO:0000269|PubMed:12364597"
FT MUTAGEN 246
FT /note="A->T: Interaction with RRP46 abolished; when
FT associated with F-162."
FT /evidence="ECO:0000269|PubMed:12364597"
FT MUTAGEN 274
FT /note="I->T: Interaction with RRP46 abolished; when
FT associated with Y-230 and Y-276."
FT /evidence="ECO:0000269|PubMed:12364597"
FT MUTAGEN 276
FT /note="C->Y: Interaction with RRP46 abolished; when
FT associated with Y-230 and T-274."
FT /evidence="ECO:0000269|PubMed:12364597"
FT CONFLICT 102
FT /note="A -> S (in Ref. 1; CAA40227)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="V -> M (in Ref. 1; CAA40227)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4IFD"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:5JEA"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4IFD"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4OO1"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 85..97
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:5K36"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:5K36"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5JEA"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 209..221
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4IFD"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4IFD"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5K36"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:5JEA"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:5JEA"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:5K36"
FT STRAND 357..367
FT /evidence="ECO:0007829|PDB:5JEA"
FT HELIX 371..390
FT /evidence="ECO:0007829|PDB:5JEA"
SQ SEQUENCE 394 AA; 44011 MW; 8801837B8184134D CRC64;
MAESTTLETI EIHPITFPPE VLARISPELS LQRHLSLGIR PCLRKYEEFR DVAIENNTLS
RYADAGNIDT KNNILGSNVL KSGKTIVITS ITGGIIEETS AAIKDLDDFG EEELFEVTKE
EDIIANYASV YPVVEVERGR VGACTDEEMT ISQKLHDSIL HSRILPKKAL KVKAGVRSAN
EDGTFSVLYP DELEDDTLNE TNLKMKRKWS YVLYAKIVVL SRTGPVFDLC WNSLMYALQS
VKLPRAFIDE RASDLRMTIR TRGRSATIRE TYEIICDQTK SVPLMINAKN IAFASNYGIV
ELDPECQLQN SDNSEEEEVD IDMDKLNTVL IADLDTEAEE TSIHSTISIL AAPSGNYKQL
TLVGGGAKIT PEMIKRSLLL SRVRADDLST RFNI
