PWP2_YEAST
ID PWP2_YEAST Reviewed; 923 AA.
AC P25635; D6VR63; P25633; P25636;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Periodic tryptophan protein 2;
DE AltName: Full=U three protein 1;
DE AltName: Full=U3 small nucleolar RNA-associated protein 1;
DE Short=U3 snoRNA-associated protein 1;
GN Name=PWP2; Synonyms=UTP1; OrderedLocusNames=YCR057C;
GN ORFNames=YCR55C/YCR57C/YCR58C;
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 FUNCTION.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8804409; DOI=10.1007/bf02173210;
RA Shafaatian R., Payton M.A., Reid J.D.;
RT "PWP2, a member of the WD-repeat family of proteins, is an essential
RT Saccharomyces cerevisiae gene involved in cell separation.";
RL Mol. Gen. Genet. 252:101-114(1996).
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.
RA Gromadka R.;
RL Submitted (JAN-1996) 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 FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-651; SER-912 AND
RP SER-913, AND IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-651; SER-664;
RP SER-912 AND SER-913, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-232; SER-651;
RP SER-912 AND SER-913, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: Required for bud-site selection and cell separation. Also
CC involved in nucleolar processing of pre-18S ribosomal RNA.
CC {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:8804409}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of
CC the ribosomal small subunit (SSU) processome composed of at least 40
CC protein subunits and snoRNA U3. {ECO:0000269|PubMed:12068309}.
CC -!- INTERACTION:
CC P25635; Q12220: DIP2; NbExp=11; IntAct=EBI-14332, EBI-5896;
CC P25635; P40362: UTP18; NbExp=14; IntAct=EBI-14332, EBI-4534;
CC P25635; Q06078: UTP21; NbExp=15; IntAct=EBI-14332, EBI-359;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}.
CC -!- MISCELLANEOUS: Present with 16700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat PWP2 family. {ECO:0000305}.
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DR EMBL; X78964; CAA55558.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42286.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07532.1; -; Genomic_DNA.
DR PIR; S44226; S44226.
DR RefSeq; NP_009984.1; NM_001178769.1.
DR PDB; 5I2T; X-ray; 2.54 A; A=1-717.
DR PDB; 5WLC; EM; 3.80 A; LO=1-923.
DR PDB; 5WYJ; EM; 8.70 A; BA=1-923.
DR PDB; 5WYK; EM; 4.50 A; BA=1-923.
DR PDB; 6KE6; EM; 3.40 A; B1=1-923.
DR PDB; 6LQP; EM; 3.20 A; B1=1-923.
DR PDB; 6LQQ; EM; 4.10 A; B1=1-923.
DR PDB; 6LQR; EM; 8.60 A; B1=1-923.
DR PDB; 6LQS; EM; 3.80 A; B1=1-900.
DR PDB; 6LQT; EM; 4.90 A; B1=1-923.
DR PDB; 6LQU; EM; 3.70 A; B1=1-923.
DR PDB; 6LQV; EM; 4.80 A; B1=1-923.
DR PDB; 6ND4; EM; 4.30 A; O=1-923.
DR PDB; 6ZQA; EM; 4.40 A; UA=1-923.
DR PDB; 6ZQB; EM; 3.90 A; UA=1-923.
DR PDB; 6ZQC; EM; 3.80 A; UA=1-923.
DR PDB; 6ZQD; EM; 3.80 A; UA=1-923.
DR PDB; 6ZQE; EM; 7.10 A; UA=1-923.
DR PDB; 6ZQF; EM; 4.90 A; UA=1-923.
DR PDB; 7AJT; EM; 4.60 A; UA=1-923.
DR PDB; 7AJU; EM; 3.80 A; UA=1-923.
DR PDB; 7D4I; EM; 4.00 A; B1=1-900.
DR PDB; 7D5S; EM; 4.60 A; B1=1-923.
DR PDB; 7D5T; EM; 6.00 A; B1=1-900.
DR PDB; 7D63; EM; 12.30 A; B1=1-900.
DR PDBsum; 5I2T; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ND4; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P25635; -.
DR SMR; P25635; -.
DR BioGRID; 31035; 236.
DR ComplexPortal; CPX-1410; UTP-B complex.
DR DIP; DIP-1868N; -.
DR IntAct; P25635; 128.
DR MINT; P25635; -.
DR STRING; 4932.YCR057C; -.
DR iPTMnet; P25635; -.
DR MaxQB; P25635; -.
DR PaxDb; P25635; -.
DR PRIDE; P25635; -.
DR EnsemblFungi; YCR057C_mRNA; YCR057C; YCR057C.
DR GeneID; 850422; -.
DR KEGG; sce:YCR057C; -.
DR SGD; S000000653; PWP2.
DR VEuPathDB; FungiDB:YCR057C; -.
DR eggNOG; KOG0291; Eukaryota.
DR GeneTree; ENSGT00550000074981; -.
DR HOGENOM; CLU_010458_0_0_1; -.
DR InParanoid; P25635; -.
DR OMA; QSEQYIM; -.
DR BioCyc; YEAST:G3O-29363-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P25635; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25635; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR027145; PWP2.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR007148; SSU_processome_Utp12.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19858; PTHR19858; 1.
DR Pfam; PF04003; Utp12; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 13.
DR SUPFAM; SSF50978; SSF50978; 2.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; WD repeat.
FT CHAIN 1..923
FT /note="Periodic tryptophan protein 2"
FT /id="PRO_0000051179"
FT REPEAT 12..52
FT /note="WD 1"
FT REPEAT 53..93
FT /note="WD 2"
FT REPEAT 94..132
FT /note="WD 3"
FT REPEAT 144..183
FT /note="WD 4"
FT REPEAT 189..228
FT /note="WD 5"
FT REPEAT 258..297
FT /note="WD 6"
FT REPEAT 300..340
FT /note="WD 7"
FT REPEAT 343..382
FT /note="WD 8"
FT REPEAT 385..424
FT /note="WD 9"
FT REPEAT 428..470
FT /note="WD 10"
FT REPEAT 471..510
FT /note="WD 11"
FT REPEAT 513..552
FT /note="WD 12"
FT REPEAT 575..614
FT /note="WD 13"
FT REPEAT 676..714
FT /note="WD 14"
FT REGION 653..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..890
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 270..273
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 274..288
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 416..419
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 525..543
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 544..547
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 548..554
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 581..585
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 589..595
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 597..605
FT /evidence="ECO:0007829|PDB:5I2T"
FT TURN 606..609
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 681..686
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 690..697
FT /evidence="ECO:0007829|PDB:5I2T"
FT STRAND 700..705
FT /evidence="ECO:0007829|PDB:5I2T"
SQ SEQUENCE 923 AA; 103983 MW; CBEE4720F81378B6 CRC64;
MKSDFKFSNL LGTVYRQGNI TFSDDGKQLL SPVGNRVSVF DLINNKSFTF EYEHRKNIAA
IDLNKQGTLL ISIDEDGRAI LVNFKARNVL HHFNFKEKCS AVKFSPDGRL FALASGRFLQ
IWKTPDVNKD RQFAPFVRHR VHAGHFQDIT SLTWSQDSRF ILTTSKDLSA KIWSVDSEEK
NLAATTFNGH RDYVMGAFFS HDQEKIYTVS KDGAVFVWEF TKRPSDDDDN ESEDDDKQEE
VDISKYSWRI TKKHFFYANQ AKVKCVTFHP ATRLLAVGFT SGEFRLYDLP DFTLIQQLSM
GQNPVNTVSV NQTGEWLAFG SSKLGQLLVY EWQSESYILK QQGHFDSTNS LAYSPDGSRV
VTASEDGKIK VWDITSGFCL ATFEEHTSSV TAVQFAKRGQ VMFSSSLDGT VRAWDLIRYR
NFRTFTGTER IQFNCLAVDP SGEVVCAGSL DNFDIHVWSV QTGQLLDALS GHEGPVSCLS
FSQENSVLAS ASWDKTIRIW SIFGRSQQVE PIEVYSDVLA LSMRPDGKEV AVSTLKGQIS
IFNIEDAKQV GNIDCRKDII SGRFNQDRFT AKNSERSKFF TTIHYSFDGM AIVAGGNNNS
ICLYDVPNEV LLKRFIVSRN MALNGTLEFL NSKKMTEAGS LDLIDDAGEN SDLEDRIDNS
LPGSQRGGDL STRKMRPEVR VTSVQFSPTA NAFAAASTEG LLIYSTNDTI LFDPFDLDVD
VTPHSTVEAL REKQFLNALV MAFRLNEEYL INKVYEAIPI KEIPLVASNI PAIYLPRILK
FIGDFAIESQ HIEFNLIWIK ALLSASGGYI NEHKYLFSTA MRSIQRFIVR VAKEVVNTTT
DNKYTYRFLV STDGSMEDGA ADDDEVLLKD DADEDNEENE ENDVVMESDD EEGWIGFNGK
DNKLPLSNEN DSSDEEENEK ELP
