ID ERB1_YEAST Reviewed; 807 AA. AC Q04660; D6VZM4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=Ribosome biogenesis protein ERB1 {ECO:0000255|HAMAP-Rule:MF_03027}; DE AltName: Full=Eukaryotic ribosome biogenesis protein 1 {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000303|PubMed:11522832}; GN Name=ERB1 {ECO:0000255|HAMAP-Rule:MF_03027, GN ECO:0000303|PubMed:11522832}; GN OrderedLocusNames=YMR049C {ECO:0000312|SGD:S000004652}; GN ORFNames=YM9796.02C; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [2] 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 [3] RP FUNCTION. RX PubMed=11522832; DOI=10.1093/nar/29.17.3621; RA Pestov D.G., Stockelman M.G., Strezoska Z., Lau L.F.; RT "ERB1, the yeast homolog of mammalian Bop1, is an essential gene required RT for maturation of the 25S and 5.8S ribosomal RNAs."; RL Nucleic Acids Res. 29:3621-3630(2001). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE NOP7 RP COMPLEX. RX PubMed=12110181; DOI=10.1016/s0092-8674(02)00773-0; RA Du Y.-C.N., Stillman B.; RT "Yph1p, an ORC-interacting protein: potential links between cell RT proliferation control, DNA replication, and ribosome biogenesis."; RL Cell 109:835-848(2002). RN [5] 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 [6] RP IDENTIFICATION IN THE NOP7 COMPLEX, AND ASSOCIATION OF THE NOP7 COMPLEX RP WITH 66S PRE-RIBOSOMES. RX PubMed=16287855; DOI=10.1128/mcb.25.23.10419-10432.2005; RA Miles T.D., Jakovljevic J., Horsey E.W., Harnpicharnchai P., Tang L., RA Woolford J.L. Jr.; RT "Ytm1, Nop7, and Erb1 form a complex necessary for maturation of yeast 66S RT preribosomes."; RL Mol. Cell. Biol. 25:10419-10432(2005). RN [7] RP INTERACTION WITH NOG1. RX PubMed=16888624; DOI=10.1038/sj.emboj.7601262; RA Honma Y., Kitamura A., Shioda R., Maruyama H., Ozaki K., Oda Y., Mini T., RA Jenoe P., Maki Y., Yonezawa K., Hurt E., Ueno M., Uritani M., Hall M.N., RA Ushimaru T.; RT "TOR regulates late steps of ribosome maturation in the nucleoplasm via RT Nog1 in response to nutrients."; RL EMBO J. 25:3832-3842(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-418, AND RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-72 AND SER-76, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [10] RP FUNCTION, CHARACTERIZATION OF THE NOP7 COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=18448671; DOI=10.1091/mbc.e07-12-1281; RA Tang L., Sahasranaman A., Jakovljevic J., Schleifman E., Woolford J.L. Jr.; RT "Interactions among Ytm1, Erb1, and Nop7 required for assembly of the Nop7- RT subcomplex in yeast preribosomes."; RL Mol. Biol. Cell 19:2844-2856(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-146; SER-149 AND RP SER-418, AND IDENTIFICATION BY 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 [12] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-127, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [13] RP INTERACTION WITH YTM1, AND MUTAGENESIS OF ARG-470. RX PubMed=26476442; DOI=10.1093/nar/gkv1043; RA Wegrecki M., Rodriguez-Galan O., de la Cruz J., Bravo J.; RT "The structure of Erb1-Ytm1 complex reveals the functional importance of a RT high-affinity binding between two beta-propellers during the assembly of RT large ribosomal subunits in eukaryotes."; RL Nucleic Acids Res. 43:11017-11030(2015). RN [14] RP INTERACTION WITH YTM1, AND MUTAGENESIS OF GLU-465; ARG-470 AND GLU-790. RX PubMed=26657628; DOI=10.1093/nar/gkv1365; RA Thoms M., Ahmed Y.L., Maddi K., Hurt E., Sinning I.; RT "Concerted removal of the Erb1-Ytm1 complex in ribosome biogenesis relies RT on an elaborate interface."; RL Nucleic Acids Res. 44:926-939(2016). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS). RX PubMed=25880847; DOI=10.1371/journal.pone.0123463; RA Wegrecki M., Neira J.L., Bravo J.; RT "The carboxy-terminal domain of Erb1 is a seven-bladed ss-propeller that RT binds RNA."; RL PLoS ONE 10:E0123463-E0123463(2015). CC -!- FUNCTION: Component of the NOP7 complex, which is required for CC maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03027, CC ECO:0000269|PubMed:11522832, ECO:0000269|PubMed:18448671}. CC -!- SUBUNIT: Component of the NOP7 complex, composed of ERB1, NOP7 and CC YTM1. The complex is held together by ERB1, which interacts with NOP7 CC via its N-terminal domain and with YTM1 via a high-affinity interaction CC between the seven-bladed beta-propeller domains of the 2 proteins. The CC NOP7 complex associates with the 66S pre-ribosome. Also interacts with CC NOG1. {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:12110181, CC ECO:0000269|PubMed:16287855, ECO:0000269|PubMed:16888624}. CC -!- INTERACTION: CC Q04660; P32892: DRS1; NbExp=4; IntAct=EBI-28098, EBI-6170; CC Q04660; Q03532: HAS1; NbExp=5; IntAct=EBI-28098, EBI-8170; CC Q04660; P39744: NOC2; NbExp=8; IntAct=EBI-28098, EBI-29259; CC Q04660; Q02892: NOG1; NbExp=4; IntAct=EBI-28098, EBI-12105; CC Q04660; P53261: NOP7; NbExp=10; IntAct=EBI-28098, EBI-13145; CC Q04660; P34241: URB1; NbExp=3; IntAct=EBI-28098, EBI-26595; CC Q04660; Q12024: YTM1; NbExp=12; IntAct=EBI-28098, EBI-29589; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP- CC Rule:MF_03027, ECO:0000269|PubMed:18448671}. Nucleus, nucleoplasm CC {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:18448671}. CC -!- MISCELLANEOUS: Present with 2680 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family. CC {ECO:0000255|HAMAP-Rule:MF_03027}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z49703; CAA89759.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09948.1; -; Genomic_DNA. DR PIR; S54549; S54549. DR RefSeq; NP_013764.1; NM_001182546.1. DR PDB; 4U7A; X-ray; 1.60 A; A=1-807. DR PDB; 6C0F; EM; 3.70 A; s=1-807. DR PDB; 6CB1; EM; 4.60 A; s=239-298, s=372-807. DR PDB; 6ELZ; EM; 3.30 A; m=1-807. DR PDB; 6EM1; EM; 3.60 A; m=1-807. DR PDB; 6EM3; EM; 3.20 A; B=1-807. DR PDB; 6EM4; EM; 4.10 A; H=1-807. DR PDB; 6EM5; EM; 4.30 A; m=1-807. DR PDB; 7NAC; EM; 3.04 A; m=1-807. DR PDB; 7NAD; EM; 3.04 A; m=392-807. DR PDB; 7OHP; EM; 3.90 A; m=1-807. DR PDB; 7OHR; EM; 4.72 A; m=1-807. DR PDB; 7OHS; EM; 4.38 A; m=1-807. DR PDB; 7OHV; EM; 3.90 A; m=1-807. DR PDB; 7OHW; EM; 3.50 A; m=1-807. DR PDB; 7OHX; EM; 3.30 A; m=1-807. DR PDB; 7R6K; EM; 3.17 A; m=1-807. DR PDB; 7R6Q; EM; 2.98 A; m=1-807. DR PDB; 7R72; EM; 3.07 A; m=392-807. DR PDB; 7R7A; EM; 3.04 A; m=1-807. DR PDB; 7R7C; EM; 3.71 A; m=153-215. DR PDB; 8E5T; EM; 4.00 A; s=1-807. DR PDBsum; 4U7A; -. DR PDBsum; 6C0F; -. DR PDBsum; 6CB1; -. DR PDBsum; 6ELZ; -. DR PDBsum; 6EM1; -. DR PDBsum; 6EM3; -. DR PDBsum; 6EM4; -. DR PDBsum; 6EM5; -. DR PDBsum; 7NAC; -. DR PDBsum; 7NAD; -. DR PDBsum; 7OHP; -. DR PDBsum; 7OHR; -. DR PDBsum; 7OHS; -. DR PDBsum; 7OHV; -. DR PDBsum; 7OHW; -. DR PDBsum; 7OHX; -. DR PDBsum; 7R6K; -. DR PDBsum; 7R6Q; -. DR PDBsum; 7R72; -. DR PDBsum; 7R7A; -. DR PDBsum; 7R7C; -. DR PDBsum; 8E5T; -. DR AlphaFoldDB; Q04660; -. DR EMDB; EMD-12904; -. DR EMDB; EMD-12906; -. DR EMDB; EMD-12907; -. DR EMDB; EMD-12910; -. DR EMDB; EMD-12911; -. DR EMDB; EMD-12912; -. DR EMDB; EMD-24269; -. DR EMDB; EMD-24280; -. DR EMDB; EMD-24286; -. DR EMDB; EMD-24296; -. DR EMDB; EMD-7324; -. DR EMDB; EMD-7445; -. DR SMR; Q04660; -. DR BioGRID; 35223; 339. DR ComplexPortal; CPX-1862; PeBoW complex. DR DIP; DIP-3970N; -. DR IntAct; Q04660; 111. DR MINT; Q04660; -. DR STRING; 4932.YMR049C; -. DR iPTMnet; Q04660; -. DR MaxQB; Q04660; -. DR PaxDb; 4932-YMR049C; -. DR PeptideAtlas; Q04660; -. DR EnsemblFungi; YMR049C_mRNA; YMR049C; YMR049C. DR GeneID; 855068; -. DR KEGG; sce:YMR049C; -. DR AGR; SGD:S000004652; -. DR SGD; S000004652; ERB1. DR VEuPathDB; FungiDB:YMR049C; -. DR eggNOG; KOG0650; Eukaryota. DR GeneTree; ENSGT00390000018422; -. DR HOGENOM; CLU_011390_0_1_1; -. DR InParanoid; Q04660; -. DR OMA; MRPAKGE; -. DR OrthoDB; 5472008at2759; -. DR BioCyc; YEAST:G3O-32754-MONOMER; -. DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR BioGRID-ORCS; 855068; 9 hits in 10 CRISPR screens. DR PRO; PR:Q04660; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q04660; Protein. DR GO; GO:0005730; C:nucleolus; HDA:SGD. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0070545; C:PeBoW complex; IDA:SGD. DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD. DR GO; GO:0003677; F:DNA binding; EXP:DisProt. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:GO_Central. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central. DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule. DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:ComplexPortal. DR GO; GO:0006364; P:rRNA processing; IDA:ComplexPortal. DR DisProt; DP00900; -. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR HAMAP; MF_03027; BOP1; 1. DR InterPro; IPR028598; BOP1/Erb1. DR InterPro; IPR012953; BOP1_N_dom. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR17605:SF0; RIBOSOME BIOGENESIS PROTEIN BOP1; 1. DR PANTHER; PTHR17605; RIBOSOME BIOGENESIS PROTEIN BOP1 BLOCK OF PROLIFERATION 1 PROTEIN; 1. DR Pfam; PF08145; BOP1NT; 1. DR Pfam; PF00400; WD40; 3. DR SMART; SM01035; BOP1NT; 1. DR SMART; SM00320; WD40; 5. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. PE 1: Evidence at protein level; KW 3D-structure; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Ribosome biogenesis; rRNA processing; Ubl conjugation; WD repeat. FT CHAIN 1..807 FT /note="Ribosome biogenesis protein ERB1" FT /id="PRO_0000050968" FT REPEAT 435..474 FT /note="WD 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027" FT REPEAT 483..523 FT /note="WD 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027" FT REPEAT 592..634 FT /note="WD 3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027" FT REPEAT 637..675 FT /note="WD 4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027" FT REPEAT 678..717 FT /note="WD 5" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027" FT REPEAT 721..760 FT /note="WD 6" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027" FT REPEAT 776..807 FT /note="WD 7" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027" FT REGION 1..108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 265..383 FT /note="Required for interaction with NOP7" FT /evidence="ECO:0000269|PubMed:18448671" FT REGION 383..419 FT /note="Required for interaction with YTM1" FT /evidence="ECO:0000269|PubMed:18448671" FT COMPBIAS 41..58 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 86..100 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956" FT MOD_RES 72 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 149 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 418 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956" FT CROSSLNK 127 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 465 FT /note="E->R: Disrupts the interaction with YTM1 and cannot FT sustain growth." FT /evidence="ECO:0000269|PubMed:26476442, FT ECO:0000269|PubMed:26657628" FT MUTAGEN 470 FT /note="R->E: Weakens the interaction with YTM1, impairs FT pre-rRNA processing and leads to a deficiency in 60S FT ribosomal subunits. Disrupts the interaction with YTM1 and FT cannot sustain growth; when associated with R-790." FT /evidence="ECO:0000269|PubMed:26476442, FT ECO:0000269|PubMed:26657628" FT MUTAGEN 790 FT /note="E->R: Disrupts the interaction with YTM1 and cannot FT sustain growth; when associated with E-470." FT /evidence="ECO:0000269|PubMed:26657628" FT HELIX 162..165 FT /evidence="ECO:0007829|PDB:7R6K" FT STRAND 168..173 FT /evidence="ECO:0007829|PDB:7R6K" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:7R6K" FT HELIX 188..196 FT /evidence="ECO:0007829|PDB:7R6K" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:7R6K" FT STRAND 208..215 FT /evidence="ECO:0007829|PDB:7R6K" FT HELIX 218..228 FT /evidence="ECO:0007829|PDB:7R6K" FT TURN 246..249 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 271..284 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 291..297 FT /evidence="ECO:0007829|PDB:7R6Q" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 348..356 FT /evidence="ECO:0007829|PDB:7R6Q" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 363..366 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 381..383 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 384..396 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 399..405 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 409..412 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 419..422 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 428..433 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 440..445 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 451..456 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 459..465 FT /evidence="ECO:0007829|PDB:4U7A" FT TURN 466..468 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 471..476 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 488..493 FT /evidence="ECO:0007829|PDB:4U7A" FT TURN 497..499 FT /evidence="ECO:0007829|PDB:7NAD" FT STRAND 502..506 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 509..513 FT /evidence="ECO:0007829|PDB:4U7A" FT HELIX 520..532 FT /evidence="ECO:0007829|PDB:4U7A" FT TURN 570..572 FT /evidence="ECO:0007829|PDB:7NAD" FT STRAND 573..576 FT /evidence="ECO:0007829|PDB:4U7A" FT HELIX 580..583 FT /evidence="ECO:0007829|PDB:4U7A" FT TURN 584..586 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 587..595 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 599..602 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 606..612 FT /evidence="ECO:0007829|PDB:4U7A" FT HELIX 617..619 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 620..625 FT /evidence="ECO:0007829|PDB:4U7A" FT HELIX 626..628 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 630..632 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 634..636 FT /evidence="ECO:0007829|PDB:7NAD" FT STRAND 642..647 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 649..660 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 662..666 FT /evidence="ECO:0007829|PDB:4U7A" FT TURN 667..670 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 671..676 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 683..688 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 692..699 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 704..708 FT /evidence="ECO:0007829|PDB:4U7A" FT TURN 709..711 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 716..719 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 726..731 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 733..742 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 747..753 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 756..759 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 763..770 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 776..778 FT /evidence="ECO:0007829|PDB:7NAD" FT STRAND 781..786 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 788..791 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 793..797 FT /evidence="ECO:0007829|PDB:4U7A" FT STRAND 802..806 FT /evidence="ECO:0007829|PDB:4U7A" SQ SEQUENCE 807 AA; 91705 MW; 6542DFE4670341CA CRC64; MMAKNNKTTE AKMSKKRAAS EESDVEEDED KLLSVDGLID AEASESDEDD DEYESAVEEK ESSSDKEAQD DSDDDSDAEL NKLLAEEEGD GEEDYDSSEF SDDTTSLTDR LSGVKLQTIV DPNIYSKYAD GSDRIIKPEI NPVYDSDDSD AETQNTIGNI PLSAYDEMPH IGYDINGKRI MRPAKGSALD QLLDSIELPE GWTGLLDKNS GSSLNLTKEE LELISKIQRN EQTDDSINPY EPLIDWFTRH EEVMPLTAVP EPKRRFVPSK NEAKRVMKIV RAIREGRIIP PKKLKEMKEK EKIENYQYDL WGDSTETNDH VMHLRAPKLP PPTNEESYNP PEEYLLSPEE KEAWENTEYS ERERNFIPQK YSALRKVPGY GESIRERFER SLDLYLAPRV RKNKLNIDPN SLIPELPSPK DLRPFPIRCS TIYAGHKGKV RTLSIDPSGL WLATGSDDGT VRVWEILTGR EVYRTTLIDD EENPDYHIEC IEWNPDANNG ILAVAVGENI HLIVPPIFGY DIENNGKTKI EDGFGYDTFG TVKKSNLEVN ENGDGDEDGE NESAKNAVKK QVAQWNKPSQ KQLEKDICIT ISCKKTVKKL SWHRKGDYFV TVQPDSGNTS VLIHQVSKHL TQSPFKKSKG IIMDAKFHPF KPQLFVCSQR YVRIYDLSQQ ILVKKLLPGA RWLSKIDIHP RGDNLIASSF DKRVLWHDLD LASTPYKTLR YHEKAVRSVN FHKKLPLFSS AADDGTIHVF HATVYDDMMK NPMIVPLKKL TGHKVINSLG VLDAIWHPRE AWLFSAGADN TARLWTT //