ERB1_YEAST
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 03-AUG-2022, entry version 184.
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, 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}.
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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; 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 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; 7OHP; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; Q04660; -.
DR SMR; Q04660; -.
DR BioGRID; 35223; 318.
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; Q04660; -.
DR PRIDE; Q04660; -.
DR EnsemblFungi; YMR049C_mRNA; YMR049C; YMR049C.
DR GeneID; 855068; -.
DR KEGG; sce:YMR049C; -.
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 BioCyc; YEAST:G3O-32754-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
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: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; -; 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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17605; PTHR17605; 1.
DR Pfam; PF08145; BOP1NT; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM01035; BOP1NT; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 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 TURN 246..249
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 270..285
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:6EM3"
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 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 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 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 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
