ID PESC_YEAST Reviewed; 605 AA.
AC P53261; D6VUN5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 186.
DE RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000303|PubMed:12022229};
DE AltName: Full=Nucleolar protein 7 {ECO:0000303|PubMed:11911362};
DE AltName: Full=Ribosomal RNA-processing protein 13;
GN Name=NOP7 {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000303|PubMed:11911362};
GN Synonyms=RRP13, YPH1 {ECO:0000303|PubMed:12110181};
GN OrderedLocusNames=YGR103W {ECO:0000312|SGD:S000003335};
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP IDENTIFICATION IN THE NOP7 COMPLEX, ASSOCIATION WITH THE ORC COMPLEX,
RP SUBCELLULAR LOCATION, DELETION PHENOTYPE, INDUCTION, AND MUTAGENESIS OF
RP ILE-380 AND TRP-431.
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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11911362; DOI=10.1017/s1355838202010026;
RA Adams C.C., Jakovljevic J., Roman J., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Saccharomyces cerevisiae nucleolar protein Nop7p is necessary for
RT biogenesis of 60S ribosomal subunits.";
RL RNA 8:150-165(2002).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12022229; DOI=10.1017/s1355838202020022;
RA Oeffinger M., Leung A., Lamond A., Tollervey D.;
RT "Yeast Pescadillo is required for multiple activities during 60S ribosomal
RT subunit synthesis.";
RL RNA 8:626-636(2002).
RN [7]
RP ERRATUM OF PUBMED:12022229.
RA Oeffinger M., Leung A., Lamond A., Tollervey D.;
RL RNA 8:851-851(2002).
RN [8]
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 [9]
RP IDENTIFICATION IN THE NOP7 COMPLEX WITH ERB1 AND YTM1, AND ASSOCIATION OF
RP THE NOP7 COMPLEX 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 [10]
RP INTERACTION WITH NOG1, AND SUBCELLULAR LOCATION.
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND THR-308, AND
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, AND IDENTIFICATION BY
RP 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).
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_03028,
CC ECO:0000269|PubMed:11911362, ECO:0000269|PubMed:12022229,
CC ECO:0000269|PubMed:12110181, 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 (PubMed:16287855).
CC Also interacts with NOG1 (PubMed:16888624). May also associate with the
CC origin recognition complex (ORC complex) (PubMed:12110181).
CC {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:12110181,
CC ECO:0000269|PubMed:16287855, ECO:0000269|PubMed:16888624}.
CC -!- INTERACTION:
CC P53261; P38779: CIC1; NbExp=4; IntAct=EBI-13145, EBI-24538;
CC P53261; Q04660: ERB1; NbExp=10; IntAct=EBI-13145, EBI-28098;
CC P53261; P39744: NOC2; NbExp=3; IntAct=EBI-13145, EBI-29259;
CC P53261; Q02892: NOG1; NbExp=4; IntAct=EBI-13145, EBI-12105;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11911362}.
CC Nucleus, nucleoplasm. Note=Accumulates in the nucleolus in response to
CC rapamycin treatment.
CC -!- INDUCTION: Expression is down-regulated prior to the diauxic shift.
CC {ECO:0000269|PubMed:12110181}.
CC -!- DISRUPTION PHENOTYPE: Essential gene. Reduced assembly of 60S ribosomes
CC and accumulation of halfmer polyribosomes.
CC {ECO:0000269|PubMed:11911362}.
CC -!- MISCELLANEOUS: Present with 4530 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP-
CC Rule:MF_03028}.
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DR EMBL; Z72888; CAA97106.1; -; Genomic_DNA.
DR EMBL; AY693015; AAT93034.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08196.1; -; Genomic_DNA.
DR PIR; S64410; S64410.
DR RefSeq; NP_011617.1; NM_001181232.1.
DR PDB; 3JCT; EM; 3.08 A; n=1-605.
DR PDB; 5Z3G; EM; 3.65 A; M=1-605.
DR PDB; 6C0F; EM; 3.70 A; n=1-605.
DR PDB; 6CB1; EM; 4.60 A; n=1-605.
DR PDB; 6ELZ; EM; 3.30 A; n=1-605.
DR PDB; 6EM1; EM; 3.60 A; n=1-605.
DR PDB; 6EM3; EM; 3.20 A; n=1-605.
DR PDB; 6EM4; EM; 4.10 A; n=1-605.
DR PDB; 6EM5; EM; 4.30 A; n=1-605.
DR PDB; 6FT6; EM; 3.90 A; n=1-605.
DR PDB; 6M62; EM; 3.20 A; n=1-605.
DR PDB; 6YLX; EM; 3.90 A; n=1-605.
DR PDB; 6YLY; EM; 3.80 A; n=1-605.
DR PDB; 7BTB; EM; 3.22 A; n=1-605.
DR PDB; 7NAC; EM; 3.04 A; n=1-605.
DR PDB; 7NAD; EM; 3.04 A; n=1-110.
DR PDB; 7OHP; EM; 3.90 A; n=1-605.
DR PDB; 7OHQ; EM; 3.10 A; n=1-605.
DR PDB; 7OHR; EM; 4.72 A; n=1-605.
DR PDB; 7OHS; EM; 4.38 A; n=1-605.
DR PDB; 7OHV; EM; 3.90 A; n=1-605.
DR PDB; 7OHW; EM; 3.50 A; n=1-605.
DR PDB; 7OHX; EM; 3.30 A; n=1-605.
DR PDB; 7R6Q; EM; 2.98 A; n=1-605.
DR PDB; 7R72; EM; 3.07 A; n=1-110.
DR PDB; 7R7A; EM; 3.04 A; n=1-605.
DR PDB; 7U0H; EM; 2.76 A; n=1-605.
DR PDB; 7UOO; EM; 2.34 A; n=1-605.
DR PDB; 7UQB; EM; 2.43 A; n=1-605.
DR PDB; 7UQZ; EM; 2.44 A; n=1-605.
DR PDB; 7V08; EM; 2.36 A; n=1-605.
DR PDB; 8E5T; EM; 4.00 A; n=1-605.
DR PDBsum; 3JCT; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7NAC; -.
DR PDBsum; 7NAD; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7R6Q; -.
DR PDBsum; 7R72; -.
DR PDBsum; 7R7A; -.
DR PDBsum; 7U0H; -.
DR PDBsum; 7UOO; -.
DR PDBsum; 7UQB; -.
DR PDBsum; 7UQZ; -.
DR PDBsum; 7V08; -.
DR PDBsum; 8E5T; -.
DR AlphaFoldDB; P53261; -.
DR EMDB; EMD-12904; -.
DR EMDB; EMD-12905; -.
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-24286; -.
DR EMDB; EMD-24296; -.
DR EMDB; EMD-30108; -.
DR EMDB; EMD-30174; -.
DR EMDB; EMD-4302; -.
DR EMDB; EMD-6878; -.
DR EMDB; EMD-7324; -.
DR EMDB; EMD-7445; -.
DR SMR; P53261; -.
DR BioGRID; 33346; 290.
DR ComplexPortal; CPX-1862; PeBoW complex.
DR DIP; DIP-6326N; -.
DR IntAct; P53261; 98.
DR MINT; P53261; -.
DR STRING; 4932.YGR103W; -.
DR iPTMnet; P53261; -.
DR MaxQB; P53261; -.
DR PaxDb; 4932-YGR103W; -.
DR PeptideAtlas; P53261; -.
DR EnsemblFungi; YGR103W_mRNA; YGR103W; YGR103W.
DR GeneID; 852995; -.
DR KEGG; sce:YGR103W; -.
DR AGR; SGD:S000003335; -.
DR SGD; S000003335; NOP7.
DR VEuPathDB; FungiDB:YGR103W; -.
DR eggNOG; KOG2481; Eukaryota.
DR GeneTree; ENSGT00390000002626; -.
DR HOGENOM; CLU_019619_1_1_1; -.
DR InParanoid; P53261; -.
DR OMA; QKVTWIV; -.
DR OrthoDB; 169151at2759; -.
DR BioCyc; YEAST:G3O-30813-MONOMER; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 852995; 0 hits in 10 CRISPR screens.
DR PRO; PR:P53261; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53261; Protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA: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:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA 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:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:SGD.
DR GO; GO:0006364; P:rRNA processing; IDA:ComplexPortal.
DR CDD; cd17709; BRCT_pescadillo_like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR HAMAP; MF_03028; Pescadillo; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR010613; PES.
DR PANTHER; PTHR12221; PESCADILLO - RELATED; 1.
DR PANTHER; PTHR12221:SF6; PESCADILLO HOMOLOG; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF06732; Pescadillo_N; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..605
FT /note="Pescadillo homolog"
FT /id="PRO_0000186192"
FT DOMAIN 355..449
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 51..484
FT /note="Sufficient for interaction with ERB1"
FT /evidence="ECO:0000269|PubMed:18448671"
FT REGION 297..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 294..342
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COILED 530..605
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 310..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..513
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 380
FT /note="I->R: Temperature sensitive mutant."
FT /evidence="ECO:0000269|PubMed:12110181"
FT MUTAGEN 431
FT /note="W->R: Temperature sensitive mutant."
FT /evidence="ECO:0000269|PubMed:12110181"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 75..95
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 125..143
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 153..173
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 215..239
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:7R6Q"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:7R6Q"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:7R6Q"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:7R6Q"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:7R6Q"
FT HELIX 561..593
FT /evidence="ECO:0007829|PDB:7R6Q"
SQ SEQUENCE 605 AA; 69877 MW; 131001C956787BE5 CRC64;
MRIKKKNTRG NARNFITRSQ AVRKLQVSLA DFRRLCIFKG IYPREPRNKK KANKGSTAPT
TFYYAKDIQY LMHEPVLAKF REHKTFARKL TRALGRGEVS SAKRLEENRD SYTLDHIIKE
RYPSFPDAIR DIDDALNMLF LFSNLPSTNQ VSSKIINDAQ KICNQWLAYV AKERLVRKVF
VSIKGVYYQA NIKGEEVRWL VPFKFPENIP SDVDFRIMLT FLEFYSTLLH FVLYKLYTDS
GLIYPPKLDL KKDKIISGLS SYILESRQED SLLKLDPTEI EEDVKVESLD ASTLKSALNA
DEANTDETEK EEEQEKKQEK EQEKEQNEET ELDTFEDNNK NKGDILIQPS KYDSPVASLF
SAFVFYVSRE VPIDILEFLI LSCGGNVISE AAMDQIENKK DIDMSKVTHQ IVDRPVLKNK
VAGRTYIQPQ WIFDCINKGE LVPANKYLPG EALPPHLSPW GDAIGYDPTA PVEEGEEEES
ESESESEDQV EEEDQEVVAG EEDDDDDEEL QAQKELELEA QGIKYSETSE ADKDVNKSKN
KKRKVDEEEE EKKLKMIMMS NKQKKLYKKM KYSNAKKEEQ AENLKKKKKQ IAKQKAKLNK
LDSKK
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