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,
GN   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
//