UTP22_YEAST
ID UTP22_YEAST Reviewed; 1237 AA.
AC P53254; D6VUM2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=U3 small nucleolar RNA-associated protein 22;
DE Short=U3 snoRNA-associated protein 22;
DE AltName: Full=U three protein 22;
GN Name=UTP22; OrderedLocusNames=YGR090W;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME, AND SUBCELLULAR LOCATION.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-58; THR-60 AND
RP SER-64, AND IDENTIFICATION BY 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).
RN [10]
RP INTERACTION WITH UBP10.
RX PubMed=22902402; DOI=10.1016/j.celrep.2012.07.009;
RA Richardson L.A., Reed B.J., Charette J.M., Freed E.F., Fredrickson E.K.,
RA Locke M.N., Baserga S.J., Gardner R.G.;
RT "A conserved deubiquitinating enzyme controls cell growth by regulating RNA
RT polymerase I stability.";
RL Cell Rep. 2:372-385(2012).
RN [11]
RP INTERACTION WITH UBP10.
RX PubMed=26149687; DOI=10.1074/jbc.m115.650952;
RA Reed B.J., Locke M.N., Gardner R.G.;
RT "A conserved deubiquitinating enzyme uses intrinsically disordered regions
RT to scaffold multiple protein interaction sites.";
RL J. Biol. Chem. 290:20601-20612(2015).
CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA and
CC ribosome assembly. {ECO:0000269|PubMed:15590835}.
CC -!- SUBUNIT: Interacts with snoRNA U3 (PubMed:15590835). Interacts with
CC MPP10 (PubMed:15590835). Component of the ribosomal small subunit (SSU)
CC processome composed of at least 40 protein subunits and snoRNA U3
CC (PubMed:15590835). Interacts with UBP10 (PubMed:22902402,
CC PubMed:26149687). {ECO:0000269|PubMed:15590835,
CC ECO:0000269|PubMed:22902402, ECO:0000269|PubMed:26149687}.
CC -!- INTERACTION:
CC P53254; P15790: CKA1; NbExp=4; IntAct=EBI-1878, EBI-9533;
CC P53254; P43639: CKB1; NbExp=3; IntAct=EBI-1878, EBI-9563;
CC P53254; P38719: DBP8; NbExp=2; IntAct=EBI-1878, EBI-5633;
CC P53254; P36009: DHR2; NbExp=3; IntAct=EBI-1878, EBI-5844;
CC P53254; Q04217: ECM16; NbExp=3; IntAct=EBI-1878, EBI-1820;
CC P53254; P38333: ENP1; NbExp=9; IntAct=EBI-1878, EBI-6482;
CC P53254; Q06344: ESF1; NbExp=2; IntAct=EBI-1878, EBI-34121;
CC P53254; P20448: HCA4; NbExp=3; IntAct=EBI-1878, EBI-5612;
CC P53254; P39520: IFH1; NbExp=6; IntAct=EBI-1878, EBI-9054;
CC P53254; P25586: KRR1; NbExp=3; IntAct=EBI-1878, EBI-21773;
CC P53254; P47083: MPP10; NbExp=4; IntAct=EBI-1878, EBI-11168;
CC P53254; Q06106: MRD1; NbExp=3; IntAct=EBI-1878, EBI-34383;
CC P53254; Q99207: NOP14; NbExp=7; IntAct=EBI-1878, EBI-35157;
CC P53254; P45818: ROK1; NbExp=3; IntAct=EBI-1878, EBI-15686;
CC P53254; Q12481: RRP36; NbExp=2; IntAct=EBI-1878, EBI-31770;
CC P53254; P25368: RRP7; NbExp=7; IntAct=EBI-1878, EBI-16019;
CC P53254; Q06506: RRP9; NbExp=4; IntAct=EBI-1878, EBI-35124;
CC P53254; P53866: SQS1; NbExp=3; IntAct=EBI-1878, EBI-29168;
CC P53254; P40362: UTP18; NbExp=4; IntAct=EBI-1878, EBI-4534;
CC P53254; P35194: UTP20; NbExp=3; IntAct=EBI-1878, EBI-1871;
CC P53254; P40498: UTP25; NbExp=2; IntAct=EBI-1878, EBI-25113;
CC P53254; Q04177: UTP5; NbExp=2; IntAct=EBI-1878, EBI-35844;
CC P53254; Q02354: UTP6; NbExp=6; IntAct=EBI-1878, EBI-22119;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15590835}.
CC -!- MISCELLANEOUS: Present with 3260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NRAP family. {ECO:0000305}.
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DR EMBL; Z72875; CAA97093.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08183.1; -; Genomic_DNA.
DR PIR; S64385; S64385.
DR RefSeq; NP_011604.3; NM_001181219.3.
DR PDB; 4M5D; X-ray; 1.97 A; A=1-1237.
DR PDB; 5WLC; EM; 3.80 A; NH=1-1237.
DR PDB; 5WYJ; EM; 8.70 A; CB=1-1237.
DR PDB; 5WYK; EM; 4.50 A; CB=1-1237.
DR PDB; 6KE6; EM; 3.40 A; RE=1-1237.
DR PDB; 6LQP; EM; 3.20 A; RE=1-1237.
DR PDB; 6LQQ; EM; 4.10 A; RE=1-1237.
DR PDB; 6LQR; EM; 8.60 A; RE=1-1237.
DR PDB; 6LQS; EM; 3.80 A; RE=1-1237.
DR PDB; 6LQT; EM; 4.90 A; RE=1-1237.
DR PDB; 6LQU; EM; 3.70 A; RE=1-1237.
DR PDB; 6ZQA; EM; 4.40 A; UV=1-1237.
DR PDB; 6ZQB; EM; 3.90 A; UV=1-1237.
DR PDB; 6ZQC; EM; 3.80 A; UV=1-1237.
DR PDB; 6ZQD; EM; 3.80 A; UV=1-1237.
DR PDB; 6ZQE; EM; 7.10 A; UV=1-1237.
DR PDB; 6ZQF; EM; 4.90 A; UV=1-1237.
DR PDB; 7AJT; EM; 4.60 A; UV=1-1237.
DR PDB; 7AJU; EM; 3.80 A; UV=1-1237.
DR PDB; 7D4I; EM; 4.00 A; RE=1-1237.
DR PDB; 7D5S; EM; 4.60 A; RE=1-1237.
DR PDB; 7D5T; EM; 6.00 A; RE=1-1237.
DR PDB; 7D63; EM; 12.30 A; RE=1-1237.
DR PDBsum; 4M5D; -.
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; 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; P53254; -.
DR SMR; P53254; -.
DR BioGRID; 33333; 191.
DR ComplexPortal; CPX-771; UTP-C complex variant 2.
DR ComplexPortal; CPX-772; UTP-C complex variant 1.
DR ComplexPortal; CPX-773; UTP-C complex variant 3.
DR ComplexPortal; CPX-774; CURI complex variant 1.
DR ComplexPortal; CPX-775; CURI complex variant 2.
DR ComplexPortal; CPX-776; CURI complex variant 3.
DR DIP; DIP-5304N; -.
DR IntAct; P53254; 111.
DR MINT; P53254; -.
DR STRING; 4932.YGR090W; -.
DR iPTMnet; P53254; -.
DR MaxQB; P53254; -.
DR PaxDb; P53254; -.
DR PRIDE; P53254; -.
DR EnsemblFungi; YGR090W_mRNA; YGR090W; YGR090W.
DR GeneID; 852982; -.
DR KEGG; sce:YGR090W; -.
DR SGD; S000003322; UTP22.
DR VEuPathDB; FungiDB:YGR090W; -.
DR eggNOG; KOG2054; Eukaryota.
DR GeneTree; ENSGT00390000018619; -.
DR HOGENOM; CLU_003502_1_0_1; -.
DR InParanoid; P53254; -.
DR OMA; NPHGGKE; -.
DR BioCyc; YEAST:G3O-30800-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P53254; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53254; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0032545; C:CURI complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0034456; C:UTP-C complex; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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); IC:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IC:ComplexPortal.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR InterPro; IPR005554; NOL6/Upt22.
DR InterPro; IPR035082; Nrap_D1.
DR InterPro; IPR035367; Nrap_D2.
DR InterPro; IPR035368; Nrap_D3.
DR InterPro; IPR035369; Nrap_D4.
DR InterPro; IPR035370; Nrap_D5.
DR InterPro; IPR035371; Nrap_D6.
DR PANTHER; PTHR17972; PTHR17972; 1.
DR Pfam; PF03813; Nrap; 1.
DR Pfam; PF17403; Nrap_D2; 1.
DR Pfam; PF17404; Nrap_D3; 1.
DR Pfam; PF17405; Nrap_D4; 1.
DR Pfam; PF17406; Nrap_D5; 1.
DR Pfam; PF17407; Nrap_D6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..1237
FT /note="U3 small nucleolar RNA-associated protein 22"
FT /id="PRO_0000215651"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 82..114
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 223..245
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 342..355
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 359..372
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 476..479
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 482..499
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 507..511
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 523..530
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 539..542
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 549..555
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 558..574
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 578..586
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 611..619
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 621..625
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 627..633
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 640..649
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 677..689
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 699..706
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 716..718
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 725..742
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 750..755
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 758..761
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 779..786
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 796..817
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 821..827
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 838..843
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 849..855
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 859..869
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 872..874
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 875..889
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 892..903
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 909..922
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 926..928
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 931..943
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 954..967
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 970..972
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1014..1030
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 1034..1036
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 1051..1055
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1058..1078
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1082..1088
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 1097..1103
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 1109..1113
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1136..1142
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1145..1157
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 1158..1160
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 1161..1165
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1169..1172
FT /evidence="ECO:0007829|PDB:4M5D"
FT TURN 1174..1177
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 1179..1186
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1188..1190
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 1204..1214
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1216..1227
FT /evidence="ECO:0007829|PDB:4M5D"
FT HELIX 1228..1230
FT /evidence="ECO:0007829|PDB:4M5D"
FT STRAND 1231..1236
FT /evidence="ECO:0007829|PDB:4M5D"
SQ SEQUENCE 1237 AA; 140485 MW; 9A2B5C885493D7D3 CRC64;
MATSVKRKAS ETSDQNIVKV QKKHSTQDST TDNGSKENDH SSQAINERTV PEQENDESDT
SPESNEVATN TAATRHNGKV TATESYDIHI ARETAELFKS NIFKLQIDEL LEQVKLKQKH
VLKVEKFLHK LYDILQEIPD WEEKSLAEVD SFFKNKIVSV PFVDPKPIPQ NTNYKFNYKK
PDISLIGSFA LKAGIYQPNG SSIDTLLTMP KELFEKKDFL NFRCLHKRSV YLAYLTHHLL
ILLKKDKLDS FLQLEYSYFD NDPLLPILRI SCSKPTGDSL SDYNFYKTRF SINLLIGFPY
KVFEPKKLLP NRNCIRIAQE SKEQSLPATP LYNFSVLSSS THENYLKYLY KTKKQTESFV
EATVLGRLWL QQRGFSSNMS HSGSLGGFGT FEFTILMAAL LNGGGINSNK ILLHGFSSYQ
LFKGVIKYLA TMDLCHDGHL QFHSNPENSS SSPASKYIDE GFQTPTLFDK STKVNILTKM
TVSSYQILKE YAGETLRMLN NVVQDQFSNI FLTNISRFDN LKYDLCYDVQ LPLGKYNNLE
TSLAATFGSM ERVKFITLEN FLAHKITNVA RYALGDRIKY IQIEMVGQKS DFPITKRKVY
SNTGGNHFNF DFVRVKLIVN PSECDKLVTK GPAHSETMST EAAVFKNFWG IKSSLRRFKD
GSITHCCVWS TSSSEPIISS IVNFALQKHV SKKAQISNET IKKFHNFLPL PNLPSSAKTS
VLNLSSFFNL KKSFDDLYKI IFQMKLPLSV KSILPVGSAF RYTSLCQPVP FAYSDPDFFQ
DVILEFETSP KWPDEITSLE KAKTAFLLKI QEELSANSST YRSFFSRDES IPYNLEIVTL
NILTPEGYGF KFRVLTERDE ILYLRAIANA RNELKPELEA TFLKFTAKYL ASVRHTRTLE
NISHSYQFYS PVVRLFKRWL DTHLLLGHIT DELAELIAIK PFVDPAPYFI PGSLENGFLK
VLKFISQWNW KDDPLILDLV KPEDDIRDTF ETSIGAGSEL DSKTMKKLSE RLTLAQYKGI
QMNFTNLRNS DPNGTHLQFF VASKNDPSGI LYSSGIPLPI ATRLTALAKV AVNLLQTHGL
NQQTINLLFT PGLKDYDFVV DLRTPIGLKS SCGILSATEF KNITNDQAPS NFPENLNDLS
EKMDPTYQLV KYLNLKYKNS LILSSRKYIG VNGGEKGDKN VITGLIKPLF KGAHKFRVNL
DCNVKPVDDE NVILNKEAIF HEIAAFGNDM VINFETD
