ID UTP10_YEAST Reviewed; 1769 AA. AC P42945; D6VW75; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 193. DE RecName: Full=U3 small nucleolar RNA-associated protein 10; DE Short=U3 snoRNA-associated protein 10; DE AltName: Full=U three protein 10; DE AltName: Full=U3 protein 10 required for transcription; DE AltName: Full=t-UTP10; GN Name=UTP10; OrderedLocusNames=YJL109C; ORFNames=J0808; 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 [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=7483851; DOI=10.1002/yea.320110909; RA Rasmussen S.W.; RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the RT DAL80 gene, and a tRNA(Arg)."; RL Yeast 11:873-883(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."; RL EMBO J. 15:2031-2049(1996). RN [3] 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 [4] RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU RP PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=12068309; DOI=10.1038/nature00769; RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M., RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J., RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.; RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA RT biogenesis."; RL Nature 417:967-970(2002). RN [5] 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 [6] 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 [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=14576278; DOI=10.1073/pnas.2135385100; RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., RA Pfanner N., Meisinger C.; RT "The proteome of Saccharomyces cerevisiae mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003). RN [8] RP FUNCTION, IDENTIFICATION IN COMPLEX WITH OTHER T-UTPS, AND SUBCELLULAR RP LOCATION. RX PubMed=15489292; DOI=10.1101/gad.1226604; RA Gallagher J.E.G., Dunbar D.A., Granneman S., Mitchell B.M., Osheim Y., RA Beyer A.L., Baserga S.J.; RT "RNA polymerase I transcription and pre-rRNA processing are linked by RT specific SSU processome components."; RL Genes Dev. 18:2506-2517(2004). RN [9] RP FUNCTION. RX PubMed=16544271; DOI=10.1002/yea.1353; RA Wade C.H., Umbarger M.A., McAlear M.A.; RT "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains RT over 200 genes."; RL Yeast 23:293-306(2006). RN [10] RP FUNCTION, INTERACTION WITH SNORNA U3 AND PRE-RIBOSOMAL RNA, AND SUBCELLULAR RP LOCATION. RX PubMed=17652137; DOI=10.1261/rna.609807; RA Dez C., Dlakic M., Tollervey D.; RT "Roles of the HEAT repeat proteins Utp10 and Utp20 in 40S ribosome RT maturation."; RL RNA 13:1516-1527(2007). RN [11] 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. CC Required for optimal pre-ribosomal RNA transcription by RNA polymerase CC I together with a subset of U3 proteins required for transcription (t- CC UTPs). Involved in ribosome biosynthesis. {ECO:0000269|PubMed:12068309, CC ECO:0000269|PubMed:15489292, ECO:0000269|PubMed:16544271, CC ECO:0000269|PubMed:17652137}. CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of CC the ribosomal small subunit (SSU) processome composed of at least 40 CC protein subunits and snoRNA U3. In the absence of snoRNA3, forms a CC complex with other t-UTPs. This complex can associate with pre-18S CC ribosomal RNAs. {ECO:0000269|PubMed:12068309, CC ECO:0000269|PubMed:15489292, ECO:0000269|PubMed:17652137}. CC -!- INTERACTION: CC P42945; P47083: MPP10; NbExp=8; IntAct=EBI-1884, EBI-11168; CC P42945; Q02931: NAN1; NbExp=8; IntAct=EBI-1884, EBI-37773; CC P42945; Q06512: NOC4; NbExp=4; IntAct=EBI-1884, EBI-36459; CC P42945; Q05022: RRP5; NbExp=5; IntAct=EBI-1884, EBI-16011; CC P42945; Q06679: UTP4; NbExp=5; IntAct=EBI-1884, EBI-35712; CC P42945; Q04177: UTP5; NbExp=3; IntAct=EBI-1884, EBI-35844; CC P42945; P40055: UTP7; NbExp=7; IntAct=EBI-1884, EBI-22597; CC P42945; P53276: UTP8; NbExp=5; IntAct=EBI-1884, EBI-23301; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Mitochondrion. CC Note=Associated with ribosomal chromatin, even in the absence of CC transcription. CC -!- MISCELLANEOUS: Present with 18200 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the HEATR1/UTP10 family. {ECO:0000305}. 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; X85021; CAA59385.1; -; Genomic_DNA. DR EMBL; Z49384; CAA89404.1; -; Genomic_DNA. DR EMBL; BK006943; DAA08691.1; -; Genomic_DNA. DR PIR; S53378; S53378. DR RefSeq; NP_012426.1; NM_001181542.1. DR PDB; 5WLC; EM; 3.80 A; LM=1-1769. DR PDB; 5WYJ; EM; 8.70 A; AE=1-808. DR PDB; 5WYK; EM; 4.50 A; AE=1-1769. DR PDB; 6KE6; EM; 3.40 A; AE=1-1769. DR PDB; 6LQP; EM; 3.20 A; AE=1-1769. DR PDB; 6LQQ; EM; 4.10 A; AE=1-1769. DR PDB; 6LQR; EM; 8.60 A; AE=1-1769. DR PDB; 6LQS; EM; 3.80 A; AE=1-1769. DR PDB; 6LQT; EM; 4.90 A; AE=1-1769. DR PDB; 6LQU; EM; 3.70 A; AE=1-1769. DR PDB; 6LQV; EM; 4.80 A; AE=1-1769. DR PDB; 6ND4; EM; 4.30 A; M=1-1769. DR PDB; 6ZQA; EM; 4.40 A; UJ=1-1769. DR PDB; 6ZQB; EM; 3.90 A; UJ=1-1769. DR PDB; 6ZQC; EM; 3.80 A; UJ=1-1769. DR PDB; 6ZQD; EM; 3.80 A; UJ=1-1769. DR PDB; 6ZQE; EM; 7.10 A; UJ=1-1769. DR PDB; 7AJT; EM; 4.60 A; UJ=1-1769. DR PDB; 7AJU; EM; 3.80 A; UJ=1-1769. DR PDB; 7D4I; EM; 4.00 A; AE=1-1769. DR PDB; 7D5S; EM; 4.60 A; AE=1-1769. DR PDB; 7D5T; EM; 6.00 A; AE=1-1769. DR PDB; 7D63; EM; 12.30 A; AE=1-1769. DR PDB; 7SUK; EM; 3.99 A; LM=2-426. DR PDB; 9G33; EM; 3.05 A; UJ=1-1769. DR PDB; 9N6V; EM; 3.16 A; LM=1-1769. DR PDB; 9N6W; EM; 3.05 A; LM=1-1769. DR PDB; 9N6X; EM; 3.71 A; LM=1-1769. DR PDB; 9N6Y; EM; 3.65 A; LM=1-1769. DR PDB; 9N6Z; EM; 4.74 A; LM=1-1769. DR PDB; 9N70; EM; 5.17 A; LM=1-1769. DR PDB; 9N72; EM; 5.94 A; LM=1-1769. DR PDB; 9N73; EM; 5.96 A; LM=1-1769. DR PDB; 9N74; EM; 2.65 A; LM=1-1769. DR PDB; 9N75; EM; 3.01 A; LM=1-1769. DR PDB; 9N76; EM; 4.20 A; LM=1-1769. DR PDB; 9N77; EM; 3.94 A; LM=1-1769. DR PDB; 9N78; EM; 4.17 A; LM=1-1769. DR AlphaFoldDB; P42945; -. DR EMDB; EMD-0441; -. DR EMDB; EMD-0949; -. DR EMDB; EMD-0950; -. DR EMDB; EMD-0951; -. DR EMDB; EMD-0952; -. DR EMDB; EMD-0953; -. DR EMDB; EMD-0954; -. DR EMDB; EMD-0955; -. DR EMDB; EMD-11357; -. DR EMDB; EMD-11358; -. DR EMDB; EMD-11359; -. DR EMDB; EMD-11360; -. DR EMDB; EMD-11361; -. DR EMDB; EMD-11807; -. DR EMDB; EMD-11808; -. DR EMDB; EMD-25441; -. DR EMDB; EMD-30574; -. DR EMDB; EMD-30584; -. DR EMDB; EMD-30585; -. DR EMDB; EMD-30588; -. DR EMDB; EMD-49075; -. DR EMDB; EMD-49076; -. DR EMDB; EMD-49077; -. DR EMDB; EMD-49078; -. DR EMDB; EMD-49079; -. DR EMDB; EMD-49080; -. DR EMDB; EMD-49082; -. DR EMDB; EMD-49083; -. DR EMDB; EMD-49084; -. DR EMDB; EMD-49085; -. DR EMDB; EMD-49086; -. DR EMDB; EMD-49087; -. DR EMDB; EMD-49088; -. DR EMDB; EMD-50991; -. DR EMDB; EMD-6695; -. DR EMDB; EMD-6696; -. DR EMDB; EMD-8859; -. DR EMDB; EMD-9964; -. DR SMR; P42945; -. DR BioGRID; 33647; 484. DR ComplexPortal; CPX-1409; UTP-A complex. DR DIP; DIP-6466N; -. DR FunCoup; P42945; 1373. DR IntAct; P42945; 103. DR MINT; P42945; -. DR STRING; 4932.YJL109C; -. DR iPTMnet; P42945; -. DR PaxDb; 4932-YJL109C; -. DR PeptideAtlas; P42945; -. DR TopDownProteomics; P42945; -. DR EnsemblFungi; YJL109C_mRNA; YJL109C; YJL109C. DR GeneID; 853335; -. DR KEGG; sce:YJL109C; -. DR AGR; SGD:S000003645; -. DR SGD; S000003645; UTP10. DR VEuPathDB; FungiDB:YJL109C; -. DR eggNOG; KOG1837; Eukaryota. DR HOGENOM; CLU_001128_3_1_1; -. DR InParanoid; P42945; -. DR OMA; GEPFDRY; -. DR OrthoDB; 31183at2759; -. DR BioCyc; YEAST:G3O-31563-MONOMER; -. DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR BioGRID-ORCS; 853335; 4 hits in 10 CRISPR screens. DR CD-CODE; BDAE0F88; Nucleolus. DR PRO; PR:P42945; -. DR Proteomes; UP000002311; Chromosome X. DR RNAct; P42945; protein. DR GO; GO:0030686; C:90S preribosome; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central. DR GO; GO:0033553; C:rDNA heterochromatin; IDA:SGD. DR GO; GO:0032040; C:small-subunit processome; IDA:SGD. DR GO; GO:0034455; C:t-UTP complex; IDA:SGD. DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central. DR GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD. DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal. 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:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD. DR FunFam; 1.25.10.10:FF:000530; UTP10p Nucleolar protein; 1. DR FunFam; 1.25.10.10:FF:000730; UTP10p Nucleolar protein; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR012954; BP28_C_dom. DR InterPro; IPR021133; HEAT_type_2. DR InterPro; IPR056473; HEAT_Utp10/HEAT1. DR InterPro; IPR022125; U3snoRNP10_N. DR InterPro; IPR040191; UTP10. DR PANTHER; PTHR13457; BAP28; 1. DR PANTHER; PTHR13457:SF1; HEAT REPEAT-CONTAINING PROTEIN 1; 1. DR Pfam; PF08146; BP28CT; 1. DR Pfam; PF23243; HEAT_HEATR1; 1. DR Pfam; PF12397; U3snoRNP10; 1. DR SMART; SM01036; BP28CT; 1. DR SUPFAM; SSF48371; ARM repeat; 3. DR PROSITE; PS50077; HEAT_REPEAT; 1. 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; 6LQV; -. DR PDBsum; 6ND4; -. DR PDBsum; 6ZQA; -. DR PDBsum; 6ZQB; -. DR PDBsum; 6ZQC; -. DR PDBsum; 6ZQD; -. DR PDBsum; 6ZQE; -. DR PDBsum; 7AJT; -. DR PDBsum; 7AJU; -. DR PDBsum; 7D4I; -. DR PDBsum; 7D5S; -. DR PDBsum; 7D5T; -. DR PDBsum; 7D63; -. DR PDBsum; 7SUK; -. DR PDBsum; 9G33; -. DR PDBsum; 9N6V; -. DR PDBsum; 9N6W; -. DR PDBsum; 9N6X; -. DR PDBsum; 9N6Y; -. DR PDBsum; 9N6Z; -. DR PDBsum; 9N70; -. DR PDBsum; 9N72; -. DR PDBsum; 9N73; -. DR PDBsum; 9N74; -. DR PDBsum; 9N75; -. DR PDBsum; 9N76; -. DR PDBsum; 9N77; -. DR PDBsum; 9N78; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Mitochondrion; Nucleus; Reference proteome; KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; Transcription. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..1769 FT /note="U3 small nucleolar RNA-associated protein 10" FT /id="PRO_0000186207" FT REPEAT 1729..1767 FT /note="HEAT" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT HELIX 4..14 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 15..17 FT /evidence="ECO:0007829|PDB:6KE6" FT HELIX 22..29 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 37..42 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 45..62 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 64..71 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:6LQP" FT HELIX 76..80 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 88..105 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 107..110 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 112..123 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 132..139 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:6KE6" FT HELIX 146..154 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:6LQP" FT TURN 163..166 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 176..183 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 186..201 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 207..223 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 228..247 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 251..267 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 272..284 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 289..305 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 309..312 FT /evidence="ECO:0007829|PDB:6LQP" FT HELIX 313..316 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 317..326 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 329..337 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 345..354 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 355..359 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 363..372 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:6KE6" FT HELIX 377..393 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 398..409 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 412..421 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 426..433 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 465..471 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 472..475 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 483..485 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 488..504 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 508..515 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 516..518 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 519..531 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 537..553 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 556..558 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 560..562 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 564..571 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 576..591 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 599..603 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 604..606 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 616..629 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 632..634 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 638..641 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 647..660 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 664..674 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 678..687 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 689..697 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 699..709 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 713..723 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 726..729 FT /evidence="ECO:0007829|PDB:6KE6" FT HELIX 731..742 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 746..759 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 760..762 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 765..781 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 783..785 FT /evidence="ECO:0007829|PDB:6LQP" FT HELIX 788..794 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 799..809 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 811..814 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 828..839 FT /evidence="ECO:0007829|PDB:6LQP" FT HELIX 842..860 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 867..886 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 891..912 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 922..931 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 935..951 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 954..966 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 967..971 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 977..997 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1002..1017 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1022..1035 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1038..1058 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1062..1078 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1081..1103 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1105..1111 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1116..1119 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1121..1123 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1126..1144 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1148..1151 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 1154..1156 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1158..1167 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1173..1201 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1224..1240 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1243..1256 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1260..1275 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1282..1299 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1303..1320 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1327..1342 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1345..1362 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 1363..1365 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1366..1386 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1391..1410 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1412..1417 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1419..1428 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1434..1447 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1450..1460 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1461..1465 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1471..1487 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 1493..1495 FT /evidence="ECO:0007829|PDB:6LQP" FT HELIX 1497..1513 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1518..1532 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 1533..1537 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1541..1556 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 1562..1564 FT /evidence="ECO:0007829|PDB:6LQP" FT HELIX 1568..1586 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1590..1609 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1616..1632 FT /evidence="ECO:0007829|PDB:9G33" FT TURN 1637..1639 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1641..1657 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1660..1676 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1677..1679 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1681..1695 FT /evidence="ECO:0007829|PDB:9G33" FT STRAND 1696..1699 FT /evidence="ECO:0007829|PDB:6LQP" FT HELIX 1701..1718 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1720..1738 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1742..1747 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1748..1752 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1753..1760 FT /evidence="ECO:0007829|PDB:9G33" FT HELIX 1764..1768 FT /evidence="ECO:0007829|PDB:9G33" SQ SEQUENCE 1769 AA; 200082 MW; 064480D1D249B241 CRC64; MSSLSDQLAQ VASNNATVAL DRKRRQKLHS ASLIYNSKTA ATQDYDFIFE NASKALEELS QIEPKFAIFS RTLFSESSIS LDRNVQTKEE IKDLDNAINA YLLLASSKWY LAPTLHATEW LVRRFQIHVK NTEMLLLSTL NYYQTPVFKR ILSIIKLPPL FNCLSNFVRS EKPPTALTMI KLFNDMDFLK LYTSYLDQCI KHNATYTNQL LFTTCCFINV VAFNSNNDEK LNQLVPILLE ISAKLLASKS KDCQIAAHTI LVVFATALPL KKTIILAAME TILSNLDAKE AKHSALLTIC KLFQTLKGQG NVDQLPSKIF KLFDSKFDTV SILTFLDKED KPVCDKFITS YTRSIARYDR SKLNIILSLL KKIRLERYEV RLIITDLIYL SEILEDKSQL VELFEYFISI NEDLVLKCLK SLGLTGELFE IRLTTSLFTN ADVNTDIVKQ LSDPVETTKK DTASFQTFLD KHSELINTTN VSMLTETGER YKKVLSLFTE AIGKGYKASS FLTSFFTTLE SRITFLLRVT ISPAAPTALK LISLNNIAKY INSIEKEVNI FTLVPCLICA LRDASIKVRT GVKKILSLIA KRPSTKHYFL SDKLYGENVT IPMLNPKDSE AWLSGFLNEY VTENYDISRI LTPKRNEKVF LMFWANQALL IPSPYAKTVL LDNLNKSPTY ASSYSSLFEE FISHYLENRS SWEKSCIANK TNFEHFERSL VNLVSPKEKQ SFMIDFVLSA LNSDYEQLAN IAAERLISIF ASLNNAQKLK IVQNIVDSSS NVESSYDTVG VLQSLPLDSD IFVSILNQNS ISNEMDQTDF SKRRRRRSST SKNAFLKEEV SQLAELHLRK LTIILEALDK VRNVGSEKLL FTLLSLLSDL ETLDQDGGLP VLYAQETLIS CTLNTITYLK EHGCTELTNV RADILVSAIR NSASPQVQNK LLLVIGSLAT LSSEVILHSV MPIFTFMGAH SIRQDDEFTT KVVERTILTV VPALIKNSKG NEKEEMEFLL LSFTTALQHV PRHRRVKLFS TLIKTLDPVK ALGSFLFLIA QQYSSALVNF KIGEARILIE FIKALLVDLH VNEELSGLND LLDIIKLLTS SKSSSEKKKS LESRVLFSNG VLNFSESEFL TFMNNTFEFI NKITEETDQD YYDVRRNLRL KVYSVLLDET SDKKLIRNIR EEFGTLLEGV LFFINSVELT FSCITSQENE EASDSETSLS DHTTEIKEIL FKVLGNVLQI LPVDEFVNAV LPLLSTSTNE DIRYHLTLVI GSKFELEGSE AIPIVNNVMK VLLDRMPLES KSVVISQVIL NTMTALVSKY GKKLEGSILT QALTLATEKV SSDMTEVKIS SLALITNCVQ VLGVKSIAFY PKIVPPSIKL FDASLADSSN PLKEQLQVAI LLLFAGLIKR IPSFLMSNIL DVLHVIYFSR EVDSSIRLSV ISLIIENIDL KEVLKVLFRI WSTEIATSND TVAVSLFLST LESTVENIDK KSATSQSPIF FKLLLSLFEF RSISSFDNNT ISRIEASVHE ISNSYVLKMN DKVFRPLFVI LVRWAFDGEG VTNAGITETE RLLAFFKFFN KLQENLRGII TSYFTYLLEP VDMLLKRFIS KDMENVNLRR LVINSLTSSL KFDRDEYWKS TSRFELISVS LVNQLSNIEN SIGKYLVKAI GALASNNSGV DEHNQILNKL IVEHMKASCS SNEKLWAIRA MKLIYSKIGE SWLVLLPQLV PVIAELLEDD DEEIEREVRT GLVKVVENVL GEPFDRYLD //