SN114_YEAST
ID SN114_YEAST Reviewed; 1008 AA.
AC P36048; D6VX27;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Pre-mRNA-splicing factor SNU114;
DE AltName: Full=114 kDa U5 small nuclear ribonucleoprotein component;
DE AltName: Full=Growth inhibitory protein 10;
GN Name=SNU114; Synonyms=GIN10; OrderedLocusNames=YKL173W; ORFNames=YKL637;
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 204508 / S288c;
RX PubMed=8091858; DOI=10.1002/yea.320100004;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "Sequencing and analysis of a 20.5 kb DNA segment located on the left arm
RT of yeast chromosome XI.";
RL Yeast 10:S25-S33(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA Fabrizio P.;
RT "Identification by mass spectrometry and functional analysis of novel
RT proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL EMBO J. 18:4535-4548(1999).
RN [5]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 823-846.
RC STRAIN=ATCC 26786 / X2180-1A;
RA Akada R., Yamamoto J., Yamashita I.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CHARACTERIZATION.
RX PubMed=9233818; DOI=10.1093/emboj/16.13.4092;
RA Fabrizio P., Laggerbauer B., Lauber J., Lane W.S., Luehrmann R.;
RT "An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding
RT factor closely related to the ribosomal translocase EF-2.";
RL EMBO J. 16:4092-4106(1997).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, 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 [12]
RP SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND ELECTRON
RP MICROSCOPY.
RX PubMed=18953335; DOI=10.1038/nsmb.1506;
RA Hacker I., Sander B., Golas M.M., Wolf E., Karagoz E., Kastner B.,
RA Stark H., Fabrizio P., Luhrmann R.;
RT "Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-
RT snRNP by electron microscopy.";
RL Nat. Struct. Mol. Biol. 15:1206-1212(2008).
RN [13]
RP INTERACTION WITH CWC21 AND PRP8.
RX PubMed=19854871; DOI=10.1261/rna.1908309;
RA Grainger R.J., Barrass J.D., Jacquier A., Rain J.-C., Beggs J.D.;
RT "Physical and genetic interactions of yeast Cwc21p, an ortholog of human
RT SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome.";
RL RNA 15:2161-2173(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND THR-88, AND
RP 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).
CC -!- FUNCTION: Component of the U5 snRNP complex required for pre-mRNA
CC splicing. Binds GTP.
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2,
CC CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24,
CC CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9,
CC PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Component
CC of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs
CC and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23,
CC SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interacts (via C-terminus)
CC with CWC21. Interacts (via N-terminus) with PRP8 (via SCwid domain).
CC {ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:11884590,
CC ECO:0000269|PubMed:18953335, ECO:0000269|PubMed:19854871}.
CC -!- INTERACTION:
CC P36048; P32357: AAR2; NbExp=3; IntAct=EBI-243, EBI-340;
CC P36048; P32639: BRR2; NbExp=14; IntAct=EBI-243, EBI-861;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; Z26878; CAA81514.1; -; Genomic_DNA.
DR EMBL; Z28173; CAA82015.1; -; Genomic_DNA.
DR EMBL; D28149; BAA05682.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08993.1; -; Genomic_DNA.
DR PIR; S38003; S38003.
DR RefSeq; NP_012748.1; NM_001179739.1.
DR PDB; 3JCM; EM; 3.80 A; H=1-1008.
DR PDB; 5GAM; EM; 3.70 A; C=1-1008.
DR PDB; 5GAN; EM; 3.60 A; C=1-1008.
DR PDB; 5GM6; EM; 3.50 A; C=1-1008.
DR PDB; 5GMK; EM; 3.40 A; C=1-1008.
DR PDB; 5LJ3; EM; 3.80 A; C=1-1008.
DR PDB; 5LJ5; EM; 3.80 A; C=1-1008.
DR PDB; 5LQW; EM; 5.80 A; B=1-1008.
DR PDB; 5MPS; EM; 3.85 A; C=1-1008.
DR PDB; 5MQ0; EM; 4.17 A; C=1-1008.
DR PDB; 5NRL; EM; 7.20 A; C=1-1008.
DR PDB; 5WSG; EM; 4.00 A; C=1-1008.
DR PDB; 5Y88; EM; 3.70 A; C=1-1008.
DR PDB; 5YLZ; EM; 3.60 A; C=1-1008.
DR PDB; 5ZWM; EM; 3.40 A; C=1-1008.
DR PDB; 5ZWO; EM; 3.90 A; C=1-1008.
DR PDB; 6BK8; EM; 3.30 A; B=1-1008.
DR PDB; 6EXN; EM; 3.70 A; C=1-1008.
DR PDB; 6J6G; EM; 3.20 A; C=1-1008.
DR PDB; 6J6H; EM; 3.60 A; C=1-1008.
DR PDB; 6J6N; EM; 3.86 A; C=1-1008.
DR PDB; 6J6Q; EM; 3.70 A; C=1-1008.
DR PDB; 6TEO; X-ray; 3.10 A; A/C=72-1008.
DR PDBsum; 3JCM; -.
DR PDBsum; 5GAM; -.
DR PDBsum; 5GAN; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5MPS; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR PDBsum; 6TEO; -.
DR AlphaFoldDB; P36048; -.
DR SMR; P36048; -.
DR BioGRID; 33965; 424.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-29; U5 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-30; U5 small nuclear ribonucleoprotein complex, AAR2 variant.
DR DIP; DIP-759N; -.
DR IntAct; P36048; 49.
DR MINT; P36048; -.
DR STRING; 4932.YKL173W; -.
DR iPTMnet; P36048; -.
DR MaxQB; P36048; -.
DR PaxDb; P36048; -.
DR PRIDE; P36048; -.
DR EnsemblFungi; YKL173W_mRNA; YKL173W; YKL173W.
DR GeneID; 853681; -.
DR KEGG; sce:YKL173W; -.
DR SGD; S000001656; SNU114.
DR VEuPathDB; FungiDB:YKL173W; -.
DR eggNOG; KOG0468; Eukaryota.
DR GeneTree; ENSGT00940000155685; -.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; P36048; -.
DR OMA; GPDEMGP; -.
DR BioCyc; YEAST:G3O-31940-MON; -.
DR PRO; PR:P36048; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36048; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR GO; GO:0005682; C:U5 snRNP; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IMP:SGD.
DR GO; GO:0030623; F:U5 snRNA binding; IDA:SGD.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IGI:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IC:ComplexPortal.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IMP:SGD.
DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IMP:SGD.
DR CDD; cd04098; eEF2_C_snRNP; 1.
DR CDD; cd04167; Snu114p; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031950; EFTUD2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR044121; Snu114_GTP-bd.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR InterPro; IPR035655; U5-116kDa_C.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF16004; EFTUD2; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1008
FT /note="Pre-mRNA-splicing factor SNU114"
FT /id="PRO_0000091565"
FT DOMAIN 131..338
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 140..147
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 188..192
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 214..217
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 268..271
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 315..317
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 504..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 214..218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 268..271
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 281..298
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 393..404
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 417..429
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 433..441
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 469..478
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 481..491
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 507..518
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 550..556
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 615..628
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 642..648
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 649..661
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 678..683
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 709..714
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 717..724
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 727..730
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 733..736
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 740..742
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 744..754
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 759..763
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 765..769
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 772..776
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 785..804
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 815..822
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 831..851
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 855..869
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 870..872
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 873..882
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 883..885
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 887..893
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 897..908
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 909..911
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 914..922
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 925..931
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 937..939
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 953..955
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 959..961
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 962..974
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 980..982
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 990..992
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 995..1003
FT /evidence="ECO:0007829|PDB:6TEO"
SQ SEQUENCE 1008 AA; 114041 MW; 5CE30CEFF154D013 CRC64;
MEGDDLFDEF GNLIGVDPFD SDEEESVLDE QEQYQTNTFE GSGNNNEIES RQLTSLGSKK
ELGISLEHPY GKEVEVLMET KNTQSPQTPL VEPVTERTKL QEHTIFTQLK KNIPKTRYNR
DYMLSMANIP ERIINVGVIG PLHSGKTSLM DLLVIDSHKR IPDMSKNVEL GWKPLRYLDN
LKQEIDRGLS IKLNGSTLLC TDLESKSRMI NFLDAPGHVN FMDETAVALA ASDLVLIVID
VVEGVTFVVE QLIKQSIKNN VAMCFVINKL DRLILDLKLP PMDAYLKLNH IIANINSFTK
GNVFSPIDNN IIFASTKLGF TFTIKEFVSY YYAHSIPSSK IDDFTTRLWG SVYYHKGNFR
TKPFENVEKY PTFVEFILIP LYKIFSYALS MEKDKLKNLL RSNFRVNLSQ EALQYDPQPF
LKHVLQLIFR QQTGLVDAIT RCYQPFELFD NKTAHLSIPG KSTPEGTLWA HVLKTVDYGG
AEWSLVRIYS GLLKRGDTVR ILDTSQSESR QKRQLHDISK TETSNEDEDE DDETPSCEVE
EIGLLGGRYV YPVHEAHKGQ IVLIKGISSA YIKSATLYSV KSKEDMKQLK FFKPLDYITE
AVFKIVLQPL LPRELPKLLD ALNKISKYYP GVIIKVEESG EHVILGNGEL YMDCLLYDLR
ASYAKIEIKI SDPLTVFSES CSNESFASIP VSNSISRLGE ENLPGLSISV AAEPMDSKMI
QDLSRNTLGK GQNCLDIDGI MDNPRKLSKI LRTEYGWDSL ASRNVWSFYN GNVLINDTLP
DEISPELLSK YKEQIIQGFY WAVKEGPLAE EPIYGVQYKL LSISVPSDVN IDVMKSQIIP
LMKKACYVGL LTAIPILLEP IYEVDITVHA PLLPIVEELM KKRRGSRIYK TIKVAGTPLL
EVRGQVPVIE SAGFETDLRL STNGLGMCQL YFWHKIWRKV PGDVLDKDAF IPKLKPAPIN
SLSRDFVMKT RRRKGISTGG FMSNDGPTLE KYISAELYAQ LRENGLVP
