PRP43_YEAST
ID PRP43_YEAST Reviewed; 767 AA.
AC P53131; D6VU28;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43;
DE EC=3.6.4.13;
DE AltName: Full=Helicase JA1;
GN Name=PRP43; OrderedLocusNames=YGL120C;
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], FUNCTION, AND MUTAGENESIS OF GLY-194;
RP SER-247 AND GLY-395.
RC STRAIN=SS330;
RX PubMed=9342317; DOI=10.1073/pnas.94.22.11798;
RA Arenas J.E., Abelson J.N.;
RT "Prp43: an RNA helicase-like factor involved in spliceosome disassembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11798-11802(1997).
RN [2]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SPP382.
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 [5]
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 [6]
RP IDENTIFICATION IN THE NTC-RELATED COMPLEX, AND INTERACTION WITH NTR1 AND
RP NTR2.
RX PubMed=16357217; DOI=10.1101/gad.1377405;
RA Tsai R.-T., Fu R.-H., Yeh F.-L., Tseng C.-K., Lin Y.-C., Huang Y.-H.,
RA Cheng S.-C.;
RT "Spliceosome disassembly catalyzed by Prp43 and its associated components
RT Ntr1 and Ntr2.";
RL Genes Dev. 19:2991-3003(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH NTR1 AND NTR2.
RX PubMed=16880513; DOI=10.1128/mcb.02347-05;
RA Boon K.-L., Auchynnikava T., Edwalds-Gilbert G., Barrass J.D., Droop A.P.,
RA Dez C., Beggs J.D.;
RT "Yeast ntr1/spp382 mediates prp43 function in postspliceosomes.";
RL Mol. Cell. Biol. 26:6016-6023(2006).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP IDENTIFICATION BY 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-9, 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: Pre-mRNA processing factor involved in disassembly of
CC spliceosomes after the release of mature mRNA.
CC {ECO:0000269|PubMed:16880513, ECO:0000269|PubMed:9342317}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Component of the NTR complex (NTC-related complex), composed
CC of NTR1, NTR2 and PRP43. Interacts with NTR1 and NTR2. Interacts with
CC SPP382. {ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:16357217,
CC ECO:0000269|PubMed:16880513}.
CC -!- INTERACTION:
CC P53131; P36009: DHR2; NbExp=2; IntAct=EBI-505, EBI-5844;
CC P53131; P36049: EBP2; NbExp=3; IntAct=EBI-505, EBI-6289;
CC P53131; P43586: LOC1; NbExp=3; IntAct=EBI-505, EBI-22906;
CC P53131; P47035: NET1; NbExp=2; IntAct=EBI-505, EBI-25953;
CC P53131; Q08208: NOP12; NbExp=2; IntAct=EBI-505, EBI-35895;
CC P53131; P53927: NOP15; NbExp=3; IntAct=EBI-505, EBI-28853;
CC P53131; P37838: NOP4; NbExp=3; IntAct=EBI-505, EBI-12122;
CC P53131; P40078: NSA2; NbExp=3; IntAct=EBI-505, EBI-22681;
CC P53131; P53335: PXR1; NbExp=6; IntAct=EBI-505, EBI-23652;
CC P53131; P10964: RPA190; NbExp=2; IntAct=EBI-505, EBI-15730;
CC P53131; Q06411: SPP382; NbExp=11; IntAct=EBI-505, EBI-576;
CC P53131; P53866: SQS1; NbExp=11; IntAct=EBI-505, EBI-29168;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 16900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX15/PRP43 sub-subfamily. {ECO:0000305}.
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DR EMBL; U41851; AAB86458.1; -; Genomic_DNA.
DR EMBL; Z72642; CAA96828.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07989.1; -; Genomic_DNA.
DR PIR; S64130; S64130.
DR RefSeq; NP_011395.1; NM_001180985.1.
DR PDB; 2XAU; X-ray; 1.90 A; A/B=1-767.
DR PDB; 3KX2; X-ray; 2.20 A; A/B=1-767.
DR PDB; 5I8Q; X-ray; 4.20 A; A/B=1-767.
DR PDB; 5JPT; X-ray; 2.94 A; A/B=1-767.
DR PDB; 5Y88; EM; 3.70 A; W=1-767.
DR PDBsum; 2XAU; -.
DR PDBsum; 3KX2; -.
DR PDBsum; 5I8Q; -.
DR PDBsum; 5JPT; -.
DR PDBsum; 5Y88; -.
DR AlphaFoldDB; P53131; -.
DR SMR; P53131; -.
DR BioGRID; 33131; 488.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR ComplexPortal; CPX-1886; Post-mRNA release spliceosomal complex.
DR DIP; DIP-5152N; -.
DR IntAct; P53131; 172.
DR MINT; P53131; -.
DR STRING; 4932.YGL120C; -.
DR iPTMnet; P53131; -.
DR MaxQB; P53131; -.
DR PaxDb; P53131; -.
DR PRIDE; P53131; -.
DR EnsemblFungi; YGL120C_mRNA; YGL120C; YGL120C.
DR GeneID; 852757; -.
DR KEGG; sce:YGL120C; -.
DR SGD; S000003088; PRP43.
DR VEuPathDB; FungiDB:YGL120C; -.
DR eggNOG; KOG0925; Eukaryota.
DR GeneTree; ENSGT00940000175573; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; P53131; -.
DR OMA; DHDLKRY; -.
DR BioCyc; YEAST:G3O-30617-MON; -.
DR EvolutionaryTrace; P53131; -.
DR PRO; PR:P53131; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53131; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IMP:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IGI:SGD.
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; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IDA:SGD.
DR CDD; cd17973; DEXHc_DHX15; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044756; DHX15_DEXHc.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..767
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT PRP43"
FT /id="PRO_0000055145"
FT DOMAIN 103..268
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 293..473
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 215..218
FT /note="DEAH box"
FT COMPBIAS 32..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 194
FT /note="G->D: In PRP43-DN1; dominant-negative phenotype."
FT /evidence="ECO:0000269|PubMed:9342317"
FT MUTAGEN 247
FT /note="S->L: In PRP43-DN2; dominant-negative phenotype."
FT /evidence="ECO:0000269|PubMed:9342317"
FT MUTAGEN 395
FT /note="G->E: In PRP43-1; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:9342317"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2XAU"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:2XAU"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2XAU"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5JPT"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:2XAU"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 222..237
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 286..300
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 313..334
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:2XAU"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 418..426
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 430..440
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 488..500
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 512..517
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 524..532
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 533..536
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 539..549
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:5JPT"
FT HELIX 562..570
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 578..589
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 592..597
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 599..605
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 610..629
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 644..656
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:2XAU"
FT TURN 665..667
FT /evidence="ECO:0007829|PDB:3KX2"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:2XAU"
FT TURN 673..675
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 678..681
FT /evidence="ECO:0007829|PDB:2XAU"
FT STRAND 692..712
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 715..721
FT /evidence="ECO:0007829|PDB:2XAU"
FT TURN 723..725
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:2XAU"
FT HELIX 735..748
FT /evidence="ECO:0007829|PDB:2XAU"
SQ SEQUENCE 767 AA; 87562 MW; DA8A085EC50FF430 CRC64;
MGSKRRFSSE HPDPVETSIP EQAAEIAEEL SKQHPLPSEE PLVHHDAGEF KGLQRHHTSA
EEAQKLEDGK INPFTGREFT PKYVDILKIR RELPVHAQRD EFLKLYQNNQ IMVFVGETGS
GKTTQIPQFV LFDEMPHLEN TQVACTQPRR VAAMSVAQRV AEEMDVKLGE EVGYSIRFEN
KTSNKTILKY MTDGMLLREA MEDHDLSRYS CIILDEAHER TLATDILMGL LKQVVKRRPD
LKIIIMSATL DAEKFQRYFN DAPLLAVPGR TYPVELYYTP EFQRDYLDSA IRTVLQIHAT
EEAGDILLFL TGEDEIEDAV RKISLEGDQL VREEGCGPLS VYPLYGSLPP HQQQRIFEPA
PESHNGRPGR KVVISTNIAE TSLTIDGIVY VVDPGFSKQK VYNPRIRVES LLVSPISKAS
AQQRAGRAGR TRPGKCFRLY TEEAFQKELI EQSYPEILRS NLSSTVLELK KLGIDDLVHF
DFMDPPAPET MMRALEELNY LACLDDEGNL TPLGRLASQF PLDPMLAVML IGSFEFQCSQ
EILTIVAMLS VPNVFIRPTK DKKRADDAKN IFAHPDGDHI TLLNVYHAFK SDEAYEYGIH
KWCRDHYLNY RSLSAADNIR SQLERLMNRY NLELNTTDYE SPKYFDNIRK ALASGFFMQV
AKKRSGAKGY ITVKDNQDVL IHPSTVLGHD AEWVIYNEFV LTSKNYIRTV TSVRPEWLIE
IAPAYYDLSN FQKGDVKLSL ERIKEKVDRL NELKQGKNKK KSKHSKK
