PRP28_YEAST
ID PRP28_YEAST Reviewed; 588 AA.
AC P23394; D6VSM3; P20450;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE EC=3.6.4.13;
DE AltName: Full=Helicase CA8;
GN Name=PRP28; OrderedLocusNames=YDR243C; ORFNames=YD8419.10C;
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-297.
RC STRAIN=YJJ48;
RX PubMed=2010088; DOI=10.1101/gad.5.4.629;
RA Strauss E.J., Guthrie C.;
RT "A cold-sensitive mRNA splicing mutant is a member of the RNA helicase gene
RT family.";
RL Genes Dev. 5:629-641(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-526.
RX PubMed=2406722; DOI=10.1073/pnas.87.4.1571;
RA Chang T.-H., Arenas J., Abelson J.;
RT "Identification of five putative yeast RNA helicase genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7520570; DOI=10.1093/nar/22.15.3187;
RA Strauss E.J., Guthrie C.;
RT "PRP28, a 'DEAD-box' protein, is required for the first step of mRNA
RT splicing in vitro.";
RL Nucleic Acids Res. 22:3187-3193(1994).
RN [6]
RP MUTAGENESIS OF ALA-221; THR-223; ARG-264; GLU-265; THR-317; GLY-319;
RP MET-376; ALA-379; PRO-438; ILE-440; PHE-442; ALA-449; HIS-468; ASN-486;
RP MET-491; ARG-499; ASP-502; TYR-521; ARG-527; VAL-541; ASP-546; LEU-549;
RP LYS-580; ASN-584 AND ILE-586.
RX PubMed=9396812; DOI=10.1093/nar/25.24.5033;
RA Chang T.-H., Latus L.J., Liu Z., Abbott J.M.;
RT "Genetic interactions of conserved regions in the DEAD-box protein
RT Prp28p.";
RL Nucleic Acids Res. 25:5033-5040(1997).
RN [7]
RP FUNCTION.
RX PubMed=10024879; DOI=10.1016/s1097-2765(00)80174-4;
RA Staley J.P., Guthrie C.;
RT "An RNA switch at the 5' splice site requires ATP and the DEAD box protein
RT Prp28p.";
RL Mol. Cell 3:55-64(1999).
RN [8]
RP FUNCTION.
RX PubMed=11172727; DOI=10.1016/s1097-2765(01)00170-8;
RA Chen J.Y.-F., Stands L., Staley J.P., Jackups R.R. Jr., Latus L.J.,
RA Chang T.-H.;
RT "Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate
RT the requirement of Prp28p, an essential DEAD box splicing factor.";
RL Mol. Cell 7:227-232(2001).
RN [9]
RP IDENTIFICATION IN THE U5 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11720284;
RA Stevens S.W., Barta I., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA Abelson J.;
RT "Biochemical and genetic analyses of the U5, U6, and U4/U6 x U5 small
RT nuclear ribonucleoproteins from Saccharomyces cerevisiae.";
RL RNA 7:1543-1553(2001).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, 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: ATP-dependent RNA helicase involved in mRNA splicing. May
CC destabilize the U1/5'-splice site duplex to permit an effective
CC competition for the 5'-splice site by the U6 snRNA, resulting in the
CC switch between U1 and U6 at the 5'-splice site. May also act to unwind
CC the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating
CC the first covalent step of splicing. {ECO:0000269|PubMed:10024879,
CC ECO:0000269|PubMed:11172727, ECO:0000269|PubMed:2010088}.
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 U5 snRNP complex, composed of at least BRR2,
CC PRP8, PRP28, DIB1, LIN1, SMB1, SMD1, SMD2, SMD3, SME1, SMX2, SMX3, and
CC SNU114, associated with the U5 snRNA. {ECO:0000269|PubMed:11720284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC subfamily. {ECO:0000305}.
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DR EMBL; X56934; CAA40255.1; -; Genomic_DNA.
DR EMBL; Z49701; CAA89729.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12083.1; -; Genomic_DNA.
DR PIR; A39624; A39624.
DR RefSeq; NP_010529.3; NM_001180551.3.
DR PDB; 4W7S; X-ray; 2.54 A; A/B=127-588.
DR PDB; 5ZWN; EM; 3.30 A; y=1-588.
DR PDBsum; 4W7S; -.
DR PDBsum; 5ZWN; -.
DR AlphaFoldDB; P23394; -.
DR SMR; P23394; -.
DR BioGRID; 32294; 250.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-29; U5 small nuclear ribonucleoprotein complex.
DR DIP; DIP-6324N; -.
DR IntAct; P23394; 19.
DR MINT; P23394; -.
DR STRING; 4932.YDR243C; -.
DR iPTMnet; P23394; -.
DR MaxQB; P23394; -.
DR PaxDb; P23394; -.
DR PRIDE; P23394; -.
DR EnsemblFungi; YDR243C_mRNA; YDR243C; YDR243C.
DR GeneID; 851830; -.
DR KEGG; sce:YDR243C; -.
DR SGD; S000002651; PRP28.
DR VEuPathDB; FungiDB:YDR243C; -.
DR eggNOG; KOG0333; Eukaryota.
DR GeneTree; ENSGT00940000155606; -.
DR HOGENOM; CLU_003041_11_4_1; -.
DR InParanoid; P23394; -.
DR OMA; KKFNFEW; -.
DR BioCyc; YEAST:G3O-29816-MON; -.
DR PRO; PR:P23394; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P23394; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IC:ComplexPortal.
DR GO; GO:0005682; C:U5 snRNP; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000384; F:first spliceosomal transesterification activity; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0003724; F:RNA helicase activity; ISS:SGD.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..588
FT /note="Pre-mRNA-splicing ATP-dependent RNA helicase PRP28"
FT /id="PRO_0000055127"
FT DOMAIN 208..399
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 427..579
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 15..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..202
FT /note="Q motif"
FT MOTIF 341..344
FT /note="DEAD box"
FT COMPBIAS 32..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 221
FT /note="A->V: In PRP28-103; no growth at 15 and 37 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 223
FT /note="T->I: In PRP28-117; no growth at 15 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 264
FT /note="R->D,E: Lethal."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 265
FT /note="E->Q: In PRP28-99; no growth at 15 and 37 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 297
FT /note="G->E: In PRP28-1; no growth at 15 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:2010088"
FT MUTAGEN 317
FT /note="T->I: In PRP28-36; slow growth at 30 degrees
FT Celsius, and no growth at 15 and 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 317
FT /note="T->Y: Lethal."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 319
FT /note="G->E,V: No growth at 15 and 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 376
FT /note="M->I: In PRP28-32; no growth at 15 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 379
FT /note="A->W: In PRP28-102; no growth at 25 degrees Celsius
FT or lower."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 438
FT /note="P->L: In PRP28-61; no growth at 37 degrees Celsius;
FT when associated with L-468 and D-486."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 440
FT /note="I->F: In PRP28-56; no growth at 37 degrees Celsius;
FT when associated with S-546 and E-584."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 442
FT /note="F->G: In PRP28-101; no growth at 15 and 37 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 442
FT /note="F->S: In PRP28-55; no growth at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 449
FT /note="A->T: In PRP28-66; no growth at 37 degrees Celsius;
FT when associated with A-541; V-549; N-580 and V-586."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 468
FT /note="H->L: In PRP28-61; no growth at 37 degrees Celsius;
FT when associated with L-438 and D-486."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 486
FT /note="N->D: In PRP28-61; no growth at 37 degrees Celsius;
FT when associated with L-438 and L-468."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 491
FT /note="M->K: In PRP28-52; no growth at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 499
FT /note="R->G: In PRP28-86; lethal."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 499
FT /note="R->K: No growth at 15 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 502
FT /note="D->N: Lethal."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 521
FT /note="Y->D: In PRP28-37; no growth at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 527
FT /note="R->D: Lethal."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 541
FT /note="V->A: In PRP28-66; no growth at 37 degrees Celsius;
FT when associated with T-449; V-549; N-580 and V-586."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 546
FT /note="D->S: In PRP28-56; no growth at 37 degrees Celsius;
FT when associated with F-440 and E-584."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 549
FT /note="L->V: In PRP28-66; no growth at 37 degrees Celsius;
FT when associated with T-449; A-541; N-580 and V-586."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 580
FT /note="K->N: In PRP28-66; no growth at 37 degrees Celsius;
FT when associated with T-449; A-541; V-549 and V-586."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 584
FT /note="N->E: In PRP28-56; no growth at 37 degrees Celsius;
FT when associated with F-440 and S-546."
FT /evidence="ECO:0000269|PubMed:9396812"
FT MUTAGEN 586
FT /note="I->V: In PRP28-66; no growth at 37 degrees Celsius;
FT when associated with T-449; A-541; V-549 and N-580."
FT /evidence="ECO:0000269|PubMed:9396812"
FT CONFLICT 493
FT /note="A -> R (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 410..417
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 421..432
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 446..459
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 473..484
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:4W7S"
FT TURN 495..500
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 506..513
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:4W7S"
FT STRAND 534..541
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 547..559
FT /evidence="ECO:0007829|PDB:4W7S"
FT HELIX 570..576
FT /evidence="ECO:0007829|PDB:4W7S"
SQ SEQUENCE 588 AA; 66641 MW; 333ADBF9D7C75C99 CRC64;
MARPIDVSQL IAGINKKKGL DENTSGKISK PRFLNKQERS KQERLKENEE SLTPTQSDSA
KVEIKKVNSR DDSFFNETND KKRNPSKQNG SKFHFSWNES EDTLSGYDPI VSTRAIDLLW
KGKTPKNAAE SSYMGKHWTE KSLHEMNERD WRILKEDYAI VTKGGTVENP LRNWEELNII
PRDLLRVIIQ ELRFPSPTPI QRITIPNVCN MKQYRDFLGV ASTGSGKTLA FVIPILIKMS
RSPPRPPSLK IIDGPKALIL APTRELVQQI QKETQKVTKI WSKESNYDCK VISIVGGHSL
EEISFSLSEG CDILVATPGR LIDSLENHLL VMKQVETLVL DEADKMIDLG FEDQVTNILT
KVDINADSAV NRQTLMFTAT MTPVIEKIAA GYMQKPVYAT IGVETGSEPL IQQVVEYADN
DEDKFKKLKP IVAKYDPPII IFINYKQTAD WLAEKFQKET NMKVTILHGS KSQEQREHSL
QLFRTNKVQI MIATNVAARG LDIPNVSLVV NFQISKKMDD YIHRIGRTGR AANEGTAVSF
VSAAEDESLI RELYKYVRKH DPLNSNIFSE AVKNKYNVGK QLSNEIIY
