PUS7_YEAST
ID PUS7_YEAST Reviewed; 676 AA.
AC Q08647; D6W2U5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Multisubstrate pseudouridine synthase 7;
DE EC=5.4.99.- {ECO:0000269|PubMed:14561887, ECO:0000269|PubMed:25219674, ECO:0000269|PubMed:35058356};
DE EC=5.4.99.27 {ECO:0000269|PubMed:14561887, ECO:0000269|PubMed:25219674, ECO:0000269|PubMed:35058356};
DE AltName: Full=RNA pseudouridylate synthase 7;
DE AltName: Full=RNA-uridine isomerase 7;
DE AltName: Full=tRNA pseudouridine(13) synthase;
GN Name=PUS7 {ECO:0000303|PubMed:14561887, ECO:0000312|SGD:S000005769};
GN OrderedLocusNames=YOR243C; ORFNames=O5254;
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=8972580;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1575::aid-yea45>3.0.co;2-e;
RA Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.;
RT "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the
RT yeast Saccharomyces cerevisiae.";
RL Yeast 12:1575-1586(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 FUNCTION.
RX PubMed=12426583; DOI=10.1038/nsb873;
RA Newby M.I., Greenbaum N.L.;
RT "Sculpting of the spliceosomal branch site recognition motif by a conserved
RT pseudouridine.";
RL Nat. Struct. Biol. 9:958-965(2002).
RN [5]
RP FUNCTION.
RX PubMed=12682021; DOI=10.1093/emboj/cdg191;
RA Ma X., Zhao X., Yu Y.T.;
RT "Pseudouridylation (Psi) of U2 snRNA in S. cerevisiae is catalyzed by an
RT RNA-independent mechanism.";
RL EMBO J. 22:1889-1897(2003).
RN [6]
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 [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-256.
RX PubMed=14561887; DOI=10.1261/rna.5520403;
RA Behm-Ansmant I., Urban A., Ma X., Yu Y.T., Motorin Y., Branlant C.;
RT "The Saccharomyces cerevisiae U2 snRNA:pseudouridine-synthase Pus7p is a
RT novel multisite-multisubstrate RNA:Psi-synthase also acting on tRNAs.";
RL RNA 9:1371-1382(2003).
RN [9]
RP FUNCTION.
RX PubMed=15611063; DOI=10.1074/jbc.m413288200;
RA Yang C., McPheeters D.S., Yu Y.T.;
RT "Psi35 in the branch site recognition region of U2 small nuclear RNA is
RT important for pre-mRNA splicing in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:6655-6662(2005).
RN [10]
RP FUNCTION.
RX PubMed=18435545; DOI=10.1021/bi7022392;
RA Lin Y., Kielkopf C.L.;
RT "X-ray structures of U2 snRNA-branchpoint duplexes containing conserved
RT pseudouridines.";
RL Biochemistry 47:5503-5514(2008).
RN [11]
RP FUNCTION.
RX PubMed=18332121; DOI=10.1128/mcb.01574-07;
RA Decatur W.A., Schnare M.N.;
RT "Different mechanisms for pseudouridine formation in yeast 5S and 5.8S
RT rRNAs.";
RL Mol. Cell. Biol. 28:3089-3100(2008).
RN [12]
RP FUNCTION.
RX PubMed=19114708; DOI=10.1074/jbc.m807986200;
RA Urban A., Behm-Ansmant I., Branlant C., Motorin Y.;
RT "RNA sequence and two-dimensional structure features required for efficient
RT substrate modification by the Saccharomyces cerevisiae RNA:{Psi}-synthase
RT Pus7p.";
RL J. Biol. Chem. 284:5845-5858(2009).
RN [13]
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).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21131909; DOI=10.1038/emboj.2010.316;
RA Wu G., Xiao M., Yang C., Yu Y.T.;
RT "U2 snRNA is inducibly pseudouridylated at novel sites by Pus7p and snR81
RT RNP.";
RL EMBO J. 30:79-89(2011).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25219674; DOI=10.1016/j.cell.2014.08.028;
RA Schwartz S., Bernstein D.A., Mumbach M.R., Jovanovic M., Herbst R.H.,
RA Leon-Ricardo B.X., Engreitz J.M., Guttman M., Satija R., Lander E.S.,
RA Fink G., Regev A.;
RT "Transcriptome-wide mapping reveals widespread dynamic-regulated
RT pseudouridylation of ncRNA and mRNA.";
RL Cell 159:148-162(2014).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVE SITE, AND MUTAGENESIS OF LYS-61; PHE-67; GLU-71; HIS-161; ASP-256;
RP ASN-305 AND PHE-307.
RX PubMed=35058356; DOI=10.1073/pnas.2109708119;
RA Purchal M.K., Eyler D.E., Tardu M., Franco M.K., Korn M.M., Khan T.,
RA McNassor R., Giles R., Lev K., Sharma H., Monroe J., Mallik L., Koutmos M.,
RA Koutmou K.S.;
RT "Pseudouridine synthase 7 is an opportunistic enzyme that binds and
RT modifies substrates with diverse sequences and structures.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
CC -!- FUNCTION: Catalyzes pseudouridylation at position 35 in U2 snRNA stem-
CC loop II region which induces particular conformation of the mRNA-U2
CC snRNA duplex and places the nucleophile in an accessible position for
CC the first step of splicing (PubMed:12426583, PubMed:12682021,
CC PubMed:15611063, PubMed:18435545, PubMed:19114708, PubMed:25219674).
CC Also catalyzes pseudouridylation at position 56 in U2 snRNA
CC (PubMed:21131909). Catalyzes also pseudouridylation at position 50 in
CC 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in pre-
CC tRNA(Tyr) (PubMed:14561887, PubMed:18332121, PubMed:25219674,
CC PubMed:35058356). Pseudouridine residues in tRNAs may stabilize the
CC local RNA conformation, favor interactions with protein partners and
CC play an important role in the stabilization of the codon-anticodon
CC interaction with mRNA (PubMed:14561887). Also catalyzes
CC pseudouridylation of mRNAs in response to heat shock: mediates
CC pseudouridylation of mRNAs with the consensus sequence 5'-UGUAR-3'
CC (PubMed:25219674, PubMed:35058356). {ECO:0000269|PubMed:12426583,
CC ECO:0000269|PubMed:12682021, ECO:0000269|PubMed:14561887,
CC ECO:0000269|PubMed:15611063, ECO:0000269|PubMed:18332121,
CC ECO:0000269|PubMed:18435545, ECO:0000269|PubMed:19114708,
CC ECO:0000269|PubMed:21131909, ECO:0000269|PubMed:25219674,
CC ECO:0000269|PubMed:35058356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA;
CC Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:14561887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in snRNA = pseudouridine in snRNA;
CC Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:14561887, ECO:0000269|PubMed:21131909,
CC ECO:0000269|PubMed:25219674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(13) in tRNA = pseudouridine(13) in tRNA;
CC Xref=Rhea:RHEA:42540, Rhea:RHEA-COMP:10105, Rhea:RHEA-COMP:10106,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.27;
CC Evidence={ECO:0000269|PubMed:14561887, ECO:0000269|PubMed:25219674,
CC ECO:0000269|PubMed:35058356};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:25219674, ECO:0000269|PubMed:35058356};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:25219674}. Cytoplasm {ECO:0000269|PubMed:25219674}.
CC Note=Predominantly nuclear in 30 degrees Celsius and primarily
CC cytoplasmic in heat shock. {ECO:0000269|PubMed:25219674}.
CC -!- DISRUPTION PHENOTYPE: Decreased level of pseudouridylated mRNAs.
CC {ECO:0000269|PubMed:25219674}.
CC -!- MISCELLANEOUS: Present with 4150 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC {ECO:0000305}.
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DR EMBL; Z75151; CAA99464.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11011.1; -; Genomic_DNA.
DR PIR; S67136; S67136.
DR RefSeq; NP_014886.1; NM_001183662.1.
DR PDB; 7MZV; X-ray; 3.20 A; A=1-676.
DR PDBsum; 7MZV; -.
DR AlphaFoldDB; Q08647; -.
DR SMR; Q08647; -.
DR BioGRID; 34634; 171.
DR DIP; DIP-6762N; -.
DR IntAct; Q08647; 11.
DR MINT; Q08647; -.
DR STRING; 4932.YOR243C; -.
DR iPTMnet; Q08647; -.
DR MaxQB; Q08647; -.
DR PaxDb; Q08647; -.
DR PRIDE; Q08647; -.
DR TopDownProteomics; Q08647; -.
DR EnsemblFungi; YOR243C_mRNA; YOR243C; YOR243C.
DR GeneID; 854417; -.
DR KEGG; sce:YOR243C; -.
DR SGD; S000005769; PUS7.
DR VEuPathDB; FungiDB:YOR243C; -.
DR eggNOG; KOG2339; Eukaryota.
DR GeneTree; ENSGT00530000063554; -.
DR HOGENOM; CLU_005281_0_2_1; -.
DR InParanoid; Q08647; -.
DR OMA; ERGYFNY; -.
DR BioCyc; MetaCyc:G3O-33737-MON; -.
DR BioCyc; YEAST:G3O-33737-MON; -.
DR BRENDA; 5.4.99.27; 984.
DR BRENDA; 5.4.99.B22; 984.
DR PRO; PR:Q08647; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08647; protein.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IDA:UniProtKB.
DR GO; GO:0001522; P:pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; TAS:Reactome.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:UniProtKB.
DR Gene3D; 3.30.2350.20; -; 2.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001656; PsdUridine_synth_TruD.
DR InterPro; IPR020119; PsdUridine_synth_TruD_CS.
DR InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR InterPro; IPR042214; TruD_catalytic.
DR PANTHER; PTHR13326; PTHR13326; 1.
DR Pfam; PF01142; TruD; 1.
DR PIRSF; PIRSF037016; Pseudouridin_synth_euk_prd; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1.
DR PROSITE; PS50984; TRUD; 1.
DR PROSITE; PS01268; UPF0024; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isomerase; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..676
FT /note="Multisubstrate pseudouridine synthase 7"
FT /id="PRO_0000152561"
FT DOMAIN 338..582
FT /note="TRUD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00342"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:14561887,
FT ECO:0000305|PubMed:35058356"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 61
FT /note="K->A: Decreased pseudouridylate synthase activity."
FT /evidence="ECO:0000269|PubMed:35058356"
FT MUTAGEN 67
FT /note="F->A: Decreased pseudouridylate synthase activity."
FT /evidence="ECO:0000269|PubMed:35058356"
FT MUTAGEN 71
FT /note="E->A: Decreased pseudouridylate synthase activity."
FT /evidence="ECO:0000269|PubMed:35058356"
FT MUTAGEN 161
FT /note="H->A: Does not affect pseudouridylate synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:35058356"
FT MUTAGEN 256
FT /note="D->A: Abolishes pseudouridylate synthase activity."
FT /evidence="ECO:0000269|PubMed:14561887,
FT ECO:0000269|PubMed:35058356"
FT MUTAGEN 305
FT /note="N->A: Strongly decreased pseudouridylate synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:35058356"
FT MUTAGEN 307
FT /note="F->A,Y: Strongly decreased pseudouridylate synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:35058356"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 283..294
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 303..315
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 388..394
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 398..402
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 416..420
FT /evidence="ECO:0007829|PDB:7MZV"
FT TURN 425..428
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 432..439
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 444..469
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 515..519
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 543..555
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 584..594
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 604..616
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:7MZV"
FT STRAND 635..648
FT /evidence="ECO:0007829|PDB:7MZV"
FT HELIX 651..659
FT /evidence="ECO:0007829|PDB:7MZV"
SQ SEQUENCE 676 AA; 77002 MW; 4B63F137B781FCCB CRC64;
MSDSSEATVK RPLDAHVGPS ENAAKKLKIE QRTQADGIHE ADVGITLFLS PELPGFRGQI
KQRYTDFLVN EIDQEGKVIH LTDKGFKMPK KPQRSKEEVN AEKESEAARR QEFNVDPELR
NQLVEIFGEE DVLKIESVYR TANKMETAKN FEDKSVRTKI HQLLREAFKN ELESVTTDTN
TFKIARSNRN SRTNKQEKIN QTRDANGVEN WGYGPSKDFI HFTLHKENKD TMEAVNVITK
LLRVPSRVIR YAGTKDRRAV TCQRVSISKI GLDRLNALNR TLKGMIIGNY NFSDASLNLG
DLKGNEFVVV IRDVTTGNSE VSLEEIVSNG CKSLSENGFI NYFGMQRFGT FSISTHTIGR
ELLLSNWKKA AELILSDQDN VLPKSKEARK IWAETKDAAL ALKQMPRQCL AENALLYSLS
NQRKEEDGTY SENAYYTAIM KIPRNLRTMY VHAYQSYVWN SIASKRIELH GLKLVVGDLV
IDTSEKSPLI SGIDDEDFDE DVREAQFIRA KAVTQEDIDS VKYTMEDVVL PSPGFDVLYP
SNEELKQLYV DILKADNMDP FNMRRKVRDF SLAGSYRTVI QKPKSLEYRI IHYDDPSQQL
VNTDLDILNN TRAKESGQKY MKAKLDRYMP DKGGEKTAVV LKFQLGTSAY ATMALRELMK
LETSRRGDMC DVKENI
