SLU7_YEAST
ID SLU7_YEAST Reviewed; 382 AA.
AC Q02775; D6VS75; P89902; Q6Q5U3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Pre-mRNA-splicing factor SLU7;
DE AltName: Full=Synthetic lethal with U2 snRNA protein 17;
DE AltName: Full=Synthetic lethal with U5 snRNA protein 7;
GN Name=SLU7; Synonyms=SLT17; OrderedLocusNames=YDR088C; ORFNames=D4483;
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], AND FUNCTION.
RX PubMed=1427075; DOI=10.1101/gad.6.11.2112;
RA Frank D.N., Guthrie C.;
RT "An essential splicing factor, SLU7, mediates 3' splice site choice in
RT yeast.";
RL Genes Dev. 6:2112-2124(1992).
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=1406691; DOI=10.1128/mcb.12.11.5197-5205.1992;
RA Frank D.N., Patterson B., Guthrie C.;
RT "Synthetic lethal mutations suggest interactions between U5 small nuclear
RT RNA and four proteins required for the second step of splicing.";
RL Mol. Cell. Biol. 12:5197-5205(1992).
RN [6]
RP FUNCTION.
RX PubMed=7664739; DOI=10.1002/j.1460-2075.1995.tb00071.x;
RA Ansari A., Schwer B.;
RT "SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of
RT yeast pre-mRNA splicing.";
RL EMBO J. 14:4001-4009(1995).
RN [7]
RP FUNCTION.
RX PubMed=7568198; DOI=10.1073/pnas.92.21.9687;
RA Jones M.H., Frank D.N., Guthrie C.;
RT "Characterization and functional ordering of Slu7p and Prp17p during the
RT second step of pre-mRNA splicing in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9687-9691(1995).
RN [8]
RP INTERACTION WITH THE 3' SPLICE SITE.
RX PubMed=7489518;
RA Umen J.G., Guthrie C.;
RT "Prp16p, Slu7p, and Prp8p interact with the 3' splice site in two distinct
RT stages during the second catalytic step of pre-mRNA splicing.";
RL RNA 1:584-597(1995).
RN [9]
RP FUNCTION, AND ASSOCIATION WITH THE SPLICEOSOME.
RX PubMed=8756413;
RA Brys A., Schwer B.;
RT "Requirement for SLU7 in yeast pre-mRNA splicing is dictated by the
RT distance between the branchpoint and the 3' splice site.";
RL RNA 2:707-717(1996).
RN [10]
RP FUNCTION, AND INTERACTION WITH PRP18.
RX PubMed=9153314; DOI=10.1093/nar/25.11.2146;
RA Zhang X., Schwer B.;
RT "Functional and physical interaction between the yeast splicing factors
RT Slu7 and Prp18.";
RL Nucleic Acids Res. 25:2146-2152(1997).
RN [11]
RP FUNCTION.
RX PubMed=9528778; DOI=10.1128/mcb.18.4.2055;
RA Xu D., Field D.J., Tang S.-J., Moris A., Bobechko B.P., Friesen J.D.;
RT "Synthetic lethality of yeast slt mutations with U2 small nuclear RNA
RT mutations suggests functional interactions between U2 and U5 snRNPs that
RT are important for both steps of pre-mRNA splicing.";
RL Mol. Cell. Biol. 18:2055-2066(1998).
RN [12]
RP INTERACTION WITH PRP18.
RX PubMed=10737784; DOI=10.1073/pnas.97.7.3022;
RA Jiang J., Horowitz D.S., Xu R.-M.;
RT "Crystal structure of the functional domain of the splicing factor Prp18.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3022-3027(2000).
RN [13]
RP INTERACTION WITH BRR2; PRP18 AND PRP22.
RX PubMed=11290703; DOI=10.1093/genetics/157.4.1451;
RA van Nues R.W., Beggs J.D.;
RT "Functional contacts with a range of splicing proteins suggest a central
RT role for Brr2p in the dynamic control of the order of events in
RT spliceosomes of Saccharomyces cerevisiae.";
RL Genetics 157:1451-1467(2001).
RN [14]
RP INTERACTION WITH ECM2, AND FUNCTION.
RX PubMed=11158289; DOI=10.1128/mcb.21.4.1011-1023.2001;
RA Xu D., Friesen J.D.;
RT "Splicing factor slt11p and its involvement in formation of U2/U6 helix II
RT in activation of the yeast spliceosome.";
RL Mol. Cell. Biol. 21:1011-1023(2001).
RN [15]
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 [16]
RP FUNCTION, INTERACTION WITH PRP18, AND MUTAGENESIS OF CYS-122; HIS-130;
RP CYS-135; 215-GLU--GLU-217; GLU-217 AND 221-LEU--TYR-224.
RX PubMed=12212850; DOI=10.1017/s1355838202022033;
RA James S.-A., Turner W., Schwer B.;
RT "How Slu7 and Prp18 cooperate in the second step of yeast pre-mRNA
RT splicing.";
RL RNA 8:1068-1077(2002).
RN [17]
RP INTERACTION WITH PRP18.
RX PubMed=12403466; DOI=10.1017/s1355838202023099;
RA Bacikova D., Horowitz D.S.;
RT "Mutational analysis identifies two separable roles of the Saccharomyces
RT cerevisiae splicing factor Prp18.";
RL RNA 8:1280-1293(2002).
RN [18]
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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND THR-212, AND
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 [22]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, 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: Essential protein involved in the second catalytic step of
CC pre-mRNA splicing. Involved in the selection of 3'-type splice sites;
CC this selection could be done via a 3'-splice site-binding factor,
CC PRP16. {ECO:0000269|PubMed:11158289, ECO:0000269|PubMed:12212850,
CC ECO:0000269|PubMed:1406691, ECO:0000269|PubMed:1427075,
CC ECO:0000269|PubMed:7568198, ECO:0000269|PubMed:7664739,
CC ECO:0000269|PubMed:8756413, ECO:0000269|PubMed:9153314,
CC ECO:0000269|PubMed:9528778}.
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. Interacts
CC with BRR2, ECM2, PRP18 and PRP22. {ECO:0000269|PubMed:10737784,
CC ECO:0000269|PubMed:11158289, ECO:0000269|PubMed:11290703,
CC ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12212850,
CC ECO:0000269|PubMed:12403466, ECO:0000269|PubMed:7489518,
CC ECO:0000269|PubMed:9153314}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The CCHC-type zinc finger probably plays a role in the ability
CC of SLU7 to bypass the requirement for PRP18.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 1490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SLU7 family. {ECO:0000305}.
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DR EMBL; X67810; CAA48011.1; -; Genomic_DNA.
DR EMBL; X82086; CAA57617.1; -; Genomic_DNA.
DR EMBL; Z46796; CAA86810.1; -; Genomic_DNA.
DR EMBL; Z74384; CAA98908.1; -; Genomic_DNA.
DR EMBL; Z74385; CAA98909.1; -; Genomic_DNA.
DR EMBL; AY557701; AAS56027.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11935.1; -; Genomic_DNA.
DR PIR; A46229; A46229.
DR RefSeq; NP_010373.3; NM_001180396.3.
DR PDB; 5MPS; EM; 3.85 A; c=1-382.
DR PDB; 5MQ0; EM; 4.17 A; c=1-382.
DR PDB; 5YLZ; EM; 3.60 A; V=1-382.
DR PDB; 6BK8; EM; 3.30 A; O=1-382.
DR PDB; 6EXN; EM; 3.70 A; c=1-382.
DR PDBsum; 5MPS; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR AlphaFoldDB; Q02775; -.
DR SMR; Q02775; -.
DR BioGRID; 32144; 472.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-220N; -.
DR IntAct; Q02775; 13.
DR MINT; Q02775; -.
DR STRING; 4932.YDR088C; -.
DR iPTMnet; Q02775; -.
DR MaxQB; Q02775; -.
DR PaxDb; Q02775; -.
DR PRIDE; Q02775; -.
DR EnsemblFungi; YDR088C_mRNA; YDR088C; YDR088C.
DR GeneID; 851661; -.
DR KEGG; sce:YDR088C; -.
DR SGD; S000002495; SLU7.
DR VEuPathDB; FungiDB:YDR088C; -.
DR eggNOG; KOG2560; Eukaryota.
DR HOGENOM; CLU_072877_0_0_1; -.
DR InParanoid; Q02775; -.
DR OMA; KSKMFRR; -.
DR BioCyc; YEAST:G3O-29693-MON; -.
DR PRO; PR:Q02775; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q02775; protein.
DR GO; GO:0005681; C:spliceosomal complex; IDA:SGD.
DR GO; GO:0071021; C:U2-type post-spliceosomal complex; IDA:SGD.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IDA:SGD.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR InterPro; IPR021715; Slu7_dom.
DR InterPro; IPR039974; Splicing_factor_SLU7.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12942; PTHR12942; 1.
DR Pfam; PF11708; Slu7; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..382
FT /note="Pre-mRNA-splicing factor SLU7"
FT /id="PRO_0000218554"
FT ZN_FING 120..137
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..224
FT /note="Interaction with PRP8"
FT REGION 362..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 122
FT /note="C->A: Affects the ability to associate with the
FT spliceosome. Loss of growth and in vitro splicing activity;
FT when associated with 215-AAA-217. Cryo- and
FT thermosensitivity; when associated with A-217."
FT /evidence="ECO:0000269|PubMed:12212850"
FT MUTAGEN 130
FT /note="H->A: Affects the ability to associate with the
FT spliceosome. Loss of growth and in vitro splicing activity;
FT when associated with 215-AAA-217. Cryo- and
FT thermosensitivity; when associated with A-217."
FT /evidence="ECO:0000269|PubMed:12212850"
FT MUTAGEN 135
FT /note="C->A: Affects the ability to associate with the
FT spliceosome. Loss of growth, spliceosome binding, and in
FT vitro splicing activity; when associated with 215-AAA-217.
FT Cryo- and thermosensitivity; when associated with A-217."
FT /evidence="ECO:0000269|PubMed:12212850"
FT MUTAGEN 215..217
FT /note="EIE->AAA: Abolishes the interaction with PRP18, and
FT temperature sensitive growth defect. Loss of growth and in
FT vitro splicing activity; when associated with A-122 or A-
FT 130 or A-135."
FT /evidence="ECO:0000269|PubMed:12212850"
FT MUTAGEN 217
FT /note="E->A: Abolishes the interaction with PRP18.
FT Cryo- and thermosensitivity; when associated with A-122 or
FT A-130 or A-135."
FT /evidence="ECO:0000269|PubMed:12212850"
FT MUTAGEN 217
FT /note="E->K: Abolishes the interaction with PRP18, and
FT temperature sensitive growth defect."
FT /evidence="ECO:0000269|PubMed:12212850"
FT MUTAGEN 221..224
FT /note="LELY->AAAA: Abolishes the interaction with PRP18,
FT and temperature sensitive growth defect."
FT /evidence="ECO:0000269|PubMed:12212850"
FT CONFLICT 235
FT /note="D -> G (in Ref. 4; AAS56027)"
FT /evidence="ECO:0000305"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 294..313
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:6BK8"
SQ SEQUENCE 382 AA; 44637 MW; 6405458FC367A7D3 CRC64;
MNNNSRNNEN RSTINRNKRQ LQQAKEKNEN IHIPRYIRNQ PWYYKDTPKE QEGKKPGNDD
TSTAEGGEKS DYLVHHRQKA KGGALDIDNN SEPKIGMGIK DEFKLIRPQK MSVRDSHSLS
FCRNCGEAGH KEKDCMEKPR KMQKLVPDLN SQKNNGTVLV RATDDDWDSR KDRWYGYSGK
EYNELISKWE RDKRNKIKGK DKSQTDETLW DTDEEIELMK LELYKDSVGS LKKDDADNSQ
LYRTSTRLRE DKAAYLNDIN STESNYDPKS RLYKTETLGA VDEKSKMFRR HLTGEGLKLN
ELNQFARSHA KEMGIRDEIE DKEKVQHVLV ANPTKYEYLK KKREQEETKQ PKIVSIGDLE
ARKVDGTKQS EEQRNHLKDL YG
