BRR2_YEAST
ID BRR2_YEAST Reviewed; 2163 AA.
AC P32639; D3DM80;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Pre-mRNA-splicing helicase BRR2;
DE EC=3.6.4.13;
DE AltName: Full=Protein Snu246;
GN Name=BRR2; Synonyms=RSS1, SNU246; OrderedLocusNames=YER172C;
GN ORFNames=SYGP-ORF66;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
RP CHARACTERIZATION.
RC STRAIN=DBY473;
RX PubMed=8722763; DOI=10.1093/genetics/143.1.67;
RA Noble S.M., Guthrie C.;
RT "Identification of novel genes required for yeast pre-mRNA splicing by
RT means of cold-sensitive mutations.";
RL Genetics 143:67-80(1996).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8670905; DOI=10.1002/j.1460-2075.1996.tb00774.x;
RA Lauber J., Fabrizio P., Teigelkamp S., Lane W.S., Hartmann E.,
RA Luehrmann R.;
RT "The HeLa 200 kDa U5 snRNP-specific protein and its homologue in
RT Saccharomyces cerevisiae are members of the DEXH-box protein family of
RT putative RNA helicases.";
RL EMBO J. 15:4001-4015(1996).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, 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 [10]
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INTERACTION WITH PRP8.
RX PubMed=19098916; DOI=10.1038/nsmb.1535;
RA Maeder C., Kutach A.K., Guthrie C.;
RT "ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the
RT C terminus of Prp8.";
RL Nat. Struct. Mol. Biol. 16:42-48(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, 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).
RN [13]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLY-858.
RX PubMed=23124065; DOI=10.1101/gad.199307.112;
RA Hahn D., Kudla G., Tollervey D., Beggs J.D.;
RT "Brr2p-mediated conformational rearrangements in the spliceosome during
RT activation and substrate repositioning.";
RL Genes Dev. 26:2408-2421(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1839-2163, CATALYTIC ACTIVITY,
RP FUNCTION, AND MUTAGENESIS OF TRP-938 AND ARG-1110.
RX PubMed=19716790; DOI=10.1016/j.molcel.2009.08.006;
RA Pena V., Jovin S.M., Fabrizio P., Orlowski J., Bujnicki J.M., Luhrmann R.,
RA Wahl M.C.;
RT "Common design principles in the spliceosomal RNA helicase Brr2 and in the
RT Hel308 DNA helicase.";
RL Mol. Cell 35:454-466(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1851-2163, CATALYTIC ACTIVITY,
RP FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-1107, AND INTERACTION WITH
RP PRP8 AND SNU114.
RX PubMed=19525970; DOI=10.1038/nsmb.1625;
RA Zhang L., Xu T., Maeder C., Bud L.O., Shanks J., Nix J., Guthrie C.,
RA Pleiss J.A., Zhao R.;
RT "Structural evidence for consecutive Hel308-like modules in the
RT spliceosomal ATPase Brr2.";
RL Nat. Struct. Mol. Biol. 16:731-739(2009).
CC -!- FUNCTION: RNA helicase that plays an essential role in pre-mRNA
CC splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes.
CC Involved in spliceosome assembly, activation and disassembly. Mediates
CC changes in the dynamic network of RNA-RNA interactions in the
CC spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA
CC duplices, an essential step in the assembly of a catalytically active
CC spliceosome. {ECO:0000269|PubMed:19098916, ECO:0000269|PubMed:19525970,
CC ECO:0000269|PubMed:19716790, ECO:0000269|PubMed:23124065}.
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 Evidence={ECO:0000269|PubMed:19098916, ECO:0000269|PubMed:19525970,
CC ECO:0000269|PubMed:19716790};
CC -!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of the
CC U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31,
CC PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
CC Interaction with PRP8 is important for recruitment to the U4/U6-U5 tri-
CC snRNP complex. Belongs to the CWC complex (or CEF1-associated complex),
CC a 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.
CC {ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:11884590,
CC ECO:0000269|PubMed:18953335, ECO:0000269|PubMed:19098916,
CC ECO:0000269|PubMed:19525970, ECO:0000269|PubMed:23124065}.
CC -!- INTERACTION:
CC P32639; P32639: BRR2; NbExp=2; IntAct=EBI-861, EBI-861;
CC P32639; P33334: PRP8; NbExp=25; IntAct=EBI-861, EBI-465;
CC P32639; P36048: SNU114; NbExp=14; IntAct=EBI-861, EBI-243;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: Contains two helicase domains. The N-terminal helicase domain
CC has catalytic activity by itself, contrary to the C-terminal helicase
CC domain that may have a regulatory role and enhance the activity of the
CC first helicase domain. {ECO:0000269|PubMed:19525970}.
CC -!- MISCELLANEOUS: Present with 1440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; U18922; AAB64699.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07834.1; -; Genomic_DNA.
DR PIR; S50675; S50675.
DR RefSeq; NP_011099.1; NM_001179062.1.
DR PDB; 3HIB; X-ray; 2.00 A; A=1851-2163.
DR PDB; 3IM1; X-ray; 1.65 A; A=1839-2163.
DR PDB; 3IM2; X-ray; 1.99 A; A=1839-2163.
DR PDB; 3JCM; EM; 3.80 A; N=1-2163.
DR PDB; 4BGD; X-ray; 3.10 A; A=442-2163.
DR PDB; 5DCA; X-ray; 2.80 A; A=113-2163.
DR PDB; 5GAN; EM; 3.60 A; B=1-2163.
DR PDB; 5GAO; EM; 3.60 A; B=1-2163.
DR PDB; 5GAP; EM; 3.60 A; B=1-2163.
DR PDB; 5GM6; EM; 3.50 A; B=1-2163.
DR PDB; 5LJ5; EM; 3.80 A; B=1-2163.
DR PDB; 5LQW; EM; 5.80 A; C=1-2163.
DR PDB; 5M52; X-ray; 3.40 A; A/B=1-2163.
DR PDB; 5M5P; X-ray; 4.20 A; A/C=271-2163.
DR PDB; 5NRL; EM; 7.20 A; B=1-2163.
DR PDB; 5ZWM; EM; 3.40 A; D=1-2163.
DR PDB; 5ZWO; EM; 3.90 A; D=1-2163.
DR PDB; 7B9V; EM; 2.80 A; B=1-2163.
DR PDBsum; 3HIB; -.
DR PDBsum; 3IM1; -.
DR PDBsum; 3IM2; -.
DR PDBsum; 3JCM; -.
DR PDBsum; 4BGD; -.
DR PDBsum; 5DCA; -.
DR PDBsum; 5GAN; -.
DR PDBsum; 5GAO; -.
DR PDBsum; 5GAP; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5M52; -.
DR PDBsum; 5M5P; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 7B9V; -.
DR AlphaFoldDB; P32639; -.
DR SMR; P32639; -.
DR BioGRID; 36925; 572.
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 DIP; DIP-850N; -.
DR IntAct; P32639; 89.
DR MINT; P32639; -.
DR STRING; 4932.YER172C; -.
DR iPTMnet; P32639; -.
DR MaxQB; P32639; -.
DR PaxDb; P32639; -.
DR PRIDE; P32639; -.
DR EnsemblFungi; YER172C_mRNA; YER172C; YER172C.
DR GeneID; 856919; -.
DR KEGG; sce:YER172C; -.
DR SGD; S000000974; BRR2.
DR VEuPathDB; FungiDB:YER172C; -.
DR eggNOG; KOG0951; Eukaryota.
DR GeneTree; ENSGT00940000174511; -.
DR HOGENOM; CLU_000335_1_0_1; -.
DR InParanoid; P32639; -.
DR OMA; ESFWIIV; -.
DR BioCyc; YEAST:G3O-30332-MON; -.
DR BRENDA; 3.6.4.13; 984.
DR EvolutionaryTrace; P32639; -.
DR PRO; PR:P32639; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32639; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IMP:SGD.
DR DisProt; DP01330; -.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF81296; SSF81296; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
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; Repeat; Spliceosome.
FT CHAIN 1..2163
FT /note="Pre-mRNA-splicing helicase BRR2"
FT /id="PRO_0000102086"
FT DOMAIN 508..692
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 718..921
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 998..1308
FT /note="SEC63 1"
FT DOMAIN 1357..1533
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1846..2160
FT /note="SEC63 2"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 634..637
FT /note="DEIH box"
FT MOTIF 1474..1477
FT /note="DDAH box"
FT COMPBIAS 36..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521..528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1370..1377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 858
FT /note="G->R: Reduces spliceosomal pre-mRNA splicing."
FT /evidence="ECO:0000269|PubMed:23124065"
FT MUTAGEN 938
FT /note="W->Q: Strongly reduced unwinding of U4/U6 snRNA."
FT /evidence="ECO:0000269|PubMed:19716790"
FT MUTAGEN 1107
FT /note="R->A: Reduced ATP-dependent RNA helicase activity."
FT /evidence="ECO:0000269|PubMed:19525970"
FT MUTAGEN 1110
FT /note="R->N: Abolishes unwinding of U4/U6 snRNA."
FT /evidence="ECO:0000269|PubMed:19716790"
FT HELIX 114..130
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:5M52"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:5M52"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 382..387
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 388..392
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 501..511
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4BGD"
FT HELIX 527..540
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 564..577
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 596..601
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 609..617
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 622..625
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 628..633
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 636..640
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 644..656
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 666..673
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 677..683
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 691..693
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:4BGD"
FT STRAND 703..710
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 715..735
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 740..743
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 747..762
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 767..770
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 776..785
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 791..798
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 801..804
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:4BGD"
FT HELIX 810..821
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 826..830
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 833..836
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 842..848
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 851..854
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 855..857
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 859..862
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 865..873
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 874..876
FT /evidence="ECO:0007829|PDB:4BGD"
FT TURN 878..880
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 882..891
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 892..894
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 895..901
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 902..904
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 912..915
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 916..925
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 932..939
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 943..950
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 952..956
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 960..963
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 964..966
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 967..983
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 986..990
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 991..994
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 995..999
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1000..1008
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1012..1021
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1028..1036
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1039..1041
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 1048..1050
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1051..1059
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1069..1071
FT /evidence="ECO:0007829|PDB:4BGD"
FT HELIX 1072..1084
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1092..1119
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1122..1137
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1141..1143
FT /evidence="ECO:0007829|PDB:4BGD"
FT HELIX 1145..1148
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1154..1163
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1168..1171
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1178..1182
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 1186..1190
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1191..1196
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1202..1224
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1230..1233
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1237..1244
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1246..1248
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1250..1259
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1261..1263
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1266..1275
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1278..1282
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1286..1297
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1301..1307
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1331..1333
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1337..1340
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1344..1347
FT /evidence="ECO:0007829|PDB:5M52"
FT HELIX 1350..1354
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1356..1360
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1366..1369
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1372..1375
FT /evidence="ECO:0007829|PDB:5M52"
FT HELIX 1376..1389
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1395..1398
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1402..1416
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 1417..1421
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1424..1426
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1432..1441
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1443..1447
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1449..1455
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1456..1461
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1463..1466
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1470..1474
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1476..1480
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1482..1502
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1507..1513
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1519..1525
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1529..1531
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1532..1534
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1537..1539
FT /evidence="ECO:0007829|PDB:4BGD"
FT STRAND 1544..1553
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1555..1558
FT /evidence="ECO:0007829|PDB:5M52"
FT HELIX 1561..1576
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1581..1587
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1588..1603
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 1604..1606
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1614..1622
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1627..1629
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1630..1634
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1637..1640
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1642..1644
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1646..1657
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1660..1667
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1668..1670
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1671..1673
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1677..1683
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1686..1689
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 1690..1693
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1694..1697
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1700..1707
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1714..1716
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1718..1725
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1726..1737
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1746..1749
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1750..1759
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1766..1773
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1777..1782
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1786..1789
FT /evidence="ECO:0007829|PDB:5DCA"
FT HELIX 1796..1816
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1819..1823
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1843..1846
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1847..1849
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 1860..1869
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 1876..1884
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 1887..1891
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 1898..1906
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 1909..1911
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 1915..1917
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 1919..1921
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 1922..1935
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 1941..1967
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 1973..1985
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 1989..1991
FT /evidence="ECO:0007829|PDB:4BGD"
FT HELIX 1993..1996
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 2002..2010
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 2016..2021
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 2024..2030
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 2035..2047
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 2051..2057
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 2060..2062
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 2067..2079
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 2099..2105
FT /evidence="ECO:0007829|PDB:3IM1"
FT HELIX 2106..2108
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 2110..2117
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 2121..2131
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 2135..2148
FT /evidence="ECO:0007829|PDB:3IM1"
FT STRAND 2154..2163
FT /evidence="ECO:0007829|PDB:3IM1"
SQ SEQUENCE 2163 AA; 246185 MW; DFAF7E3B7168D944 CRC64;
MTEHETKDKA KKIREIYRYD EMSNKVLKVD KRFMNTSQNP QRDAEISQPK SMSGRISAKD
MGQGLCNNIN KGLKENDVAV EKTGKSASLK KIQQHNTILN SSSDFRLHYY PKDPSNVETY
EQILQWVTEV LGNDIPHDLI IGTADIFIRQ LKENEENEDG NIEERKEKIQ HELGINIDSL
KFNELVKLMK NITDYETHPD NSNKQAVAIL ADDEKSDEEE VTEMSNNANV LGGEINDNED
DDEEYDYNDV EVNSKKKNKR ALPNIENDII KLSDSKTSNI ESVPIYSIDE FFLQRKLRSE
LGYKDTSVIQ DLSEKILNDI ETLEHNPVAL EQKLVDLLKF ENISLAEFIL KNRSTIFWGI
RLAKSTENEI PNLIEKMVAK GLNDLVEQYK FRETTHSKRE LDSGDDQPQS SEAKRTKFSN
PAIPPVIDLE KIKFDESSKL MTVTKVSLPE GSFKRVKPQY DEIHIPAPSK PVIDYELKEI
TSLPDWCQEA FPSSETTSLN PIQSKVFHAA FEGDSNMLIC APTGSGKTNI ALLTVLKALS
HHYNPKTKKL NLSAFKIVYI APLKALVQEQ VREFQRRLAF LGIKVAELTG DSRLSRKQID
ETQVLVSTPE KWDITTRNSN NLAIVELVRL LIIDEIHLLH DDRGPVLESI VARTFWASKY
GQEYPRIIGL SATLPNYEDV GRFLRVPKEG LFYFDSSFRP CPLSQQFCGI KERNSLKKLK
AMNDACYEKV LESINEGNQI IVFVHSRKET SRTATWLKNK FAEENITHKL TKNDAGSKQI
LKTEAANVLD PSLRKLIESG IGTHHAGLTR SDRSLSEDLF ADGLLQVLVC TATLAWGVNL
PAHTVIIKGT DVYSPEKGSW EQLSPQDVLQ MLGRAGRPRY DTFGEGIIIT DQSNVQYYLS
VLNQQLPIES QFVSKLVDNL NAEVVAGNIK CRNDAVNWLA YTYLYVRMLA SPMLYKVPDI
SSDGQLKKFR ESLVHSALCI LKEQELVLYD AENDVIEATD LGNIASSFYI NHASMDVYNR
ELDEHTTQID LFRIFSMSEE FKYVSVRYEE KRELKQLLEK APIPIREDID DPLAKVNVLL
QSYFSQLKFE GFALNSDIVF IHQNAGRLLR AMFEICLKRG WGHPTRMLLN LCKSATTKMW
PTNCPLRQFK TCPVEVIKRL EASTVPWGDY LQLETPAEVG RAIRSEKYGK QVYDLLKRFP
KMSVTCNAQP ITRSVMRFNI EIIADWIWDM NVHGSLEPFL LMLEDTDGDS ILYYDVLFIT
PDIVGHEFTL SFTYELKQHN QNNLPPNFFL TLISENWWHS EFEIPVSFNG FKLPKKFPPP
TPLLENISIS TSELGNDDFS EVFEFKTFNK IQSQVFESLY NSNDSVFVGS GKGTGKTAMA
ELALLNHWRQ NKGRAVYINP SGEKIDFLLS DWNKRFSHLA GGKIINKLGN DPSLNLKLLA
KSHVLLATPV QFELLSRRWR QRKNIQSLEL MIYDDAHEIS QGVYGAVYET LISRMIFIAT
QLEKKIRFVC LSNCLANARD FGEWAGMTKS NIYNFSPSER IEPLEINIQS FKDVEHISFN
FSMLQMAFEA SAAAAGNRNS SSVFLPSRKD CMEVASAFMK FSKAIEWDML NVEEEQIVPY
IEKLTDGHLR APLKHGVGIL YKGMASNDER IVKRLYEYGA VSVLLISKDC SAFACKTDEV
IILGTNLYDG AEHKYMPYTI NELLEMVGLA SGNDSMAGKV LILTSHNMKA YYKKFLIEPL
PTESYLQYII HDTLNNEIAN SIIQSKQDCV DWFTYSYFYR RIHVNPSYYG VRDTSPHGIS
VFLSNLVETC LNDLVESSFI EIDDTEAEVT AEVNGGDDEA TEIISTLSNG LIASHYGVSF
FTIQSFVSSL SNTSTLKNML YVLSTAVEFE SVPLRKGDRA LLVKLSKRLP LRFPEHTSSG
SVSFKVFLLL QAYFSRLELP VDFQNDLKDI LEKVVPLINV VVDILSANGY LNATTAMDLA
QMLIQGVWDV DNPLRQIPHF NNKILEKCKE INVETVYDIM ALEDEERDEI LTLTDSQLAQ
VAAFVNNYPN VELTYSLNNS DSLISGVKQK ITIQLTRDVE PENLQVTSEK YPFDKLESWW
LVLGEVSKKE LYAIKKVTLN KETQQYELEF DTPTSGKHNL TIWCVCDSYL DADKELSFEI
NVK
