BLM10_YEAST
ID BLM10_YEAST Reviewed; 2143 AA.
AC P43583; D6VTM3; P43584;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Proteasome activator BLM10;
DE AltName: Full=Bleomycin resistance protein BLM10;
GN Name=BLM10; Synonyms=BLM3; OrderedLocusNames=YFL007W; ORFNames=YFL006W;
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 IDENTIFICATION OF FRAMESHIFT.
RC STRAIN=ATCC 201390 / BY4743, and ATCC 96604 / S288c / FY1679;
RX PubMed=12185839; DOI=10.1002/yea.870;
RA Robben J., Hertveldt K., Volckaert G.;
RT "Revisiting the yeast chromosome VI DNA sequence reveals a correction
RT merging YFL007w and YFL006w to a single ORF.";
RL Yeast 19:699-702(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION OF FRAMESHIFT.
RC STRAIN=CM1469-5C;
RX PubMed=15449308; DOI=10.1002/yea.1146;
RA Doherty K., Pramanik A., Pride L., Lukose J., Moore C.W.;
RT "Expression of the expanded YFL007w ORF and assignment of the gene name
RT BLM10.";
RL Yeast 21:1021-1023(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8789262;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<77::aid-yea887>3.0.co;2-5;
RA Naitou M., Ozawa M., Sasanuma S., Kobayashi M., Hagiwara H., Shibata T.,
RA Hanaoka F., Watanabe K., Ono A., Yamazaki M., Tashiro H., Eki T.,
RA Murakami Y.;
RT "Sequencing of a 23 kb fragment from Saccharomyces cerevisiae chromosome
RT VI.";
RL Yeast 12:77-84(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1804, AND FUNCTION.
RX PubMed=11842813;
RA Febres D.E., Pramanik A., Caton M., Doherty K., McKoy J., Garcia E.,
RA Alejo W., Moore C.W.;
RT "The novel BLM3 gene encodes a protein that protects against lethal effects
RT of oxidative damage.";
RL Cell. Mol. Biol. 47:1149-1162(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1890-2143.
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 [8]
RP PROTEIN SEQUENCE OF 340-346; 481-490; 813-830; 860-867; 950-958; 1039-1046;
RP 1086-1102; 1164-1174; 1250-1271; 1513-1525; 1528-1548; 1562-1567;
RP 1578-1585; 1601-1608; 1687-1706 AND 2123-2139, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15778719; DOI=10.1038/nsmb914;
RA Schmidt M., Haas W., Crosas B., Santamaria P.G., Gygi S.P., Walz T.,
RA Finley D.;
RT "The HEAT repeat protein Blm10 regulates the yeast proteasome by capping
RT the core particle.";
RL Nat. Struct. Mol. Biol. 12:294-303(2005).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12973301; DOI=10.1038/sj.embor.embor938;
RA Fehlker M., Wendler P., Lehmann A., Enenkel C.;
RT "Blm3 is part of nascent proteasomes and is involved in a late stage of
RT nuclear proteasome assembly.";
RL EMBO Rep. 4:959-963(2003).
RN [10]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [11]
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-1041, AND
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-62; THR-64 AND
RP SER-1041, AND 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 [15]
RP FUNCTION, AND INTERACTION WITH THE PROTEASOME.
RX PubMed=18927584; DOI=10.1038/embor.2008.190;
RA Lehmann A., Jechow K., Enenkel C.;
RT "Blm10 binds to pre-activated proteasome core particles with open gate
RT conformation.";
RL EMBO Rep. 9:1237-1243(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-56 AND SER-62, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-64; THR-66 AND
RP SER-1041, AND 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).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF ARG-2139; SER-2140; TYR-2141; TYR-2142 AND
RP ALA-2143.
RX PubMed=22025621; DOI=10.1074/jbc.m111.300178;
RA Dange T., Smith D., Noy T., Rommel P.C., Jurzitza L., Cordero R.J.,
RA Legendre A., Finley D., Goldberg A.L., Schmidt M.;
RT "Blm10 protein promotes proteasomal substrate turnover by an active gating
RT mechanism.";
RL J. Biol. Chem. 286:42830-42839(2011).
RN [19]
RP FUNCTION, AND MUTAGENESIS OF 1663-TYR-ASN-1664.
RX PubMed=23706739; DOI=10.1016/j.cell.2013.04.032;
RA Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F.,
RA Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B.,
RA Zhang Z.H., Liang Y.N., Liu S., Cha H., Yang D., Zhai Y., Komatsu T.,
RA Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L.,
RA Goldberg A.L., Shen Y., Qiu X.B.;
RT "Acetylation-mediated proteasomal degradation of core histones during DNA
RT repair and spermatogenesis.";
RL Cell 153:1012-1024(2013).
RN [20]
RP STRUCTURE OF THE PROTEASOME BY ELECTRON MICROSCOPY.
RX PubMed=16952374; DOI=10.1016/j.jmb.2006.08.010;
RA Iwanczyk J., Sadre-Bazzaz K., Ferrell K., Kondrashkina E., Formosa T.,
RA Hill C.P., Ortega J.;
RT "Structure of the Blm10-20 S proteasome complex by cryo-electron
RT microscopy. Insights into the mechanism of activation of mature yeast
RT proteasomes.";
RL J. Mol. Biol. 363:648-659(2006).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 79-2143 IN COMPLEX WITH THE
RP PROTEASOME, FUNCTION, AND MUTAGENESIS OF 2141-TYR--ALA-2143.
RX PubMed=20227375; DOI=10.1016/j.molcel.2010.02.002;
RA Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.;
RT "Structure of a Blm10 complex reveals common mechanisms for proteasome
RT binding and gate opening.";
RL Mol. Cell 37:728-735(2010).
CC -!- FUNCTION: Associated component of the proteasome that specifically
CC recognizes acetylated histones and promotes ATP- and ubiquitin-
CC independent degradation of core histones during DNA damage response.
CC Recognizes and binds acetylated histones via its bromodomain-like
CC (BRDL) region and activates the proteasome by opening the gated channel
CC for substrate entry. Binds to the core proteasome via its C-terminus,
CC which occupies the same binding sites as the proteasomal ATPases,
CC opening the closed structure of the proteasome via an active gating
CC mechanism. Involved in DNA damage response in somatic cells: binds to
CC acetylated histones and promotes degradation of histones following DNA
CC double-strand breaks. {ECO:0000269|PubMed:11842813,
CC ECO:0000269|PubMed:12973301, ECO:0000269|PubMed:15778719,
CC ECO:0000269|PubMed:18927584, ECO:0000269|PubMed:20227375,
CC ECO:0000269|PubMed:22025621, ECO:0000269|PubMed:23706739}.
CC -!- SUBUNIT: According to PubMed:12973301, colocalizes with nascent
CC proteasome. According to PubMed:15778719, associates with proteasome
CC core particles and also forms a complex with regulatory particle-core
CC particle (RP-CP). {ECO:0000269|PubMed:12973301,
CC ECO:0000269|PubMed:15778719, ECO:0000269|PubMed:20227375}.
CC -!- INTERACTION:
CC P43583; P32835: GSP1; NbExp=2; IntAct=EBI-22761, EBI-7926;
CC P43583; P30656: PRE2; NbExp=3; IntAct=EBI-22761, EBI-14001;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- DOMAIN: The bromodomain-like (BRDL) region specifically recognizes and
CC binds acetylated histones. {ECO:0000269|PubMed:23706739}.
CC -!- DOMAIN: The YYX motif is required for the association with the
CC proteasome. {ECO:0000269|PubMed:22025621}.
CC -!- MISCELLANEOUS: Present with 2600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BLM10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09231.1; Type=Frameshift; Note=Produces 2 separate ORFs.; Evidence={ECO:0000305};
CC Sequence=BAA09232.1; Type=Frameshift; Note=Produces 2 separate ORFs.; Evidence={ECO:0000305};
CC Sequence=Ref.6; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D50617; BAA09231.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D50617; BAA09232.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY693254; AAT93273.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12433.1; -; Genomic_DNA.
DR PIR; S56247; S56247.
DR PIR; S56248; S56248.
DR RefSeq; NP_116648.2; NM_001179959.1.
DR PDB; 4V7O; X-ray; 3.00 A; A5/A7/B4/B7=239-1037, A6/A8/B5/B8=1147-2143, AE/AF/B3/B6=79-154.
DR PDBsum; 4V7O; -.
DR AlphaFoldDB; P43583; -.
DR SMR; P43583; -.
DR BioGRID; 31140; 316.
DR DIP; DIP-6344N; -.
DR IntAct; P43583; 16.
DR MINT; P43583; -.
DR STRING; 4932.YFL007W; -.
DR CarbonylDB; P43583; -.
DR iPTMnet; P43583; -.
DR MaxQB; P43583; -.
DR PaxDb; P43583; -.
DR PRIDE; P43583; -.
DR EnsemblFungi; YFL007W_mRNA; YFL007W; YFL007W.
DR GeneID; 850541; -.
DR KEGG; sce:YFL007W; -.
DR SGD; S000001887; BLM10.
DR VEuPathDB; FungiDB:YFL007W; -.
DR eggNOG; KOG1851; Eukaryota.
DR GeneTree; ENSGT00390000011433; -.
DR HOGENOM; CLU_000772_0_0_1; -.
DR InParanoid; P43583; -.
DR OMA; GKDWSDE; -.
DR BioCyc; YEAST:G3O-30449-MON; -.
DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P43583; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43583; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0016504; F:peptidase activator activity; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0043248; P:proteasome assembly; IMP:SGD.
DR GO; GO:1990236; P:proteasome core complex import into nucleus; IMP:SGD.
DR GO; GO:1902906; P:proteasome storage granule assembly; IMP:SGD.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032430; Blm10_mid.
DR InterPro; IPR032372; Blm10_N.
DR InterPro; IPR035309; PSME4.
DR InterPro; IPR021843; PSME4_C.
DR PANTHER; PTHR32170; PTHR32170; 1.
DR Pfam; PF16507; BLM10_mid; 1.
DR Pfam; PF16547; BLM10_N; 1.
DR Pfam; PF11919; DUF3437; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2143
FT /note="Proteasome activator BLM10"
FT /id="PRO_0000076182"
FT REPEAT 1316..1355
FT /note="HEAT 1"
FT REPEAT 1779..1814
FT /note="HEAT 2"
FT REPEAT 1902..1941
FT /note="HEAT 3"
FT REPEAT 1985..2023
FT /note="HEAT 4"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1732
FT /note="Bromodomain-like (BRDL)"
FT MOTIF 2141..2143
FT /note="YYX motif"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MUTAGEN 1663..1664
FT /note="YN->HD: Abolihes binding to acetylated histones."
FT /evidence="ECO:0000269|PubMed:23706739"
FT MUTAGEN 2139
FT /note="R->D: Does not affect binding to the proteasome."
FT /evidence="ECO:0000269|PubMed:22025621"
FT MUTAGEN 2140
FT /note="S->H: Abolishes binding to the proteasome."
FT /evidence="ECO:0000269|PubMed:22025621"
FT MUTAGEN 2141..2143
FT /note="Missing: Loss of function."
FT /evidence="ECO:0000269|PubMed:20227375"
FT MUTAGEN 2141
FT /note="Y->M: Does not affect viability in the presence of
FT cycloheximide."
FT /evidence="ECO:0000269|PubMed:22025621"
FT MUTAGEN 2142
FT /note="Y->A,V: Loss of function; abolishes binding to the
FT proteasome."
FT /evidence="ECO:0000269|PubMed:22025621"
FT MUTAGEN 2142
FT /note="Y->V: Abolishes binding to the proteasome."
FT /evidence="ECO:0000269|PubMed:22025621"
FT MUTAGEN 2143
FT /note="A->S: Does not affect viability in the presence of
FT cycloheximide."
FT /evidence="ECO:0000269|PubMed:22025621"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 133..153
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 422..443
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 465..480
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 488..496
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 508..522
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 531..552
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 553..559
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 568..586
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 591..606
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 612..627
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 628..633
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 635..646
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 649..652
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 658..661
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 662..671
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 678..693
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 709..712
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 714..725
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 739..747
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 748..750
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 751..765
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 773..787
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 791..806
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 819..831
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 833..835
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 836..852
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 853..856
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 861..863
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 866..868
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 869..882
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 883..885
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 886..890
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 893..905
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 910..916
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 919..928
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 937..941
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 953..956
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 957..960
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 962..964
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 974..997
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1009..1023
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1026..1029
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1032..1035
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1158..1161
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1162..1165
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1167..1193
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1199..1211
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1215..1217
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1231..1238
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1249..1266
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1276..1288
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1293..1307
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1308..1310
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1313..1330
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1335..1343
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1347..1352
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1353..1355
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1357..1369
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1374..1377
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1378..1380
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1381..1390
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1404..1406
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1408..1410
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1420..1427
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1430..1451
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1460..1471
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1481..1488
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1489..1493
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1496..1506
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1508..1519
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1523..1526
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1527..1530
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1536..1541
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1544..1546
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1547..1554
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1577..1582
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1593..1603
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1608..1620
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1621..1625
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1630..1643
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1652..1654
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1655..1661
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1668..1681
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1690..1692
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1693..1708
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1716..1730
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1733..1735
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1737..1743
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1764..1774
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1782..1787
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1795..1810
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1820..1828
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1831..1834
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1843..1856
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1858..1861
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1869..1873
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1875..1890
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1893..1895
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1896..1899
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1900..1902
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1903..1907
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1908..1911
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1919..1923
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1929..1934
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1936..1938
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1942..1951
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1955..1958
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 1961..1963
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1964..1978
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1979..1981
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1986..1989
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 1991..1994
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 1995..1999
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2004..2019
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2024..2034
FT /evidence="ECO:0007829|PDB:4V7O"
FT TURN 2039..2041
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2045..2054
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2056..2069
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2081..2090
FT /evidence="ECO:0007829|PDB:4V7O"
FT STRAND 2093..2095
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2099..2102
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2104..2113
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2118..2121
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2122..2124
FT /evidence="ECO:0007829|PDB:4V7O"
FT HELIX 2131..2133
FT /evidence="ECO:0007829|PDB:4V7O"
SQ SEQUENCE 2143 AA; 245996 MW; A195A4455C687644 CRC64;
MTANNDDDIK SPIPITNKTL SQLKRFERSP GRPSSSQGEI KRKKSRLYAA DGRPHSPLRA
RSATPTLQDQ KLFNGMDSTS LLNERLQHYT LDYVSDRAQH MKNIYDPSSR WFSRSVRPEF
PIEEFLPYKT ESHEDQAKYL CHVLVNLYIA ISSLDIQGLI SISSKDLADL KKEVDDLALK
TDLFRLSNNT AENDLLGNDI ADYDDAEGLE DELDEYFDLA GPDFNATGKI TAKSATIVNV
NHWTNELKNC LHFDFPVALR KSLATVYYYL SLVQGQKVYR QMHVDMFERL VSLDDDRTNF
TELLQKQGLL LDHQIMLNFL CEFLPYPDPD YARYELSSKE DLQLFRLLLK HAHNAKPFFD
KSKESLLVDT MNFLLSSLAP STMMAVMPIV TSVVPYHYHI HSKIIDYFPF CYSIWSSVSA
NVAIDTHMYD FVGSISKDVH NKILSSEHEK DVVGVEFGEF GIFTDDQMTF MFNRLQGHLR
TDGQIHSYSR TVKPFVYAIN GSKKDRFFEK LVSLAKAIET FIHPSNNGFW TKPNAKFVHA
FIKSYHGRVK YEEDICARGV TNGICLTSFC HEEIVEIFLN IISLGSQNKN PDIANYYISC
FAYLLELDPS NAYLIYDKIL IDLYDTLADQ FINSRHRIIS SLKQFTRVIR FIVMDKLYRV
HITNVLSMLV SKLDMNDTNL TSNLINGIVS IAAFIPIQDL TGEDDYISFE SDTLPLVQQH
FYHIKCGESS KTFRVDDELL NNAFKASTTV FQSMLKVYVE KIFQLVDVDL EDSLVTKINQ
TTMILQESMD DKIFNYFASL LQRNFWSNDS FKEKDPNYEL VTIPLAALVR RNNGLSKELV
RTLLFHIKEQ IKRGAGSVRS TSEIQQRDVK LVLYLTALND VLRQCHESLL EYSDELITFM
KYLYDNVTNP PLDVITSIVI HSALATLCTT EITDCRLFPE DSKIPEKDRW GGLQFDPRRF
DKQHLSFQWH VPSSDEITLS ISILESLSEY CINNVEELMK APRHDSEYGD MIQKYVLVMT
HTLSGSSLLF DPDFNKYRTQ SNLSYREKLI LLKNIRENNC DPQELDIDIE QIRSGKDDED
YIESKDIEAG LNAGVSDVVQ LRDEFPDELI VDEEVVSEMP SGVNTPIAGT HGTDNSAMSS
DLAFRDLDIY TCNYYFGNTT EEKLQNPQYL QVHRVRARIG HFFHKLYVFL STNFENNTNM
FQILLHGLKV WFTDLGQETV FNEDPNAFID VDFLENVQSL SHVNEPFTRT NFAIRANSLH
QSRVLLHSTN RKASKLENLL LVDIIQLATS LYPDIYKPAQ GTLVHCMKQL VGSYGVVINK
IIPSLEKAIK DHDYMKIQVI LNVLLIKKIH RKLMTDYKDI GRLIFLLIEC CRVNELEIGM
YADKILTDIV IGIKIPSSVC VISDQAFLPL APPDGTINLQ VEAVKLAKKK KREYYLSLLV
DLQDKLLDKL DNEKDMGWKI RMFILRFVTQ IQSNLESKPD KRAVFSIISQ ISTKHPEIIH
LVVKSLLSTC NKIISLSDYE YDITRAYKNE FNPSFVEILD TSTTSFPKTF TEEMNNFDNP
KYFIDLRAYV GWLCWGRLMY VMSPKALKLN LRENELEVLK TAGHLLTREF LRDVTMNLVQ
DNETRGVFSS GNVSFFSLVI LLISSGFCEL NMSDLFELCE SYYNKDDKAS MIMSVEIVAG
LVCGSKFMSV SDLDKRDTFI ENFLAKCLDY ELNHDAFEIW STLAWWLPAV VDLRRSKTFF
CHFINADGMF DRESDAATHQ TSKIYMLRSI LMSMEFRAPD VGKLFDELVF DHPYDQVRQA
VAKLLTTLVQ NQSNPSISDP TTLLEAERND PDGLGLPLKS VPEKVDAYIK KQFEIIKNLE
DSVVGLNPQQ FIKTDYFYRT STIFYWIKEM ARGPNKVLLV PYLVDYVLPF LIGLVKHKDV
CALASLDPVR LYAGLGYMPI RKNHVAAIVD YVCSSNVALS SNQTKLQLAF IQHFLSAELL
QLTEEEKNKI LEFVVSNLYN EQFVEVRVRA ASILSDIVHN WKEEQPLLSL IERFAKGLDV
NKYTSKERQK LSKTDIKIHG NVLGLGAIIS AFPYVFPLPP WIPKQLSNLS SWARTSGMTG
QAAKNTISEF KKVRADTWKF DRASFNTEEL EDLEGVLWRS YYA
