TRA1_YEAST
ID TRA1_YEAST Reviewed; 3744 AA.
AC P38811; D3DL49;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Transcription-associated protein 1;
DE AltName: Full=p400 kDa component of SAGA;
GN Name=TRA1; OrderedLocusNames=YHR099W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 PROTEIN SEQUENCE OF 149-164; 353-360; 438-445; 603-614; 751-760; 1060-1070;
RP 1124-1134; 1311-1324; 1399-1412; 1451-1464; 1643-1658; 2197-2208;
RP 2389-2399; 2401-2425; 2536-2550; 2601-2612; 2703-2713; 2797-2807;
RP 3239-3247; 3440-3456; 3479-3492 AND 3681-3689, AND IDENTIFICATION IN A SAGA
RP COMPLEX WITH SPT2; SPT7; SPT8; SPT20; HFI1; ADA2; ADA3 AND GCN5.
RX PubMed=9885573; DOI=10.1016/s1097-2765(00)80300-7;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.;
RT "The ATM-related cofactor Tra1 is a component of the purified SAGA
RT complex.";
RL Mol. Cell 2:863-867(1998).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH ADA3 AND SPT7.
RX PubMed=9756893; DOI=10.1074/jbc.273.41.26559;
RA Saleh A., Schieltz D., Ting N., McMahon S.B., Litchfield D.W.,
RA Yates J.R. III, Lees-Miller S.P., Cole M.D., Brandl C.J.;
RT "Tra1p is a component of the yeast Ada.Spt transcriptional regulatory
RT complexes.";
RL J. Biol. Chem. 273:26559-26565(1998).
RN [5]
RP IDENTIFICATION IN A NUA4 COMPLEX WITH ESA1.
RX PubMed=10487762; DOI=10.1093/emboj/18.18.5108;
RA Allard S., Utley R.T., Savard J., Clarke A.S., Grant P.A., Brandl C.J.,
RA Pillus L., Workman J.L., Cote J.;
RT "NuA4, an essential transcription adaptor/histone H4 acetyltransferase
RT complex containing Esa1p and the ATM-related cofactor Tra1p.";
RL EMBO J. 18:5108-5119(1999).
RN [6]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [7]
RP FUNCTION, AND MUTANT TRA1-2.
RX PubMed=11423663; DOI=10.1126/science.1060214;
RA Brown C.E., Howe L., Sousa K., Alley S.C., Carrozza M.J., Tan S.,
RA Workman J.L.;
RT "Recruitment of HAT complexes by direct activator interactions with the
RT ATM-related Tra1 subunit.";
RL Science 292:2333-2337(2001).
RN [8]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [9]
RP IDENTIFICATION IN THE SALSA COMPLEX.
RX PubMed=12186975; DOI=10.1073/pnas.182021199;
RA Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT with activated transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN [10]
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 [11]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-542, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-542, AND
RP 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 [14]
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 [15]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
CC -!- FUNCTION: Essential component of histone acetyltransferase (HAT)
CC complexes, which serves as a target for activators during recruitment
CC of HAT complexes. Essential for vegetative growth. Functions as a
CC component of the transcription regulatory histone acetylation (HAT)
CC complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-
CC dependent transcriptional regulation of approximately 10% of yeast
CC genes. At the promoters, SAGA is required for recruitment of the basal
CC transcription machinery. It influences RNA polymerase II
CC transcriptional activity through different activities such as TBP
CC interaction (SPT3, SPT8 and SPT20) and promoter selectivity,
CC interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1),
CC and chromatin modification through histone acetylation (GCN5) and
CC deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some
CC extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts
CC with DNA via upstream activating sequences (UASs). SALSA, an altered
CC form of SAGA, may be involved in positive transcriptional regulation.
CC SLIK is proposed to have partly overlapping functions with SAGA. It
CC preferentially acetylates methylated histone H3, at least after
CC activation at the GAL1-10 locus. {ECO:0000269|PubMed:10026213,
CC ECO:0000269|PubMed:11423663}.
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC copies. SAGA is built of 5 distinct domains with specialized functions.
CC Domain I (containing TRA1) probably represents the activator
CC interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC an architectural role. Domain III also harbors the HAT activity. Domain
CC V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA.
CC Component of the SALSA complex, which consists of at least TRA1, SPT7
CC (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1,
CC GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of
CC at least TRA1, CHD1, SPT7,TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1,
CC UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Also identified in the
CC NuA4 complex with ESA1. Identified in the Ada.spt complex with ADA3 and
CC SPT7. {ECO:0000269|PubMed:10487762, ECO:0000269|PubMed:12186975,
CC ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:15647753,
CC ECO:0000269|PubMed:9756893, ECO:0000269|PubMed:9885573}.
CC -!- INTERACTION:
CC P38811; Q02336: ADA2; NbExp=26; IntAct=EBI-24638, EBI-2186;
CC P38811; Q08649: ESA1; NbExp=10; IntAct=EBI-24638, EBI-6648;
CC P38811; Q12060: HFI1; NbExp=8; IntAct=EBI-24638, EBI-8287;
CC P38811; P32494: NGG1; NbExp=3; IntAct=EBI-24638, EBI-2192;
CC P38811; P35177: SPT7; NbExp=10; IntAct=EBI-24638, EBI-17958;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The C-terminal domain (2233-2836) is essential for its ability
CC to interact with activators.
CC -!- MISCELLANEOUS: Although strongly related to the PI3/PI4-kinase family,
CC it lacks the typical motifs that constitute the catalytic site of
CC PI3/PI4-kinase proteins, suggesting that it may lack such activity.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
CC {ECO:0000305}.
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DR EMBL; U00060; AAB68923.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06793.1; -; Genomic_DNA.
DR PIR; S46715; S46715.
DR RefSeq; NP_011967.1; NM_001179229.1.
DR PDB; 5OJS; EM; 3.70 A; T=1-3744.
DR PDB; 6IG9; EM; 4.60 A; T=1-3744.
DR PDB; 6T9I; EM; 3.90 A; T=1-3744.
DR PDB; 6T9J; EM; 3.40 A; T=1-3744.
DR PDBsum; 5OJS; -.
DR PDBsum; 6IG9; -.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9J; -.
DR SMR; P38811; -.
DR BioGRID; 36532; 270.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-805N; -.
DR IntAct; P38811; 73.
DR MINT; P38811; -.
DR STRING; 4932.YHR099W; -.
DR iPTMnet; P38811; -.
DR MaxQB; P38811; -.
DR PaxDb; P38811; -.
DR PRIDE; P38811; -.
DR EnsemblFungi; YHR099W_mRNA; YHR099W; YHR099W.
DR GeneID; 856499; -.
DR KEGG; sce:YHR099W; -.
DR SGD; S000001141; TRA1.
DR VEuPathDB; FungiDB:YHR099W; -.
DR eggNOG; KOG0889; Eukaryota.
DR GeneTree; ENSGT00390000017961; -.
DR HOGENOM; CLU_000129_1_0_1; -.
DR InParanoid; P38811; -.
DR OMA; NPIFAMD; -.
DR BioCyc; YEAST:G3O-31144-MON; -.
DR PRO; PR:P38811; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38811; protein.
DR GO; GO:0070209; C:ASTRA complex; HDA:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR033317; TRA1/TRRAP.
DR PANTHER; PTHR11139:SF1; PTHR11139:SF1; 2.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Chromatin regulator;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..3744
FT /note="Transcription-associated protein 1"
FT /id="PRO_0000088854"
FT DOMAIN 2622..3177
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 3374..3732
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 3712..3744
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 185..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3380..3386
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3563..3571
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3600..3625
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 185..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 241
FT /note="L->S: In TRA1-2; when associated with L-604; R-2733;
FT P-3145; S-3222 and G-3302. Defects in its ability to
FT interact with acidic activators."
FT MUTAGEN 604
FT /note="F->L: In TRA1-2; when associated with S-241; R-2733;
FT P-3145; S-3222 and G-3302. Defects in its ability to
FT interact with acidic activators."
FT MUTAGEN 2733
FT /note="W->R: In TRA1-2; when associated with S-241; L-604;
FT P-3145; S-3222 and G-3302. Defects in its ability to
FT interact with acidic activators."
FT MUTAGEN 3145
FT /note="S->P: In TRA1-2; when associated with S-241; L-604;
FT R-2733; S-3222 and G-3302. Defects in its ability to
FT interact with acidic activators."
FT MUTAGEN 3222
FT /note="L->S: In TRA1-2; when associated with S-241; L-604;
FT R-2733; P-3145 and G-3302. Defects in its ability to
FT interact with acidic activators."
FT MUTAGEN 3302
FT /note="D->G: In TRA1-2; when associated with S-241; L-604;
FT R-2733; P-3145 and S-3222. Defects in its ability to
FT interact with acidic activators."
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 342..355
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 388..402
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 408..423
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 429..452
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 457..479
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 482..497
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 498..502
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 513..519
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 562..566
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 579..600
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 608..612
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 616..621
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 628..643
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 677..689
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 695..713
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 720..727
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 733..747
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 751..754
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 756..775
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 776..779
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 782..784
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 789..798
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 807..818
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 828..830
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 832..843
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 854..862
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 868..871
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 880..888
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 891..893
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 894..906
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 909..912
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 914..916
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 918..920
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 921..928
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 929..931
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 939..942
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 943..951
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 952..954
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 955..959
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 977..980
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 985..987
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 989..993
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 997..1005
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1011..1030
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1039..1048
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1069..1088
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1089..1091
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1096..1120
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1121..1123
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1124..1129
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1146..1148
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1149..1153
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1158..1179
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1181..1184
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1189..1200
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1203..1205
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1206..1222
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1229..1232
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1234..1246
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1255..1271
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1284..1293
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1294..1297
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1301..1312
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1313..1317
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1322..1325
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1326..1329
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1330..1339
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1342..1345
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1347..1362
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1363..1365
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1372..1382
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1387..1389
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1397..1399
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1402..1404
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1405..1423
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1426..1428
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1429..1436
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1437..1446
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1447..1449
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1453..1466
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1467..1469
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1478..1481
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1483..1488
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1497..1507
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1518..1527
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1533..1537
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1538..1540
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1543..1545
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1547..1557
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1558..1561
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1568..1570
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1571..1583
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1594..1603
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1606..1612
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1618..1628
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1634..1641
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1644..1658
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1662..1678
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1679..1682
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1691..1708
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1716..1733
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1735..1737
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1740..1749
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1751..1754
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1759..1761
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1763..1769
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1772..1774
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1778..1791
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1797..1816
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1826..1828
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1834..1842
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1843..1846
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1847..1849
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1850..1852
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1859..1874
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1876..1878
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1883..1892
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1893..1895
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1900..1915
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1921..1930
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1936..1938
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1939..1957
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 1960..1962
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1965..1976
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 1983..1987
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 1988..1991
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2002..2014
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2025..2042
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2091..2106
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2117..2128
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2156..2172
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2173..2175
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2176..2178
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2180..2183
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2184..2195
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2204..2216
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2222..2225
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2229..2244
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2252..2266
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2276..2289
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2290..2293
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2294..2297
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2303..2320
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2329..2341
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2346..2360
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2370..2377
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2378..2381
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2382..2385
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2388..2401
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2413..2417
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2418..2423
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2425..2427
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2429..2442
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2447..2455
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2461..2463
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2469..2476
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2477..2479
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2488..2491
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2497..2499
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2500..2502
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2519..2533
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2538..2549
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2554..2567
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2568..2570
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2576..2587
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2590..2595
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2602..2610
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2611..2613
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2614..2616
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2623..2626
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2629..2631
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2633..2644
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2652..2654
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2655..2668
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2672..2682
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2686..2697
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2700..2715
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2722..2724
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2725..2739
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2743..2752
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2756..2760
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2762..2765
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2773..2783
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2789..2805
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 2806..2808
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2813..2830
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2839..2863
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2865..2867
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2870..2872
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2874..2885
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2895..2915
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2921..2923
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2943..2956
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2960..2965
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 2966..2972
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2980..2991
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 2999..3006
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3018..3032
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3037..3047
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 3048..3050
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3054..3068
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3078..3090
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3094..3096
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3098..3108
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3116..3122
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3131..3136
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3137..3141
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 3142..3145
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3146..3148
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3152..3162
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3164..3179
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3203..3217
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3220..3236
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3241..3259
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3264..3266
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3274..3285
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 3289..3292
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3293..3296
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3297..3299
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3301..3303
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3306..3308
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3309..3326
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3330..3332
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3334..3337
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3339..3342
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3344..3347
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3357..3360
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3370..3374
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3376..3382
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3387..3395
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3400..3408
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3413..3425
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 3426..3428
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3429..3432
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3434..3438
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3448..3454
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3456..3459
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3462..3466
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3467..3477
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3483..3494
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3497..3500
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3506..3520
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3526..3534
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3535..3537
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3538..3560
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3561..3563
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3571..3575
FT /evidence="ECO:0007829|PDB:6T9J"
FT TURN 3576..3578
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3581..3584
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3601..3604
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3619..3622
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3626..3632
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3635..3639
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3641..3653
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3656..3658
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3659..3677
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3686..3706
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 3716..3718
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3719..3726
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 3730..3733
FT /evidence="ECO:0007829|PDB:6T9J"
SQ SEQUENCE 3744 AA; 433180 MW; AE3588676F5D5777 CRC64;
MSLTEQIEQF ASRFRDDDAT LQSRYSTLSE LYDIMELLNS PEDYHFFLQA VIPLLLNQLK
EVPISYDAHS PEQKLRNSML DIFNRCLMNQ TFQPYAMEVL EFLLSVLPKE NEENGILCMK
VLTTLFKSFK SILQDKLDSF IRIIIQIYKN TPNLINQTFY EAGKAEQGDL DSPKEPQADE
LLDEFSKNDE EKDFPSKQSS TEPRFENSTS SNGLRSSMFS FKILSECPIT MVTLYSSYKQ
LTSTSLPEFT PLIMNLLNIQ IKQQQEAREQ AESRGEHFTS ISTEIINRPA YCDFILAQIK
ATSFLAYVFI RGYAPEFLQD YVNFVPDLII RLLQDCPSEL SSARKELLHA TRHILSTNYK
KLFLPKLDYL FDERILIGNG FTMHETLRPL AYSTVADFIH NIRSELQLSE IEKTIKIYTG
YLLDESLALT VQIMSAKLLL NLVERILKLG KENPQEAPRA KKLLMIIIDS YMNRFKTLNR
QYDTIMKYYG RYETHKKEKA EKLKNSIQDN DKESEEFMRK VLEPSDDDHL MPQPKKEDIN
DSPDVEMTES DKVVKNDVEM FDIKNYAPIL LLPTPTNDPI KDAFYLYRTL MSFLKTIIHD
LKVFNPPPNE YTVANPKLWA SVSRVFSYEE VIVFKDLFHE CIIGLKFFKD HNEKLSPETT
KKHFDISMPS LPVSATKDAR ELMDYLAFMF MQMDNATFNE IIEQELPFVY ERMLEDSGLL
HVAQSFLTSE ITSPNFAGIL LRFLKGKLKD LGNVDFNTSN VLIRLFKLSF MSVNLFPNIN
EVVLLPHLND LILNSLKYST TAEEPLVYFY LIRTLFRSIG GGRFENLYRS IKPILQVLLQ
SLNQMILTAR LPHERELYVE LCITVPVRLS VLAPYLPFLM KPLVFALQQY PDLVSQGLRT
LELCIDNLTA EYFDPIIEPV IDDVSKALFN LLQPQPFNHA ISHNVVRILG KLGGRNRQFL
KPPTDLTEKT ELDIDAIADF KINGMPEDVP LSVTPGIQSA LNILQSYKSD IHYRKSAYKY
LTCVLLLMTK SSAEFPTNYT ELLKTAVNSI KLERIGIEKN FDLEPTVNKR DYSNQENLFL
RLLESVFYAT SIKELKDDAM DLLNNLLDHF CLLQVNTTLL NKRNYNGTFN IDLKNPNFML
DSSLILDAIP FALSYYIPEV REVGVLAYKR IYEKSCLIYG EELALSHSFI PELAKQFIHL
CYDETYYNKR GGVLGIKVLI DNVKSSSVFL KKYQYNLANG LLFVLKDTQS EAPSAITDSA
EKLLIDLLSI TFADVKEEDL GNKVLENTLT DIVCELSNAN PKVRNACQKS LHTISNLTGI
PIVKLMDHSK QFLLSPIFAK PLRALPFTMQ IGNVDAITFC LSLPNTFLTF NEELFRLLQE
SIVLADAEDE SLSTNIQKTT EYSTSEQLVQ LRIACIKLLA IALKNEEFAT AQQGNIRIRI
LAVFFKTMLK TSPEIINTTY EALKGSLAEN SKLPKELLQN GLKPLLMNLS DHQKLTVPGL
DALSKLLELL IAYFKVEIGR KLLDHLTAWC RVEVLDTLFG QDLAEQMPTK IIVSIINIFH
LLPPQADMFL NDLLLKVMLL ERKLRLQLDS PFRTPLARYL NRFHNPVTEY FKKNMTLRQL
VLFMCNIVQR PEAKELAEDF EKELDNFYDF YISNIPKNQV RVVSFFTNMV DLFNTMVITN
GDEWLKKKGN MILKLKDMLN LTLKTIKENS FYIDHLQLNQ SIAKFQALYL RFTELSERDQ
NPLLLDFIDF SFSNGIKASY SLKKFIFHNI IASSNKEKQN NFINDATLFV LSDKCLDARI
FVLKNVINST LIYEVATSGS LKSYLVEDKK PKWLELLHNK IWKNSNAILA YDVLDHHDLF
RFELLQLSAI FIKADPEIIA EIKKDIIKFC WNFIKLEDTL IKQSAYLVTS YFISKFDFPI
KVVTQVFVAL LRSSHVEARY LVKQSLDVLT PVLHERMNAA GTPDTWINWV KRVMVENSSS
QNNILYQFLI SHPDLFFNSR DLFISNIIHH MNKITFMSNS NSDSHTLAID LASLILYWEN
KTLEITNVNN TKTDSDGDVV MSDSKSDINP VEADTTAIIV DANNNSPISL HLREACTAFL
IRYVCASNHR AIETELGLRA INILSELISD KHWTNVNVKL VYFEKFLIFQ DLDSENILYY
CMNALDVLYV FFKNKTKEWI MENLPTIQNL LEKCIKSDHH DVQEALQKVL QVIMKAIKAQ
GVSVIIEEES PGKTFIQMLT SVITQDLQET SSVTAGVTLA WVLFMNFPDN IVPLLTPLMK
TFSKLCKDHL SISQPKDAMA LEEARITTKL LEKVLYILSL KVSLLGDSRR PFLSTVALLI
DHSMDQNFLR KIVNMSRSWI FNTEIFPTVK EKAAILTKML AFEIRGEPSL SKLFYEIVLK
LFDQEHFNNT EITVRMEQPF LVGTRVEDIG IRKRFMTILD NSLERDIKER LYYVIRDQNW
EFIADYPWLN QALQLLYGSF NREKELSLKN IYCLSPPSIL QEYLPENAEM VTEVNDLELS
NFVKGHIASM QGLCRIISSD FIDSLIEIFY QDPKAIHRAW VTLFPQVYKS IPKNEKYGFV
RSIITLLSKP YHTRQISSRT NVINMLLDSI SKIESLELPP HLVKYLAISY NAWYQSINIL
ESIQSNTSID NTKIIEANED ALLELYVNLQ EEDMFYGLWR RRAKYTETNI GLSYEQIGLW
DKAQQLYEVA QVKARSGALP YSQSEYALWE DNWIQCAEKL QHWDVLTELA KHEGFTDLLL
ECGWRVADWN SDRDALEQSV KSVMDVPTPR RQMFKTFLAL QNFAESRKGD QEVRKLCDEG
IQLSLIKWVS LPIRYTPAHK WLLHGFQQYM EFLEATQIYA NLHTTTVQNL DSKAQEIKRI
LQAWRDRLPN TWDDVNMWND LVTWRQHAFQ VINNAYLPLI PALQQSNSNS NINTHAYRGY
HEIAWVINRF AHVARKHNMP DVCISQLARI YTLPNIEIQE AFLKLREQAK CHYQNMNELT
TGLDVISNTN LVYFGTVQKA EFFTLKGMFL SKLRAYEEAN QAFATAVQID LNLAKAWAQW
GFFNDRRLSE EPNNISFASN AISCYLQAAG LYKNSKIREL LCRILWLISI DDASGMLTNA
FDSFRGEIPV WYWITFIPQL LTSLSHKEAN MVRHILIRIA KSYPQALHFQ LRTTKEDFAV
IQRQTMAVMG DKPDTNDRNG RRQPWEYLQE LNNILKTAYP LLALSLESLV AQINDRFKST
TDEDLFRLIN VLLIDGTLNY NRLPFPRKNP KLPENTEKNL VKFSTTLLAP YIRPKFNADF
IDNKPDYETY IKRLRYWRRR LENKLDRASK KENLEVLCPH LSNFHHQKFE DIEIPGQYLL
NKDNNVHFIK IARFLPTVDF VRGTHSSYRR LMIRGHDGSV HSFAVQYPAV RHSRREERMF
QLYRLFNKSL SKNVETRRRS IQFNLPIAIP LSPQVRIMND SVSFTTLHEI HNEFCKKKGF
DPDDIQDFMA DKLNAAHDDA LPAPDMTILK VEIFNSIQTM FVPSNVLKDH FTSLFTQFED
FWLFRKQFAS QYSSFVFMSY MMMINNRTPH KIHVDKTSGN VFTLEMLPSR FPYERVKPLL
KNHDLSLPPD SPIFHNNEPV PFRLTPNIQS LIGDSALEGI FAVNLFTISR ALIEPDNELN
TYLALFIRDE IISWFSNLHR PIIENPQLRE MVQTNVDLII RKVAQLGHLN STPTVTTQFI
LDCIGSAVSP RNLARTDVNF MPWF
