THO2_YEAST
ID THO2_YEAST Reviewed; 1597 AA.
AC P53552; D6W142;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=THO complex subunit 2;
DE AltName: Full=Low dye-binding protein 5;
DE AltName: Full=THO complex subunit RLR1;
DE AltName: Full=Zinc-regulated gene 13 protein;
GN Name=THO2; Synonyms=LDB5, RLR1, ZRG13; OrderedLocusNames=YNL139C;
GN ORFNames=N1209, N1835;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YM256;
RX PubMed=10675628; DOI=10.1016/s0378-1119(99)00510-7;
RA West R.W. Jr., Kruger B., Thomas S., Ma J., Milgrom E.;
RT "RLR1 (THO2), required for expressing lacZ fusions in yeast, is conserved
RT from yeast to humans and is a suppressor of SIN4.";
RL Gene 243:195-205(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP CHARACTERIZATION.
RX PubMed=9707445; DOI=10.1093/emboj/17.16.4859;
RA Piruat J.I., Aguilera A.;
RT "A novel yeast gene, THO2, is involved in RNA pol II transcription and
RT provides new evidence for transcriptional elongation-associated
RT recombination.";
RL EMBO J. 17:4859-4872(1998).
RN [6]
RP IDENTIFICATION IN THO COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11060033; DOI=10.1093/emboj/19.21.5824;
RA Chavez S., Beilharz T., Rondon A.G., Erdjument-Bromage H., Tempst P.,
RA Svejstrup J.Q., Lithgow T., Aguilera A.;
RT "A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2,
RT connects transcription elongation with mitotic recombination in
RT Saccharomyces cerevisiae.";
RL EMBO J. 19:5824-5834(2000).
RN [7]
RP FUNCTION.
RX PubMed=12093753; DOI=10.1093/emboj/cdf335;
RA Jimeno S., Rondon A.G., Luna R., Aguilera A.;
RT "The yeast THO complex and mRNA export factors link RNA metabolism with
RT transcription and genome instability.";
RL EMBO J. 21:3526-3535(2002).
RN [8]
RP IDENTIFICATION IN TREX COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11979277; DOI=10.1038/nature746;
RA Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M.,
RA Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R.,
RA Hurt E.;
RT "TREX is a conserved complex coupling transcription with messenger RNA
RT export.";
RL Nature 417:304-308(2002).
RN [9]
RP FUNCTION.
RX PubMed=12871933; DOI=10.1074/jbc.m305718200;
RA Rondon A.G., Jimeno S., Garcia-Rubio M., Aguilera A.;
RT "Molecular evidence that the eukaryotic THO/TREX complex is required for
RT efficient transcription elongation.";
RL J. Biol. Chem. 278:39037-39043(2003).
RN [10]
RP FUNCTION.
RX PubMed=14527416; DOI=10.1016/j.molcel.2003.08.010;
RA Huertas P., Aguilera A.;
RT "Cotranscriptionally formed DNA:RNA hybrids mediate transcription
RT elongation impairment and transcription-associated recombination.";
RL Mol. Cell 12:711-721(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 FUNCTION.
RX PubMed=15192704; DOI=10.1038/sj.emboj.7600261;
RA Abruzzi K.C., Lacadie S., Rosbash M.;
RT "Biochemical analysis of TREX complex recruitment to intronless and intron-
RT containing yeast genes.";
RL EMBO J. 23:2620-2631(2004).
RN [14]
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).
CC -!- FUNCTION: Component the THO subcomplex of the TREX complex, which
CC operates in coupling transcription elongation to mRNA export. The THO
CC complex is recruited to transcribed genes and moves along the gene with
CC the elongating polymerase during transcription. THO is important for
CC stabilizing nascent RNA in the RNA polymerase II elongation complex by
CC preventing formation of DNA:RNA hybrids behind the elongating
CC polymerase. It functions in cotranscriptional formation of an export-
CC competent messenger ribonucleoprotein particle (mRNP) by facilitating
CC the loading of ATP-dependent RNA helicase SUB2 and the mRNA export
CC factor YRA1 along the nascent mRNA. {ECO:0000269|PubMed:12093753,
CC ECO:0000269|PubMed:12871933, ECO:0000269|PubMed:14527416,
CC ECO:0000269|PubMed:15192704}.
CC -!- SUBUNIT: Component of the THO complex, which is composed of HPR1, MFT1,
CC THO2 and THP2. Together with SUB2, TEX1 and YRA1, THO forms the
CC transcription/export (TREX) complex. THO associates with DNA and RNA in
CC vitro. {ECO:0000269|PubMed:11060033, ECO:0000269|PubMed:11979277}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11060033,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the THOC2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U22361; AAA93160.1; -; Genomic_DNA.
DR EMBL; Z46843; CAA86886.1; -; Genomic_DNA.
DR EMBL; Z71416; CAA96023.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10408.1; -; Genomic_DNA.
DR PIR; S55144; S55144.
DR RefSeq; NP_014260.3; NM_001182977.3.
DR PDB; 7APX; EM; 3.40 A; A=1-1597.
DR PDB; 7AQO; EM; 4.50 A; A/G=1-1597.
DR PDB; 7LUV; EM; 3.70 A; C=1-1257.
DR PDBsum; 7APX; -.
DR PDBsum; 7AQO; -.
DR PDBsum; 7LUV; -.
DR AlphaFoldDB; P53552; -.
DR SMR; P53552; -.
DR BioGRID; 35687; 92.
DR ComplexPortal; CPX-1792; THO complex.
DR ComplexPortal; CPX-1793; TREX complex.
DR DIP; DIP-6265N; -.
DR IntAct; P53552; 15.
DR MINT; P53552; -.
DR STRING; 4932.YNL139C; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; P53552; -.
DR MaxQB; P53552; -.
DR PaxDb; P53552; -.
DR PRIDE; P53552; -.
DR EnsemblFungi; YNL139C_mRNA; YNL139C; YNL139C.
DR GeneID; 855583; -.
DR KEGG; sce:YNL139C; -.
DR SGD; S000005083; THO2.
DR VEuPathDB; FungiDB:YNL139C; -.
DR eggNOG; KOG1874; Eukaryota.
DR GeneTree; ENSGT00710000106792; -.
DR HOGENOM; CLU_003123_0_0_1; -.
DR InParanoid; P53552; -.
DR OMA; PEIAFWI; -.
DR BioCyc; YEAST:G3O-33158-MON; -.
DR PRO; PR:P53552; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53552; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0000446; C:nucleoplasmic THO complex; IMP:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IDA:SGD.
DR GO; GO:0000346; C:transcription export complex; IPI:ComplexPortal.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IDA:SGD.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:2001209; P:positive regulation of transcription elongation from RNA polymerase I promoter; IMP:SGD.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:SGD.
DR InterPro; IPR040007; Tho2.
DR InterPro; IPR021418; THO_THOC2_C.
DR InterPro; IPR021726; THO_THOC2_N.
DR InterPro; IPR032302; THOC2_N.
DR PANTHER; PTHR21597; PTHR21597; 1.
DR Pfam; PF11262; Tho2; 1.
DR Pfam; PF11732; Thoc2; 1.
DR Pfam; PF16134; THOC2_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1597
FT /note="THO complex subunit 2"
FT /id="PRO_0000097359"
FT REGION 1250..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 179..193
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 323..342
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 404..413
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 436..455
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 521..535
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 536..541
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 543..559
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 566..579
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 582..585
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 592..602
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 607..619
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 626..643
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 651..664
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 671..679
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 683..690
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 696..711
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 728..741
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 748..757
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 758..760
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 763..775
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 787..792
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 794..796
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 797..806
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 811..814
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 815..826
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 827..829
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 831..846
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 852..876
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 879..884
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 889..894
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 900..916
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 923..929
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 933..935
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 942..950
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 954..956
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 961..969
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 984..992
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 994..1017
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1025..1033
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1036..1039
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1043..1053
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 1054..1057
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1059..1070
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 1071..1073
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1075..1081
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1084..1106
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1114..1132
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1138..1151
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1152..1154
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1159..1169
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1177..1186
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 1187..1191
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 1198..1200
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 1206..1221
FT /evidence="ECO:0007829|PDB:7APX"
SQ SEQUENCE 1597 AA; 183931 MW; 5F1993C3726EF298 CRC64;
MAEQTLLSKL NALSQKVIPP ASPSQASILT EEVIRNWPER SKTLCSDFTA LESNDEKEDW
LRTLFIELFD FINKNDENSP LKLSDVASFT NELVNHERQV SQASIVGKMF IAVSSTVPNI
NDLTTISLCK LIPSLHEELF KFSWISSKLL NKEQTTLLRH LLKKSKYELK KYNLLVENSV
GYGQLVALLI LAYYDPDNFS KVSAYLKEIY HIMGKYSLDS IRTLDVILNV SSQFITEGYK
FFIALLRKSD SWPSSHVANN SNYSSLNEGG NMIAANIISF NLSQYNEEVD KENYERYMDM
CCILLKNGFV NFYSIWDNVK PEMEFLQEYI QNLETELEEE STKGVENPLA MAAALSTENE
TDEDNALVVN DDVNMKDKIS EETNADIESK GKQKTQQDIL LFGKIKLLER LLIHGCVIPV
IHVLKQYPKV LYVSESLSRY LGRVFEYLLN PLYTSMTSSG ESKDMATALM ITRIDNGILA
HKPRLIHKYK THEPFESLEL NSSYVFYYSE WNSNLTPFAS VNDLFENSHI YLSIIGPYLG
RIPTLLSKIS RIGVADIQKN HGSESLHVTI DKWIDYVRKF IFPATSLLQN NPIATSEVYE
LMKFFPFEKR YFIYNEMMTK LSQDILPLKV SFNKAEREAK SILKALSIDT IAKESRRFAK
LISTNPLASL VPAVKQIENY DKVSELVVYT TKYFNDFAYD VLQFVLLLRL TYNRPAVQFD
GVNQAMWVQR LSIFIAGLAK NCPNMDISNI ITYILKTLHN GNIIAVSILK ELIITVGGIR
DLNEVNMKQL LMLNSGSPLK QYARHLIYDF RDDNSVISSR LTSFFTDQSA ISEIILLLYT
LNLKANTQNS HYKILSTRCD EMNTLLWSFI ELIKHCLKGK AFEENVLPFV ELNNRFHLST
PWTFHIWRDY LDNQLNSNEN FSIDELIEGA EFSDVDLTKI SKDLFTTFWR LSLYDIHFDK
SLYDERKNAL SGENTGHMSN RKKHLIQNQI KDILVTGISH QRAFKKTSEF ISEKSNVWNK
DCGEDQIKIF LQNCVVPRVL FSPSDALFSS FFIFMAFRTE NLMSILNTCI TSNILKTLLF
CCTSSEAGNL GLFFTDVLKK LEKMRLNGDF NDQASRKLYE WHSVITEQVI DLLSEKNYMS
IRNGIEFMKH VTSVFPVVKA HIQLVYTTLE ENLINEERED IKLPSSALIG HLKARLKDAL
ELDEFCTLTE EEAEQKRIRE MELEEIKNYE TACQNEQKQV ALRKQLELNK SQRLQNDPPK
SVASGSAGLN SKDRYTYSRN EPVIPTKPSS SQWSYSKVTR HVDDINHYLA TNHLQKAISL
VENDDETRNL RKLSKQNMPI FDFRNSTLEI FERYFRTLIQ NPQNPDFAEK IDSLKRYIKN
ISREPYPDTT SSYSEAAAPE YTKRSSRYSG NAGGKDGYGS SNYRGPSNDR SAPKNIKPIS
SYAHKRSELP TRPSKSKTYN DRSRALRPTG PDRGDGFDQR DNRLREEYKK NSSQRSQLRF
PEKPFQEGKD SSKANPYQAS SYKRDSPSEN EEKPNKRFKK DETIRNKFQT QDYRNTRDSG
AAHRANENQR YNGNRKSNTQ ALPQGPKGGN YVSRYQR
