RRP5_YEAST
ID RRP5_YEAST Reviewed; 1729 AA.
AC Q05022; D6W054;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=rRNA biogenesis protein RRP5;
DE AltName: Full=Ribosomal RNA-processing protein 5;
DE AltName: Full=U3 small nucleolar RNA-associated protein RRP5;
DE Short=U3 snoRNA-associated protein RRP5;
GN Name=RRP5; Synonyms=FMI1; OrderedLocusNames=YMR229C; ORFNames=YM9959.11C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8896463; DOI=10.1002/j.1460-2075.1996.tb00954.x;
RA Venema J., Tollervey D.;
RT "RRP5 is required for formation of both 18S and 5.8S rRNA in yeast.";
RL EMBO J. 15:5701-5714(1996).
RN [4]
RP INTERACTION WITH MPP10 AND SNORNA U3, AND IDENTIFICATION IN SSU PROCESSOME
RP BY MASS SPECTROMETRY.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-187 AND SER-188, 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 [8]
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-188 AND SER-1724,
RP AND 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-188 AND SER-1724,
RP 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).
CC -!- FUNCTION: Involved in the biogenesis of rRNA. Required for the
CC formation of 18S and 5.8S rRNA. {ECO:0000269|PubMed:8896463}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of
CC the ribosomal small subunit (SSU) processome composed of at least 40
CC protein subunits and snoRNA U3. {ECO:0000269|PubMed:12068309}.
CC -!- INTERACTION:
CC Q05022; Q08235: BRX1; NbExp=3; IntAct=EBI-16011, EBI-3775;
CC Q05022; P53914: KRE33; NbExp=2; IntAct=EBI-16011, EBI-28914;
CC Q05022; Q12176: MAK21; NbExp=7; IntAct=EBI-16011, EBI-10944;
CC Q05022; P39744: NOC2; NbExp=4; IntAct=EBI-16011, EBI-29259;
CC Q05022; Q12499: NOP58; NbExp=4; IntAct=EBI-16011, EBI-12126;
CC Q05022; P42945: UTP10; NbExp=4; IntAct=EBI-16011, EBI-1884;
CC Q05022; P35194: UTP20; NbExp=2; IntAct=EBI-16011, EBI-1871;
CC Q05022; Q06078: UTP21; NbExp=2; IntAct=EBI-16011, EBI-359;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:8896463}.
CC -!- MISCELLANEOUS: Present with 8860 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49939; CAA90200.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10128.1; -; Genomic_DNA.
DR PIR; S57596; S57596.
DR RefSeq; NP_013956.1; NM_001182736.1.
DR PDB; 5C9S; X-ray; 2.70 A; B=1163-1729.
DR PDB; 5NLG; X-ray; 2.35 A; A=1408-1721.
DR PDB; 5WLC; EM; 3.80 A; NJ=1-1729.
DR PDB; 5WWM; X-ray; 2.81 A; A=1399-1729.
DR PDB; 5WYJ; EM; 8.70 A; R2=1-1729.
DR PDB; 6LQQ; EM; 4.10 A; RD=1-1729.
DR PDB; 6LQR; EM; 8.60 A; RD=1-1729.
DR PDB; 6LQS; EM; 3.80 A; RD=1-1729.
DR PDB; 6LQT; EM; 4.90 A; RD=1-1729.
DR PDB; 6LQU; EM; 3.70 A; RD=1-1729.
DR PDB; 6ZQC; EM; 3.80 A; JI=1-1729.
DR PDB; 6ZQD; EM; 3.80 A; JI=1-1729.
DR PDB; 7AJT; EM; 4.60 A; JI=1-1729.
DR PDB; 7AJU; EM; 3.80 A; JI=1-1729.
DR PDB; 7D4I; EM; 4.00 A; RD=1-1729.
DR PDB; 7D5S; EM; 4.60 A; RD=1-1729.
DR PDB; 7D5T; EM; 6.00 A; RD=1-1729.
DR PDB; 7D63; EM; 12.30 A; RD=1-1729.
DR PDBsum; 5C9S; -.
DR PDBsum; 5NLG; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WWM; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q05022; -.
DR SMR; Q05022; -.
DR BioGRID; 35407; 389.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-6535N; -.
DR IntAct; Q05022; 170.
DR MINT; Q05022; -.
DR STRING; 4932.YMR229C; -.
DR iPTMnet; Q05022; -.
DR MaxQB; Q05022; -.
DR PaxDb; Q05022; -.
DR PRIDE; Q05022; -.
DR EnsemblFungi; YMR229C_mRNA; YMR229C; YMR229C.
DR GeneID; 855269; -.
DR KEGG; sce:YMR229C; -.
DR SGD; S000004842; RRP5.
DR VEuPathDB; FungiDB:YMR229C; -.
DR eggNOG; KOG1070; Eukaryota.
DR GeneTree; ENSGT00390000012228; -.
DR HOGENOM; CLU_000845_0_0_1; -.
DR InParanoid; Q05022; -.
DR OMA; GQYLRAY; -.
DR BioCyc; YEAST:G3O-32910-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q05022; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05022; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0034512; F:box C/D RNA binding; IDA:SGD.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0030515; F:snoRNA binding; IDA:SGD.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
DR GO; GO:0034463; P:90S preribosome assembly; IMP:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000464; P:endonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IDA:SGD.
DR GO; GO:0006364; P:rRNA processing; TAS:UniProtKB.
DR DisProt; DP02513; -.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.40.50.140; -; 10.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045209; Rrp5.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR23270; PTHR23270; 3.
DR Pfam; PF00575; S1; 3.
DR SMART; SM00386; HAT; 6.
DR SMART; SM00316; S1; 12.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50249; SSF50249; 10.
DR PROSITE; PS50126; S1; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..1729
FT /note="rRNA biogenesis protein RRP5"
FT /id="PRO_0000205763"
FT DOMAIN 119..200
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 338..410
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 510..580
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 607..676
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 690..769
FT /note="S1 motif 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 794..863
FT /note="S1 motif 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 895..971
FT /note="S1 motif 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1003..1083
FT /note="S1 motif 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1088..1159
FT /note="S1 motif 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1177..1245
FT /note="S1 motif 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1265..1336
FT /note="S1 motif 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REPEAT 1455..1487
FT /note="HAT 1"
FT REPEAT 1561..1594
FT /note="HAT 2"
FT REPEAT 1632..1664
FT /note="HAT 3"
FT REPEAT 1666..1701
FT /note="HAT 4"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 1409..1417
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1461..1470
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1475..1487
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1491..1504
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1510..1527
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1530..1543
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1546..1559
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1563..1577
FT /evidence="ECO:0007829|PDB:5NLG"
FT TURN 1578..1580
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1582..1594
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1598..1611
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1614..1616
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1617..1631
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1634..1647
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1652..1665
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1668..1678
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1685..1700
FT /evidence="ECO:0007829|PDB:5NLG"
FT TURN 1701..1703
FT /evidence="ECO:0007829|PDB:5NLG"
FT HELIX 1705..1720
FT /evidence="ECO:0007829|PDB:5NLG"
SQ SEQUENCE 1729 AA; 193134 MW; 39BF46E5587B3B0A CRC64;
MVASTKRKRD EDFPLSREDS TKQPSTSSLV RNTEEVSFPR GGASALTPLE LKQVANEAAS
DVLFGNESVK ASEPASRPLK KKKTTKKSTS KDSEASSANS DEARAGLIEH VNFKTLKNGS
SLLGQISAIT KQDLCITFTD GISGYVNLTH ISEEFTSILE DLDEDMDSDT DAADEKKSKV
EDAEYESSDD EDEKLDKSNE LPNLRRYFHI GQWLRCSVIK NTSLEPSTKK SKKKRIELTI
EPSSVNIYAD EDLVKSTSIQ CAVKSIEDHG ATLDVGLPGF TGFIAKKDFG NFEKLLPGAV
FLGNITKKSD RSIVVNTDFS DKKNKITQIS SIDAIIPGQI VDLLCESITK NGIAGKVFGL
VSGVVNVSHL RTFSEEDLKH KFVIGSSIRC RIIACLENKS GDKVLILSNL PHILKLEDAL
RSTEGLDAFP IGYTFESCSI KGRDSEYLYL ALDDDRLGKV HSSRVGEIEN SENLSSRVLG
YSPVDDIYQL STDPKYLKLK YLRTNDIPIG ELLPSCEITS VSSSGIELKI FNGQFKASVP
PLHISDTRLV YPERKFKIGS KVKGRVISVN SRGNVHVTLK KSLVNIEDNE LPLVSTYENA
KNIKEKNEKT LATIQVFKPN GCIISFFGGL SGFLPNSEIS EVFVKRPEEH LRLGQTVIVK
LLDVDADRRR IIATCKVSNE QAAQQKDTIE NIVPGRTIIT VHVIEKTKDS VIVEIPDVGL
RGVIYVGHLS DSRIEQNRAQ LKKLRIGTEL TGLVIDKDTR TRVFNMSLKS SLIKDAKKET
LPLTYDDVKD LNKDVPMHAY IKSISDKGLF VAFNGKFIGL VLPSYAVDSR DIDISKAFYI
NQSVTVYLLR TDDKNQKFLL SLKAPKVKEE KKKVESNIED PVDSSIKSWD DLSIGSIVKA
KIKSVKKNQL NVILAANLHG RVDIAEVFDT YEEITDKKQP LSNYKKDDVI KVKIIGNHDV
KSHKFLPITH KISKASVLEL SMKPSELKSK EVHTKSLEEI NIGQELTGFV NNSSGNHLWL
TISPVLKARI SLLDLADNDS NFSENIESVF PLGSALQVKV ASIDREHGFV NAIGKSHVDI
NMSTIKVGDE LPGRVLKIAE KYVLLDLGNK VTGISFITDA LNDFSLTLKE AFEDKINNVI
PTTVLSVDEQ NKKIELSLRP ATAKTRSIKS HEDLKQGEIV DGIVKNVNDK GIFVYLSRKV
EAFVPVSKLS DSYLKEWKKF YKPMQYVLGK VVTCDEDSRI SLTLRESEIN GDLKVLKTYS
DIKAGDVFEG TIKSVTDFGV FVKLDNTVNV TGLAHITEIA DKKPEDLSAL FGVGDRVKAI
VLKTNPEKKQ ISLSLKASHF SKEAELASTT TTTTTVDQLE KEDEDEVMAD AGFNDSDSES
DIGDQNTEVA DRKPETSSDG LSLSAGFDWT ASILDQAQEE EESDQDQEDF TENKKHKHKR
RKENVVQDKT IDINTRAPES VADFERLLIG NPNSSVVWMN YMAFQLQLSE IEKARELAER
ALKTINFREE AEKLNIWIAM LNLENTFGTE ETLEEVFSRA CQYMDSYTIH TKLLGIYEIS
EKFDKAAELF KATAKKFGGE KVSIWVSWGD FLISHNEEQE ARTILGNALK ALPKRNHIEV
VRKFAQLEFA KGDPERGRSL FEGLVADAPK RIDLWNVYVD QEVKAKDKKK VEDLFERIIT
KKITRKQAKF FFNKWLQFEE SEGDEKTIEY VKAKATEYVA SHESQKADE
