ID   BCK1_YEAST              Reviewed;        1478 AA.
AC   Q01389; D6VW89; P32894;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 213.
DE   RecName: Full=Serine/threonine-protein kinase BCK1/SLK1/SSP31;
DE            EC=2.7.11.1;
GN   Name=BCK1; Synonyms=LAS3, SLK1, SSP31; OrderedLocusNames=YJL095W;
GN   ORFNames=J0906;
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].
RX   PubMed=1545797; DOI=10.1128/mcb.12.3.1162-1178.1992;
RA   Costigan C., Gehrung S., Snyder M.;
RT   "A synthetic lethal screen identifies SLK1, a novel protein kinase homolog
RT   implicated in yeast cell morphogenesis and cell growth.";
RL   Mol. Cell. Biol. 12:1162-1178(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1840547; DOI=10.1016/0378-1119(91)90499-2;
RA   Irie K., Araki H., Oshima Y.;
RT   "A new protein kinase, SSP31, modulating the SMP3 gene-product involved in
RT   plasmid maintenance in Saccharomyces cerevisiae.";
RL   Gene 108:139-144(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-1119; ILE-1120;
RP   GLY-1146 AND ALA-1174.
RC   STRAIN=ATCC 204278 / EG123 / SM1058;
RX   PubMed=1729597; DOI=10.1128/mcb.12.1.172-182.1992;
RA   Lee K.S., Levin D.E.;
RT   "Dominant mutations in a gene encoding a putative protein kinase (BCK1)
RT   bypass the requirement for a Saccharomyces cerevisiae protein kinase C
RT   homolog.";
RL   Mol. Cell. Biol. 12:172-182(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7871887; DOI=10.1002/yea.320101112;
RA   Miosga T., Boles E., Schaaff-Gerstenschlaeger I., Schmitt S.,
RA   Zimmermann F.K.;
RT   "Sequence and function analysis of a 9.74 kb fragment of Saccharomyces
RT   cerevisiae chromosome X including the BCK1 gene.";
RL   Yeast 10:1481-1488(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 459-1173.
RA   Cusick M.E.;
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747 AND SER-1058, 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407; SER-411; SER-491;
RP   SER-816; SER-1058 AND SER-1061, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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: Serine/threonine protein kinase involved in a signal
CC       transduction pathway that plays a role in yeast cell morphogenesis and
CC       cell growth. This pathway seems to start by SMP3; then involve the
CC       kinase PKC1 that may act on this kinase. BCK1 probably phosphorylates
CC       MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- INTERACTION:
CC       Q01389; Q00684: CDC14; NbExp=4; IntAct=EBI-3470, EBI-4192;
CC       Q01389; P36006: MYO3; NbExp=6; IntAct=EBI-3470, EBI-11670;
CC       Q01389; Q04439: MYO5; NbExp=6; IntAct=EBI-3470, EBI-11687;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 112 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA21179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAA21179.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M84389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; D10389; BAA01226.1; -; Genomic_DNA.
DR   EMBL; X60227; CAA42788.1; -; Genomic_DNA.
DR   EMBL; X77923; CAA54896.1; -; Genomic_DNA.
DR   EMBL; Z49370; CAA89389.1; -; Genomic_DNA.
DR   EMBL; Z49369; CAA89388.1; -; Genomic_DNA.
DR   EMBL; M88604; AAA21179.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006943; DAA08705.1; -; Genomic_DNA.
DR   PIR; S20117; S20117.
DR   RefSeq; NP_012440.1; NM_001181528.1.
DR   AlphaFoldDB; Q01389; -.
DR   SMR; Q01389; -.
DR   BioGRID; 33662; 836.
DR   DIP; DIP-2223N; -.
DR   IntAct; Q01389; 56.
DR   MINT; Q01389; -.
DR   STRING; 4932.YJL095W; -.
DR   CarbonylDB; Q01389; -.
DR   GlyGen; Q01389; 8 sites, 1 O-linked glycan (8 sites).
DR   iPTMnet; Q01389; -.
DR   MaxQB; Q01389; -.
DR   PaxDb; 4932-YJL095W; -.
DR   PeptideAtlas; Q01389; -.
DR   EnsemblFungi; YJL095W_mRNA; YJL095W; YJL095W.
DR   GeneID; 853350; -.
DR   KEGG; sce:YJL095W; -.
DR   AGR; SGD:S000003631; -.
DR   SGD; S000003631; BCK1.
DR   VEuPathDB; FungiDB:YJL095W; -.
DR   eggNOG; KOG0198; Eukaryota.
DR   GeneTree; ENSGT00980000202011; -.
DR   HOGENOM; CLU_002516_0_0_1; -.
DR   InParanoid; Q01389; -.
DR   OMA; PWSNFEV; -.
DR   OrthoDB; 55507at2759; -.
DR   BioCyc; YEAST:G3O-31550-MONOMER; -.
DR   Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-SCE-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-SCE-5676590; NIK-->noncanonical NF-kB signaling.
DR   BioGRID-ORCS; 853350; 2 hits in 13 CRISPR screens.
DR   PRO; PR:Q01389; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; Q01389; Protein.
DR   GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IMP:SGD.
DR   GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000196; P:cell wall integrity MAPK cascade; IGI:SGD.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR   GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IMP:SGD.
DR   GO; GO:0000425; P:pexophagy; IMP:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR   GO; GO:0010447; P:response to acidic pH; IMP:SGD.
DR   CDD; cd06629; STKc_Bck1_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR   PANTHER; PTHR48016:SF48; SERINE_THREONINE-PROTEIN KINASE BCK1_SLK1_SSP31; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..1478
FT                   /note="Serine/threonine-protein kinase BCK1/SLK1/SSP31"
FT                   /id="PRO_0000085662"
FT   DOMAIN          1175..1440
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..806
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..877
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1082
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1303
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         1181..1189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         407
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         491
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         747
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         816
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1058
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1061
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1134
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         1119
FT                   /note="T->P: In BCK1-19; Dominant active."
FT                   /evidence="ECO:0000269|PubMed:1729597"
FT   MUTAGEN         1120
FT                   /note="I->K: In BCK1-11; Dominant active."
FT                   /evidence="ECO:0000269|PubMed:1729597"
FT   MUTAGEN         1120
FT                   /note="I->T: In BCK1-16; Dominant active."
FT                   /evidence="ECO:0000269|PubMed:1729597"
FT   MUTAGEN         1146
FT                   /note="G->V: In BCK1-10; Dominant active."
FT                   /evidence="ECO:0000269|PubMed:1729597"
FT   MUTAGEN         1174
FT                   /note="A->P: In BCK1-20; Dominant active."
FT                   /evidence="ECO:0000269|PubMed:1729597"
FT   CONFLICT        59
FT                   /note="F -> I (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="E -> V (in Ref. 2; BAA01226)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="A -> P (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279
FT                   /note="N -> I (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        703..714
FT                   /note="RYPQTPSYYYDR -> STPKPRVITMTE (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        795
FT                   /note="S -> A (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        802
FT                   /note="L -> V (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        808
FT                   /note="A -> S (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        903
FT                   /note="T -> N (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        919
FT                   /note="T -> N (in Ref. 3; CAA42788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        960
FT                   /note="A -> R (in Ref. 7; AAA21179)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        962
FT                   /note="A -> R (in Ref. 7; AAA21179)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1478 AA;  164195 MW;  D586C3A497A5BB33 CRC64;
     MPFLRKIAGT AHTHSRSDSN SSVKFGHQPT SSVASTKSSS KSPRATSRKS IYDDIRSQFP
     NLTPNSTSSQ FYESTPVIEQ SFNWTTDDHI SAGTLENPTS FTNSSYKNDN GPSSLSDSRK
     SSGGNSVNSL SFDKLILSWD PTDPDEWTMH RVTSWFKFHD FPESWILFFK KHQLFGHRFI
     KLLAYDNFAV YEKYLPQTKT ASYTRFQQLL KKTMTKNVTN SHIRQKSASK LKSSRSSSES
     IKSKLKNSKS QEDISNSRST SESALSPTKS GPSKTDEKNF LHSTSTHQKT KSASSLYRRS
     FISLRGSSSS NASSAKSPSN IKLSIPARPH SIIESNSTLT KSASPPASPS YPSIFRRHHK
     SSSSESSLLN SLFGSGIGEE APTKPNPQGH SLSSENLAKG KSKHYETNVS SPLKQSSLPT
     SDDKGNLWNK FKRKSQIGVP SPNTVAYVTS QETPSLKSNS STATLTVQTA DVNIPSPSSS
     PPPIPKTANR SLEVISTEDT PKISSTTASF KETYPDCINP DKTVPVPVNN QKYSVKNFLL
     DQKFYPLKKT GLNDSENKYI LVTKDNVSFV PLNLKSVAKL SSFKESALTK LGINHKNVTF
     HMTDFDCDIG AAIPDDTLEF LKKSLFLNTS GKIYIKDQMK LQQKPKPAPL TSENNVPLKS
     VKSKSSMRSG TSSLIASTDD VSIVTSSSDI TSFDEHASGS GRRYPQTPSY YYDRVSNTNP
     TEELNYWNIK EVLSHEENAP KMVFKTSPKL ELNLPDKGSK LNIPTPITEN ESKSSFQVLR
     KDEGTEIDFN HRRESPYTKP ELAPKREAPK PPANTSPQRT LSTSKQNKPI RLVRASTKIS
     RSKRSKPLPP QLLSSPIEAS SSSPDSLTSS YTPASTHVLI PQPYKGANDV MRRLKTDQDS
     TSTSPSLKMK QKVNRSNSTV STSNSIFYSP SPLLKRGNSK RVVSSTSAAD IFEENDITFA
     DAPPMFDSDD SDDDSSSSDD IIWSKKKTAP ETNNENKKDE KSDNSSTHSD EIFYDSQTQD
     KMERKMTFRP SPEVVYQNLE KFFPRANLDK PITEGIASPT SPKSLDSLLS PKNVASSRTE
     PSTPSRPVPP DSSYEFIQDG LNGKNKPLNQ AKTPKRTKTI RTIAHEASLA RKNSVKLKRQ
     NTKMWGTRMV EVTENHMVSI NKAKNSKGEY KEFAWMKGEM IGKGSFGAVY LCLNVTTGEM
     MAVKQVEVPK YSSQNEAILS TVEALRSEVS TLKDLDHLNI VQYLGFENKN NIYSLFLEYV
     AGGSVGSLIR MYGRFDEPLI KHLTTQVLKG LAYLHSKGIL HRDMKADNLL LDQDGICKIS
     DFGISRKSKD IYSNSDMTMR GTVFWMAPEM VDTKQGYSAK VDIWSLGCIV LEMFAGKRPW
     SNLEVVAAMF KIGKSKSAPP IPEDTLPLIS QIGRNFLDAC FEINPEKRPT ANELLSHPFS
     EVNETFNFKS TRLAKFIKSN DKLNSSKLRI TSQENKTE
//