DCR1_SCHPO
ID DCR1_SCHPO Reviewed; 1374 AA.
AC Q09884; Q9UUN1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein Dicer;
DE AltName: Full=Cell cycle control protein dcr1;
DE AltName: Full=RNA interference pathway protein dcr1;
DE Includes:
DE RecName: Full=Endoribonuclease dcr1;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase dcr1;
DE EC=3.6.4.-;
GN Name=dcr1; ORFNames=SPCC188.13c, SPCC584.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND RNA CLEAVAGE.
RX PubMed=12482946; DOI=10.1073/pnas.212633199;
RA Provost P., Silverstein R.A., Dishart D., Walfridsson J., Djupedal I.,
RA Kniola B., Wright A., Samuelsson B., Raadmark O., Ekwall K.;
RT "Dicer is required for chromosome segregation and gene silencing in fission
RT yeast cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16648-16653(2002).
RN [3]
RP FUNCTION.
RX PubMed=12193640; DOI=10.1126/science.1074973;
RA Volpe T.A., Kidner C., Hall I.M., Teng G., Grewal S.I.S., Martienssen R.A.;
RT "Regulation of heterochromatic silencing and histone H3 lysine-9
RT methylation by RNAi.";
RL Science 297:1833-1837(2002).
RN [4]
RP FUNCTION.
RX PubMed=12215653; DOI=10.1126/science.1076466;
RA Hall I.M., Shankaranarayana G.D., Noma K., Ayoub N., Cohen A.,
RA Grewal S.I.S.;
RT "Establishment and maintenance of a heterochromatin domain.";
RL Science 297:2232-2237(2002).
RN [5]
RP FUNCTION.
RX PubMed=12733640; DOI=10.1023/a:1022815931524;
RA Volpe T., Schramke V., Hamilton G.L., White S.A., Teng G.,
RA Martienssen R.A., Allshire R.C.;
RT "RNA interference is required for normal centromere function in fission
RT yeast.";
RL Chromosome Res. 11:137-146(2003).
RN [6]
RP FUNCTION.
RX PubMed=12509501; DOI=10.1073/pnas.232688099;
RA Hall I.M., Noma K., Grewal S.I.S.;
RT "RNA interference machinery regulates chromosome dynamics during mitosis
RT and meiosis in fission yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:193-198(2003).
RN [7]
RP FUNCTION.
RX PubMed=15371329; DOI=10.1101/gad.1218004;
RA Sigova A., Rhind N., Zamore P.D.;
RT "A single Argonaute protein mediates both transcriptional and
RT posttranscriptional silencing in Schizosaccharomyces pombe.";
RL Genes Dev. 18:2359-2367(2004).
RN [8]
RP FUNCTION.
RX PubMed=14699070; DOI=10.1091/mbc.e03-06-0433;
RA Carmichael J.B., Provost P., Ekwall K., Hobman T.C.;
RT "ago1 and dcr1, two core components of the RNA interference pathway,
RT functionally diverge from rdp1 in regulating cell cycle events in
RT Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 15:1425-1435(2004).
RN [9]
RP FUNCTION, AND RNA CLEAVAGE.
RX PubMed=15907173; DOI=10.2174/0929866053765590;
RA Qian Z., Xuan B., Hong J., Hao Z., Wang L., Huang W.;
RT "Expression and purification of the carboxyl terminus domain of
RT Schizosaccharomyces pombe dicer in Escherichia coli.";
RL Protein Pept. Lett. 12:311-314(2005).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [11]
RP STRUCTURE BY NMR OF 1259-1358 IN COMPLEX WITH ZINC, DOMAIN, SUBCELLULAR
RP LOCATION, FUNCTION, AND MUTAGENESIS OF LYS-1265; CYS-1275;
RP 1287-VAL--THR-1302; ARG-1322; ARG-1334; ASN-1344; TYR-1348; SER-1349;
RP CYS-1350 AND CYS-1352.
RX PubMed=21847092; DOI=10.1038/emboj.2011.300;
RA Barraud P., Emmerth S., Shimada Y., Hotz H.R., Allain F.H., Buehler M.;
RT "An extended dsRBD with a novel zinc-binding motif mediates nuclear
RT retention of fission yeast Dicer.";
RL EMBO J. 30:4223-4235(2011).
CC -!- FUNCTION: Required for G1 arrest and mating in response to nitrogen
CC starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints
CC occurs downstream of dcr1. Required, indirectly, for regulated
CC hyperphosphorylation of cdc2.
CC -!- FUNCTION: Has a role in the RNA interference (RNAi) pathway which is
CC important for heterochromatin formation, accurate chromosome
CC segregation, centromere cohesion and telomere function during mitosis
CC and meiosis. Digests double-stranded RNA (dsRNA) producing 21 to 23 bp
CC dsRNAs, so-called interfering RNAs (siRNA). Required for both post-
CC transcriptional and transcriptional gene silencing. Required for
CC silencing at the centromeres and for initiation of transcriptionally
CC silent heterochromatin at the mating type locus. Promotes histone H3
CC 'Lys-10' methylation necessary for centromere function. Required for
CC recruitment of swi6 and cohesin to an ectopic dg repeat.
CC {ECO:0000269|PubMed:12193640, ECO:0000269|PubMed:12215653,
CC ECO:0000269|PubMed:12482946, ECO:0000269|PubMed:12509501,
CC ECO:0000269|PubMed:12733640, ECO:0000269|PubMed:21847092}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21847092}.
CC -!- DOMAIN: The C-terminal dsRNA-binding fold contains a bound zinc ion and
CC is important for normal nuclear retention and function in RNAi-
CC dependent heterochromatin assembly. It binds double-stranded DNA and
CC RNA (in vitro). {ECO:0000269|PubMed:21847092}.
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00657}.
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DR EMBL; CU329672; CAB41233.1; -; Genomic_DNA.
DR PIR; T39130; S62524.
DR RefSeq; NP_588215.2; NM_001023205.2.
DR PDB; 2L6M; NMR; -; A=1259-1358.
DR PDBsum; 2L6M; -.
DR AlphaFoldDB; Q09884; -.
DR SMR; Q09884; -.
DR BioGRID; 275506; 210.
DR STRING; 4896.SPCC188.13c.1; -.
DR SwissPalm; Q09884; -.
DR PaxDb; Q09884; -.
DR PRIDE; Q09884; -.
DR EnsemblFungi; SPCC188.13c.1; SPCC188.13c.1:pep; SPCC188.13c.
DR GeneID; 2538930; -.
DR KEGG; spo:SPCC188.13c; -.
DR PomBase; SPCC188.13c; dcr1.
DR VEuPathDB; FungiDB:SPCC188.13c; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_3_1; -.
DR InParanoid; Q09884; -.
DR OMA; ATICDET; -.
DR PhylomeDB; Q09884; -.
DR PRO; PR:Q09884; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0000791; C:euchromatin; IDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0016442; C:RISC complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:PomBase.
DR GO; GO:1990188; F:euchromatin binding; IDA:PomBase.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0033562; P:co-transcriptional gene silencing by RNA interference machinery; IMP:PomBase.
DR GO; GO:0070314; P:G1 to G0 transition; IMP:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0070317; P:negative regulation of G0 to G1 transition; IMP:PomBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0061188; P:negative regulation of ribosomal DNA heterochromatin assembly; IMP:PomBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IMP:PomBase.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 1.10.1520.10; -; 2.
DR Gene3D; 3.30.160.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF69065; SSF69065; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Chromosome partition; Cytoplasm;
KW Endonuclease; Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nuclease; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW RNA-mediated gene silencing; Zinc.
FT CHAIN 1..1374
FT /note="Protein Dicer"
FT /id="PRO_0000102194"
FT DOMAIN 19..206
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 340..517
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 537..628
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 916..1038
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1083..1233
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT REGION 1263..1355
FT /note="C-terminal dsRNA-binding fold"
FT /evidence="ECO:0000269|PubMed:21847092"
FT MOTIF 145..148
FT /note="DECH box"
FT /evidence="ECO:0000305"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21847092,
FT ECO:0007744|PDB:2L6M"
FT BINDING 1312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21847092,
FT ECO:0007744|PDB:2L6M"
FT BINDING 1350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21847092,
FT ECO:0007744|PDB:2L6M"
FT BINDING 1352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:21847092,
FT ECO:0007744|PDB:2L6M"
FT SITE 1215
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MUTAGEN 1265
FT /note="K->A: Abolishes binding to dsRNA and dsDNA. No
FT effect on retention in the nucleus, nor on function in
FT RNAi-dependent heterochromatin assembly."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1275
FT /note="C->S: Abolishes retention in the nucleus and
FT function in RNAi-dependent heterochromatin assembly; when
FT associated with S-1350 and S-1352."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1287..1302
FT /note="Missing: Abolishes binding to dsRNA and dsDNA. No
FT effect on retention in the nucleus, nor on function in
FT RNAi-dependent heterochromatin assembly."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1322
FT /note="R->A: Abolishes binding to dsRNA and dsDNA. No
FT effect on retention in the nucleus, nor on function in
FT RNAi-dependent heterochromatin assembly."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1334
FT /note="R->A: No effect on retention in the nucleus."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1344
FT /note="N->A: Decreases location in the nucleus. Abolishes
FT retention in the nucleus; when associated with A-1348 and
FT A-1349."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1348
FT /note="Y->A: Decreases location in the nucleus. Abolishes
FT retention in the nucleus; when associated with A-1344 and
FT A-1349."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1349
FT /note="S->A: Decreases location in the nucleus. Abolishes
FT retention in the nucleus; when associated with A-1344 and
FT A-1348."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1350
FT /note="C->S: Abolishes retention in the nucleus and
FT function in RNAi-dependent heterochromatin assembly; when
FT associated with S-1275 and S-1352."
FT /evidence="ECO:0000269|PubMed:21847092"
FT MUTAGEN 1352
FT /note="C->S: Abolishes retention in the nucleus and
FT function in RNAi-dependent heterochromatin assembly; when
FT associated with S-1275 and S-1350."
FT /evidence="ECO:0000269|PubMed:21847092"
FT HELIX 1262..1270
FT /evidence="ECO:0007829|PDB:2L6M"
FT TURN 1271..1274
FT /evidence="ECO:0007829|PDB:2L6M"
FT STRAND 1278..1286
FT /evidence="ECO:0007829|PDB:2L6M"
FT STRAND 1294..1297
FT /evidence="ECO:0007829|PDB:2L6M"
FT STRAND 1303..1311
FT /evidence="ECO:0007829|PDB:2L6M"
FT STRAND 1314..1323
FT /evidence="ECO:0007829|PDB:2L6M"
FT HELIX 1324..1341
FT /evidence="ECO:0007829|PDB:2L6M"
FT HELIX 1344..1347
FT /evidence="ECO:0007829|PDB:2L6M"
FT TURN 1351..1353
FT /evidence="ECO:0007829|PDB:2L6M"
SQ SEQUENCE 1374 AA; 158040 MW; 89AE9EF8DE7966C6 CRC64;
MDISSFLLPQ LLRKYQQDVY NIASKQNTLL VMRTGAGKTL LAVKLIKQKL EEQILIQESN
LEHKKISVFL VNKVPLVFQQ AEYIRSQLPA KVGMFYGELS IEMSEQLLTN IILKYNVIVI
TADLFYLFLA RGFLSINDLN LIIFDECHHA IGNDAYARIM NDFYHRAKAV LSKKHFTLPR
IFGMTASPFT GKKGNLYHRL YQWEQLFDSK AHVVSENELA DYFCLPEESY VMYSNKLVVP
PSDSIIKKCE ETLQGCKLIS RAVKTALAET IDMGLWFGEQ VWLYLVDFVE TKRLKKKALG
KQLSDDEELA IDRLKIFVED WKNNKYSDNG PRIPVFDSTD VTDKVFKLLE LLKATYRKSD
SVRTVIFVER KATAFTLSLF MKTLNLPNIR AHSFIGHGPS DQGEFSMTFR RQKDTLHKFK
TGKYNVLIAT AVAEEGIDVP SCNLVIRFNI CRTVTQYVQS RGRARAMASK FLIFLNTEEL
LIHERILHEE KNLKFALSEL SNSNIFDSLV CEERERVTDD IVYEVGETGA LLTGLYAVSL
LYNFCNTLSR DVYTRYYPTF TAQPCLSGWY CFEVELPKAC KVPAAQGSPA KSIRKAKQNA
AFIMCLDLIR MGLIDKHLKP LDFRRKIADL ETLEEDELKD EGYIETYERY VPKSWMKVPE
DITRCFVSLL YTDANEGDNH IFHPLVFVQA HSFPKIDSFI LNSTVGPRVK IVLETIEDSF
KIDSHLLELL KKSTRYLLQF GLSTSLEQQI PTPYWLAPLN LSCTDYRFLE NLIDVDTIQN
FFKLPEPVQN VTDLQSDTVL LVNPQSIYEQ YAFEGFVNSE FMIPAKKKDK APSALCKKLP
LRLNYSLWGN RAKSIPKSQQ VRSFYINDLY ILPVSRHLKN SALLIPSILY HIENLLVASS
FIEHFRLDCK IDTACQALTS AESQLNFDYD RLEFYGDCFL KLGASITVFL KFPDTQEYQL
HFNRKKIISN CNLYKVAIDC ELPKYALSTP LEIRHWCPYG FQKSTSDKCR YAVLQKLSVK
RIADMVEASI GACLLDSGLD SALKICKSLS VGLLDISNWD EWNNYFDLNT YADSLRNVQF
PYSSYIEETI GYSFKNKKLL HLAFIHPSMM SQQGIYENYQ QLEFLGDAVL DYIIVQYLYK
KYPNATSGEL TDYKSFYVCN KSLSYIGFVL NLHKYIQHES AAMCDAIFEY QELIEAFRET
ASENPWFWFE IDSPKFISDT LEAMICAIFL DSGFSLQSLQ FVLPLFLNSL GDATHTKAKG
DIEHKVYQLL KDQGCEDFGT KCVIEEVKSS HKTLLNTELH LTKYYGFSFF RHGNIVAYGK
SRKVANAKYI MKQRLLKLLE DKSNLLLYSC NCKFSKKKPS DEQIKGDGKV KSLT
