GenomeNet

Database: UniProt
Entry: Q09884
LinkDB: Q09884
Original site: Q09884 
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   13-NOV-2019, entry version 160.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
RT   fission 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.,
RA   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
RT   fission 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
RT   mitosis 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
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [11]
RP   STRUCTURE BY NMR OF 1259-1358 IN COMPLEX WITH ZINC, DOMAIN,
RP   SUBCELLULAR 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.,
RA   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
CC       nitrogen starvation. Ago1 regulation of cytokinesis and cell cycle
CC       checkpoints occurs downstream of dcr1. Required, indirectly, for
CC       regulated hyperphosphorylation of cdc2.
CC   -!- FUNCTION: Has a role in the RNA interference (RNAi) pathway which
CC       is important for heterochromatin formation, accurate chromosome
CC       segregation, centromere cohesion and telomere function during
CC       mitosis and meiosis. Digests double-stranded RNA (dsRNA) producing
CC       21 to 23 bp dsRNAs, so-called interfering RNAs (siRNA). Required
CC       for both post-transcriptional and transcriptional gene silencing.
CC       Required for silencing at the centromeres and for initiation of
CC       transcriptionally silent heterochromatin at the mating type locus.
CC       Promotes histone H3 'Lys-10' methylation necessary for centromere
CC       function. Required for recruitment of swi6 and cohesin to an
CC       ectopic dg repeat. {ECO:0000269|PubMed:12193640,
CC       ECO:0000269|PubMed:12215653, ECO:0000269|PubMed:12482946,
CC       ECO:0000269|PubMed:12509501, ECO:0000269|PubMed:12733640,
CC       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}.
CC       Nucleus {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:21847092}.
CC   -!- DOMAIN: The C-terminal dsRNA-binding fold contains a bound zinc
CC       ion and is important for normal nuclear retention and function in
CC       RNAi-dependent heterochromatin assembly. It binds double-stranded
CC       DNA and RNA (in vitro). {ECO:0000269|PubMed:21847092}.
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00657}.
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   SMR; Q09884; -.
DR   BioGrid; 275506; 199.
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   EuPathDB; FungiDB:SPCC188.13c; -.
DR   PomBase; SPCC188.13c; dcr1.
DR   InParanoid; Q09884; -.
DR   KO; K11592; -.
DR   OMA; ECSKPEN; -.
DR   PhylomeDB; Q09884; -.
DR   PRO; PR:Q09884; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:PomBase.
DR   GO; GO:0005719; C:nuclear euchromatin; IDA:PomBase.
DR   GO; GO:0031618; C:nuclear pericentric heterochromatin; IDA:PomBase.
DR   GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; 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:0004540; F:ribonuclease activity; IDA:PomBase.
DR   GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0034613; P:cellular protein localization; IMP: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:0035389; P:establishment of chromatin silencing at silent mating-type cassette; IMP:PomBase.
DR   GO; GO:0070868; P:heterochromatin organization involved in chromatin silencing; IMP:PomBase.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR   GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IMP:PomBase.
DR   GO; GO:0070919; P:production of siRNA involved in chromatin silencing by small RNA; IMP:PomBase.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; IDA:PomBase.
DR   GO; GO:0090052; P:regulation of chromatin silencing at centromere; IMP:PomBase.
DR   GO; GO:0051570; P:regulation of histone H3-K9 methylation; IMP:PomBase.
DR   GO; GO:0006396; P:RNA processing; IDA:PomBase.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 2.
DR   Gene3D; 3.30.160.380; -; 1.
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; PF03368; Dicer_dimer; 1.
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;
KW   Complete proteome; Cytoplasm; Endonuclease; Helicase; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Nuclease; Nucleotide-binding;
KW   Nucleus; Reference proteome; Repeat; RNA-mediated gene silencing;
KW   Zinc.
FT   CHAIN         1   1374       Protein Dicer.
FT                                /FTId=PRO_0000102194.
FT   DOMAIN       19    206       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      340    517       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      537    628       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      916   1038       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1083   1233       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   NP_BIND      32     39       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION     1263   1355       C-terminal dsRNA-binding fold.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MOTIF       145    148       DECH box. {ECO:0000305}.
FT   METAL      1123   1123       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1219   1219       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1222   1222       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1275   1275       Zinc. {ECO:0000244|PDB:2L6M,
FT                                ECO:0000269|PubMed:21847092}.
FT   METAL      1312   1312       Zinc; via tele nitrogen.
FT                                {ECO:0000244|PDB:2L6M,
FT                                ECO:0000269|PubMed:21847092}.
FT   METAL      1350   1350       Zinc. {ECO:0000244|PDB:2L6M,
FT                                ECO:0000269|PubMed:21847092}.
FT   METAL      1352   1352       Zinc. {ECO:0000244|PDB:2L6M,
FT                                ECO:0000269|PubMed:21847092}.
FT   SITE       1215   1215       Important for activity. {ECO:0000250}.
FT   MUTAGEN    1265   1265       K->A: Abolishes binding to dsRNA and
FT                                dsDNA. No effect on retention in the
FT                                nucleus, nor on function in RNAi-
FT                                dependent heterochromatin assembly.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1275   1275       C->S: Abolishes retention in the nucleus
FT                                and function in RNAi-dependent
FT                                heterochromatin assembly; when associated
FT                                with S-1350 and S-1352.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1287   1302       Missing: Abolishes binding to dsRNA and
FT                                dsDNA. No effect on retention in the
FT                                nucleus, nor on function in RNAi-
FT                                dependent heterochromatin assembly.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1322   1322       R->A: Abolishes binding to dsRNA and
FT                                dsDNA. No effect on retention in the
FT                                nucleus, nor on function in RNAi-
FT                                dependent heterochromatin assembly.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1334   1334       R->A: No effect on retention in the
FT                                nucleus. {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1344   1344       N->A: Decreases location in the nucleus.
FT                                Abolishes retention in the nucleus; when
FT                                associated with A-1348 and A-1349.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1348   1348       Y->A: Decreases location in the nucleus.
FT                                Abolishes retention in the nucleus; when
FT                                associated with A-1344 and A-1349.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1349   1349       S->A: Decreases location in the nucleus.
FT                                Abolishes retention in the nucleus; when
FT                                associated with A-1344 and A-1348.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1350   1350       C->S: Abolishes retention in the nucleus
FT                                and function in RNAi-dependent
FT                                heterochromatin assembly; when associated
FT                                with S-1275 and S-1352.
FT                                {ECO:0000269|PubMed:21847092}.
FT   MUTAGEN    1352   1352       C->S: Abolishes retention in the nucleus
FT                                and function in RNAi-dependent
FT                                heterochromatin assembly; when associated
FT                                with S-1275 and S-1350.
FT                                {ECO:0000269|PubMed:21847092}.
FT   HELIX      1262   1270       {ECO:0000244|PDB:2L6M}.
FT   TURN       1271   1274       {ECO:0000244|PDB:2L6M}.
FT   STRAND     1278   1286       {ECO:0000244|PDB:2L6M}.
FT   STRAND     1294   1297       {ECO:0000244|PDB:2L6M}.
FT   STRAND     1303   1311       {ECO:0000244|PDB:2L6M}.
FT   STRAND     1314   1323       {ECO:0000244|PDB:2L6M}.
FT   HELIX      1324   1341       {ECO:0000244|PDB:2L6M}.
FT   HELIX      1344   1347       {ECO:0000244|PDB:2L6M}.
FT   TURN       1351   1353       {ECO:0000244|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
//
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