GenomeNet

Database: UniProt
Entry: Q9VCU9
LinkDB: Q9VCU9
Original site: Q9VCU9 
ID   DCR1_DROME              Reviewed;        2249 AA.
AC   Q9VCU9; Q961S7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-OCT-2019, entry version 153.
DE   RecName: Full=Endoribonuclease Dcr-1;
DE            Short=Protein dicer-1;
DE            EC=3.1.26.-;
GN   Name=Dcr-1 {ECO:0000312|EMBL:AAF56056.1}; ORFNames=CG4792;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000312|EMBL:AAF56056.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAF56056.1}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAK84929.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1338-2249.
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=11201747; DOI=10.1038/35053110;
RA   Bernstein E., Caudy A.A., Hammond S.M., Hannon G.J.;
RT   "Role for a bidentate ribonuclease in the initiation step of RNA
RT   interference.";
RL   Nature 409:363-366(2001).
RN   [5] {ECO:0000305}
RP   FUNCTION, AND INTERACTION WITH AGO2.
RX   PubMed=11498593; DOI=10.1126/science.1064023;
RA   Hammond S.M., Boettcher S., Caudy A.A., Kobayashi R., Hannon G.J.;
RT   "Argonaute2, a link between genetic and biochemical analyses of
RT   RNAi.";
RL   Science 293:1146-1150(2001).
RN   [6] {ECO:0000305}
RP   INTERACTION WITH FMR1.
RX   PubMed=12368261; DOI=10.1101/gad.1022002;
RA   Ishizuka A., Siomi M.C., Siomi H.;
RT   "A Drosophila fragile X protein interacts with components of RNAi and
RT   ribosomal proteins.";
RL   Genes Dev. 16:2497-2508(2002).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH PIWI AND VAS.
RX   PubMed=16949822; DOI=10.1016/j.cub.2006.08.051;
RA   Megosh H.B., Cox D.N., Campbell C., Lin H.;
RT   "The role of PIWI and the miRNA machinery in Drosophila germline
RT   determination.";
RL   Curr. Biol. 16:1884-1894(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1423; SER-1877 AND
RP   SER-1880, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Essential for RNA interference (RNAi); double-stranded
CC       RNA (dsRNA) induces potent and specific gene silencing. RNAi is
CC       mediated by the RNA-induced silencing complex (RISC), a sequence-
CC       specific, multicomponent nuclease that destroys or silences
CC       messenger RNAs homologous to the silencing trigger. May carry out
CC       the initiation step of RNAi by cleaving dsRNA to produce 22 bp
CC       dsRNAs (siRNAs) which target the selective destruction of
CC       homologous RNAs. During embryogenesis, involved in germline fate
CC       determination. {ECO:0000269|PubMed:11201747,
CC       ECO:0000269|PubMed:11498593, ECO:0000269|PubMed:16949822}.
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   -!- SUBUNIT: Interacts with AGO2 and Fmr1 to form the RNA-induced
CC       silencing complex (RISC), a ribonucleoprotein (RNP) complex
CC       involved in translation regulation; other components of the
CC       complex are RpL5, RpL11, AGO2 and Rm62 (PubMed:11498593,
CC       PubMed:12368261). Interacts with piwi and vas; these interactions
CC       occur in the polar granules (PubMed:16949822).
CC       {ECO:0000269|PubMed:11498593, ECO:0000269|PubMed:12368261,
CC       ECO:0000269|PubMed:16949822}.
CC   -!- INTERACTION:
CC       Q8IP72:loqs; NbExp=4; IntAct=EBI-112170, EBI-162836;
CC       Q9VJY9:loqs; NbExp=12; IntAct=EBI-112170, EBI-638074;
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00657}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK84929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE014297; AAF56056.1; -; Genomic_DNA.
DR   EMBL; AY050230; AAK84929.1; ALT_INIT; mRNA.
DR   RefSeq; NP_524453.1; NM_079729.3.
DR   SMR; Q9VCU9; -.
DR   BioGrid; 67642; 23.
DR   DIP; DIP-23028N; -.
DR   IntAct; Q9VCU9; 11.
DR   STRING; 7227.FBpp0083717; -.
DR   iPTMnet; Q9VCU9; -.
DR   PaxDb; Q9VCU9; -.
DR   PRIDE; Q9VCU9; -.
DR   EnsemblMetazoa; FBtr0084324; FBpp0083717; FBgn0039016.
DR   GeneID; 42693; -.
DR   KEGG; dme:Dmel_CG4792; -.
DR   UCSC; CG4792-RA; d. melanogaster.
DR   CTD; 42693; -.
DR   FlyBase; FBgn0039016; Dcr-1.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   GeneTree; ENSGT00940000156287; -.
DR   InParanoid; Q9VCU9; -.
DR   KO; K11592; -.
DR   OMA; YLMLFDP; -.
DR   OrthoDB; 1337630at2759; -.
DR   PhylomeDB; Q9VCU9; -.
DR   Reactome; R-DME-203927; MicroRNA (miRNA) biogenesis.
DR   Reactome; R-DME-426486; Small interfering RNA (siRNA) biogenesis.
DR   GenomeRNAi; 42693; -.
DR   PRO; PR:Q9VCU9; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0039016; Expressed in 26 organ(s), highest expression level in embryo.
DR   Genevisible; Q9VCU9; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016442; C:RISC complex; IDA:FlyBase.
DR   GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016443; F:bidentate ribonuclease III activity; IDA:FlyBase.
DR   GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:FlyBase.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070883; F:pre-miRNA binding; IDA:FlyBase.
DR   GO; GO:0004525; F:ribonuclease III activity; IDA:MGI.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:FlyBase.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
DR   GO; GO:0042078; P:germ-line stem cell division; IMP:FlyBase.
DR   GO; GO:0030727; P:germarium-derived female germ-line cyst formation; IMP:FlyBase.
DR   GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR   GO; GO:0045448; P:mitotic cell cycle, embryonic; IMP:FlyBase.
DR   GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR   GO; GO:0031054; P:pre-miRNA processing; IDA:FlyBase.
DR   GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:FlyBase.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; IDA:UniProtKB.
DR   GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR   GO; GO:0016246; P:RNA interference; IDA:FlyBase.
DR   GO; GO:0007367; P:segment polarity determination; IGI:FlyBase.
DR   GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; IMP:FlyBase.
DR   CDD; cd00048; DSRM; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   Gene3D; 3.30.160.380; -; 1.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003100; PAZ_dom.
DR   InterPro; IPR036085; PAZ_dom_sf.
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; PF02170; PAZ; 1.
DR   Pfam; PF00636; Ribonuclease_3; 2.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00949; PAZ; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF101690; SSF101690; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF69065; SSF69065; 2.
DR   PROSITE; PS51327; DICER_DSRBF; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50821; PAZ; 1.
DR   PROSITE; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Endonuclease; Helicase; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Nuclease; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW   RNA-mediated gene silencing.
FT   CHAIN         1   2249       Endoribonuclease Dcr-1.
FT                                /FTId=PRO_0000180474.
FT   DOMAIN      485    648       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      825    920       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1099   1246       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN     1698   1919       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1993   2150       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     2175   2241       DRBM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00266}.
FT   NP_BIND      37     44       ATP. {ECO:0000255}.
FT   METAL      2032   2032       Magnesium or manganese. {ECO:0000250}.
FT   METAL      2136   2136       Magnesium or manganese. {ECO:0000250}.
FT   METAL      2139   2139       Magnesium or manganese. {ECO:0000250}.
FT   SITE       2132   2132       Important for activity. {ECO:0000250}.
FT   MOD_RES    1423   1423       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1877   1877       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1880   1880       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   CONFLICT   1338   1339       PT -> AI (in Ref. 3). {ECO:0000305}.
FT   CONFLICT   1345   1345       L -> I (in Ref. 3). {ECO:0000305}.
SQ   SEQUENCE   2249 AA;  255330 MW;  D693F0432AC8033D CRC64;
     MAFHWCDNNL HTTVFTPRDF QVELLATAYE RNTIICLGHR SSKEFIALKL LQELSRRARR
     HGRVSVYLSC EVGTSTEPCS IYTMLTHLTD LRVWQEQPDM QIPFDHCWTD YHVSILRPEG
     FLYLLETREL LLSSVELIVL EDCHDSAVYQ RIRPLFENHI MPAPPADRPR ILGLAGPLHS
     AGCELQQLSA MLATLEQSVL CQIETASDIV TVLRYCSRPH EYIVQCAPFE MDELSLVLAD
     VLNTHKSFLL DHRYDPYEIY GTDQFMDELK DIPDPKVDPL NVINSLLVVL HEMGPWCTQR
     AAHHFYQCNE KLKVKTPHER HYLLYCLVST ALIQLYSLCE HAFHRHLGSG SDSRQTIERY
     SSPKVRRLLQ TLRCFKPEEV HTQADGLRRM RHQVDQADFN RLSHTLESKC RMVDQMDQPP
     TETRALVATL EQILHTTEDR QTNRSAARVT PTPTPAHAKP KPSSGANTAQ PRTRRRVYTR
     RHHRDHNDGS DTLCALIYCN QNHTARVLFE LLAEISRRDP DLKFLRCQYT TDRVADPTTE
     PKEAELEHRR QEEVLKRFRM HDCNVLIGTS VLEEGIDVPK CNLVVRWDPP TTYRSYVQCK
     GRARAAPAYH VILVAPSYKS PTVGSVQLTD RSHRYICATG DTTEADSDSD DSAMPNSSGS
     DPYTFGTARG TVKILNPEVF SKQPPTACDI KLQEIQDELP AAAQLDTSNS SDEAVSMSNT
     SPSESSTEQK SRRFQCELSS LTEPEDTSDT TAEIDTAHSL ASTTKDLVHQ MAQYREIEQM
     LLSKCANTEP PEQEQSEAER FSACLAAYRP KPHLLTGASV DLGSAIALVN KYCARLPSDT
     FTKLTALWRC TRNERAGVTL FQYTLRLPIN SPLKHDIVGL PMPTQTLARR LAALQACVEL
     HRIGELDDQL QPIGKEGFRA LEPDWECFEL EPEDEQIVQL SDEPRPGTTK RRQYYYKRIA
     SEFCDCRPVA GAPCYLYFIQ LTLQCPIPEE QNTRGRKIYP PEDAQQGFGI LTTKRIPKLS
     AFSIFTRSGE VKVSLELAKE RVILTSEQIV CINGFLNYTF TNVLRLQKFL MLFDPDSTEN
     CVFIVPTVKA PAGGKHIDWQ FLELIQANGN TMPRAVPDEE RQAQPFDPQR FQDAVVMPWY
     RNQDQPQYFY VAEICPHLSP LSCFPGDNYR TFKHYYLVKY GLTIQNTSQP LLDVDHTSAR
     LNFLTPRYVN RKGVALPTSS EETKRAKREN LEQKQILVPE LCTVHPFPAS LWRTAVCLPC
     ILYRINGLLL ADDIRKQVSA DLGLGRQQIE DEDFEWPMLD FGWSLSEVLK KSRESKQKES
     LKDDTINGKD LADVEKKPTS EETQLDKDSK DDKVEKSAIE LIIEGEEKLQ EADDFIEIGT
     WSNDMADDIA SFNQEDDDED DAFHLPVLPA NVKFCDQQTR YGSPTFWDVS NGESGFKGPK
     SSQNKQGGKG KAKGPAKPTF NYYDSDNSLG SSYDDDDNAG PLNYMHHNYS SDDDDVADDI
     DAGRIAFTSK NEAETIETAQ EVEKRQKQLS IIQATNANER QYQQTKNLLI GFNFKHEDQK
     EPATIRYEES IAKLKTEIES GGMLVPHDQQ LVLKRSDAAE AQVAKVSMME LLKQLLPYVN
     EDVLAKKLGD RRELLLSDLV ELNADWVARH EQETYNVMGC GDSFDNYNDH HRLNLDEKQL
     KLQYERIEIE PPTSTKAITS AILPAGFSFD RQPDLVGHPG PSPSIILQAL TMSNANDGIN
     LERLETIGDS FLKYAITTYL YITYENVHEG KLSHLRSKQV ANLNLYRLGR RKRLGEYMIA
     TKFEPHDNWL PPCYYVPKEL EKALIEAKIP THHWKLADLL DIKNLSSVQI CEMVREKADA
     LGLEQNGGAQ NGQLDDSNDS CNDFSCFIPY NLVSQHSIPD KSIADCVEAL IGAYLIECGP
     RGALLFMAWL GVRVLPITRQ LDGGNQEQRI PGSTKPNAEN VVTVYGAWPT PRSPLLHFAP
     NATEELDQLL SGFEEFEESL GYKFRDRSYL LQAMTHASYT PNRLTDCYQR LEFLGDAVLD
     YLITRHLYED PRQHSPGALT DLRSALVNNT IFASLAVRHG FHKFFRHLSP GLNDVIDRFV
     RIQQENGHCI SEEYYLLSEE ECDDAEDVEV PKALGDVFES IAGAIFLDSN MSLDVVWHVY
     SNMMSPEIEQ FSNSVPKSPI RELLELEPET AKFGKPEKLA DGRRVRVTVD VFCKGTFRGI
     GRNYRIAKCT AAKCALRQLK KQGLIAKKD
//
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