GenomeNet

Database: UniProt
Entry: DCL4_ARATH
LinkDB: DCL4_ARATH
Original site: DCL4_ARATH 
ID   DCL4_ARATH              Reviewed;        1702 AA.
AC   P84634; Q3SA53;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   31-JUL-2019, entry version 116.
DE   RecName: Full=Dicer-like protein 4;
DE            EC=3.1.26.-;
GN   Name=DCL4; OrderedLocusNames=At5g20320; ORFNames=F5O24.210;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Columbia; TISSUE=Shoot;
RX   PubMed=16129836; DOI=10.1073/pnas.0506426102;
RA   Xie Z., Allen E., Wilken A., Carrington J.C.;
RT   "DICER-LIKE 4 functions in trans-acting small interfering RNA
RT   biogenesis and vegetative phase change in Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12984-12989(2005).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000269|PubMed:11130714};
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH DRB4.
RX   PubMed=15821876; DOI=10.1007/s11103-004-6853-5;
RA   Hiraguri A., Itoh R., Kondo N., Nomura Y., Aizawa D., Murai Y.,
RA   Koiwa H., Seki M., Shinozaki K., Fukuhara T.;
RT   "Specific interactions between Dicer-like proteins and HYL1/DRB-family
RT   dsRNA-binding proteins in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 57:173-188(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=16040244; DOI=10.1016/j.cub.2005.07.024;
RA   Gasciolli V., Mallory A.C., Bartel D.P., Vaucheret H.;
RT   "Partially redundant functions of Arabidopsis DICER-like enzymes and a
RT   role for DCL4 in producing trans-acting siRNAs.";
RL   Curr. Biol. 15:1494-1500(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=16131612; DOI=10.1101/gad.1352605;
RA   Yoshikawa M., Peragine A., Park M.Y., Poethig R.S.;
RT   "A pathway for the biogenesis of trans-acting siRNAs in Arabidopsis.";
RL   Genes Dev. 19:2164-2175(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=16273107; DOI=10.1038/ng1675;
RA   Dunoyer P., Himber C., Voinnet O.;
RT   "DICER-LIKE 4 is required for RNA interference and produces the 21-
RT   nucleotide small interfering RNA component of the plant cell-to-cell
RT   silencing signal.";
RL   Nat. Genet. 37:1356-1360(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=16682354; DOI=10.1016/j.cub.2006.03.035;
RA   Adenot X., Elmayan T., Lauressergues D., Boutet S., Bouche N.,
RA   Gasciolli V., Vaucheret H.;
RT   "DRB4-dependent TAS3 trans-acting siRNAs control leaf morphology
RT   through AGO7.";
RL   Curr. Biol. 16:927-932(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=16810317; DOI=10.1038/sj.emboj.7601217;
RA   Bouche N., Lauressergues D., Gasciolli V., Vaucheret H.;
RT   "An antagonistic function for Arabidopsis DCL2 in development and a
RT   new function for DCL4 in generating viral siRNAs.";
RL   EMBO J. 25:3347-3356(2006).
RN   [10]
RP   FUNCTION.
RX   PubMed=18003861; DOI=10.1101/gad.1595107;
RA   Katiyar-Agarwal S., Gao S., Vivian-Smith A., Jin H.;
RT   "A novel class of bacteria-induced small RNAs in Arabidopsis.";
RL   Genes Dev. 21:3123-3134(2007).
RN   [11]
RP   FUNCTION.
RX   PubMed=17586651; DOI=10.1105/tpc.106.047449;
RA   Diaz-Pendon J.A., Li F., Li W.X., Ding S.W.;
RT   "Suppression of antiviral silencing by cucumber mosaic virus 2b
RT   protein in Arabidopsis is associated with drastically reduced
RT   accumulation of three classes of viral small interfering RNAs.";
RL   Plant Cell 19:2053-2063(2007).
RN   [12]
RP   FUNCTION.
RX   PubMed=17592042; DOI=10.1261/rna.541307;
RA   Moissiard G., Parizotto E.A., Himber C., Voinnet O.;
RT   "Transitivity in Arabidopsis can be primed, requires the redundant
RT   action of the antiviral Dicer-like 4 and Dicer-like 2, and is
RT   compromised by viral-encoded suppressor proteins.";
RL   RNA 13:1268-1278(2007).
RN   [13]
RP   FUNCTION.
RX   PubMed=18353962; DOI=10.1128/JVI.00272-08;
RA   Donaire L., Barajas D., Martinez-Garcia B., Martinez-Priego L.,
RA   Pagan I., Llave C.;
RT   "Structural and genetic requirements for the biogenesis of tobacco
RT   rattle virus-derived small interfering RNAs.";
RL   J. Virol. 82:5167-5177(2008).
RN   [14]
RP   FUNCTION.
RX   PubMed=18799732; DOI=10.1073/pnas.0805760105;
RA   Qu F., Ye X., Morris T.J.;
RT   "Arabidopsis DRB4, AGO1, AGO7, and RDR6 participate in a DCL4-
RT   initiated antiviral RNA silencing pathway negatively regulated by
RT   DCL1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:14732-14737(2008).
RN   [15]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
RN   [16]
RP   STRUCTURE BY NMR OF 651-752.
RX   PubMed=20106953; DOI=10.1261/rna.1965310;
RA   Qin H., Chen F., Huan X., Machida S., Song J., Yuan Y.A.;
RT   "Structure of the Arabidopsis thaliana DCL4 DUF283 domain reveals a
RT   noncanonical double-stranded RNA-binding fold for protein-protein
RT   interaction.";
RL   RNA 16:474-481(2010).
CC   -!- FUNCTION: Ribonuclease (RNase) III involved in RNA-mediated post-
CC       transcriptional gene silencing (PTGS). Functions in the biogenesis
CC       of trans-acting small interfering RNAs (ta-siRNAs, derived from
CC       the TAS1, TAS2 or TAS3 endogenous transcripts) by cleaving small
CC       dsRNAs into 21-24 nucleotide ta-siRNAs. Functions with the dsRNA-
CC       binding protein DRB4 in ta-siRNAs processing. Acts in the
CC       RDR6/SGS3/DCL4/AGO7 ta-siRNA pathway involved in leaf
CC       developmental timing. Plays a role in transitive silencing of
CC       transgenes by processing secondary siRNAs. This pathway, which
CC       requires DCL2 and RDR6, amplifies silencing by using the target
CC       RNA as substrate to generate secondary siRNAs, providing an
CC       efficient mechanism for long-distance silencing. Required for the
CC       production of the 30-40 nucleotide bacterial-induced long siRNAs
CC       (lsiRNA). May participate with DCL3 in the production of 24
CC       nucleotide repeat-associated siRNAs (ra-siRNAs) which derive from
CC       heterochromatin and DNA repeats such as transposons. Plays an
CC       important role in antiviral RNA silencing. Involved in the
CC       production of viral siRNAs derived from the cucumber mosaic virus
CC       (CMV), turnip crinkle virus (TCV) and tobacco rattle virus (TRV).
CC       Targeted by the viral silencing suppressor (VSR) protein 2b of the
CC       cucumber mosaic virus (CMV) that inactivates DCL4 function in RNA
CC       silencing. Does not seem to be involved in microRNAs (miRNAs)
CC       processing. {ECO:0000269|PubMed:16040244,
CC       ECO:0000269|PubMed:16129836, ECO:0000269|PubMed:16131612,
CC       ECO:0000269|PubMed:16273107, ECO:0000269|PubMed:16682354,
CC       ECO:0000269|PubMed:16810317, ECO:0000269|PubMed:17586651,
CC       ECO:0000269|PubMed:17592042, ECO:0000269|PubMed:18003861,
CC       ECO:0000269|PubMed:18353962, ECO:0000269|PubMed:18799732}.
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 DRB4. {ECO:0000269|PubMed:15821876}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15821876}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P84634-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00657}.
DR   EMBL; DQ118423; AAZ80387.1; -; mRNA.
DR   EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92830.1; -; Genomic_DNA.
DR   RefSeq; NP_197532.3; NM_122039.5. [P84634-1]
DR   PDB; 2KOU; NMR; -; A=651-752.
DR   PDBsum; 2KOU; -.
DR   SMR; P84634; -.
DR   BioGrid; 17430; 4.
DR   IntAct; P84634; 2.
DR   MINT; P84634; -.
DR   STRING; 3702.AT5G20320.1; -.
DR   iPTMnet; P84634; -.
DR   PaxDb; P84634; -.
DR   PRIDE; P84634; -.
DR   EnsemblPlants; AT5G20320.1; AT5G20320.1; AT5G20320. [P84634-1]
DR   GeneID; 832154; -.
DR   Gramene; AT5G20320.1; AT5G20320.1; AT5G20320. [P84634-1]
DR   KEGG; ath:AT5G20320; -.
DR   Araport; AT5G20320; -.
DR   TAIR; locus:2149259; AT5G20320.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   eggNOG; COG1111; LUCA.
DR   HOGENOM; HOG000083706; -.
DR   InParanoid; P84634; -.
DR   KO; K11592; -.
DR   OrthoDB; 1337630at2759; -.
DR   PhylomeDB; P84634; -.
DR   EvolutionaryTrace; P84634; -.
DR   PRO; PR:P84634; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P84634; baseline and differential.
DR   Genevisible; P84634; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0016442; C:RISC complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IGI:TAIR.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IMP:TAIR.
DR   GO; GO:0010216; P:maintenance of DNA methylation; IMP:TAIR.
DR   GO; GO:0010492; P:maintenance of shoot apical meristem identity; IEA:EnsemblPlants.
DR   GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IEA:EnsemblPlants.
DR   GO; GO:0010599; P:production of lsiRNA involved in RNA interference; IMP:TAIR.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; IBA:GO_Central.
DR   GO; GO:0010267; P:production of ta-siRNAs involved in RNA interference; IMP:TAIR.
DR   GO; GO:0048608; P:reproductive structure development; IEA:EnsemblPlants.
DR   GO; GO:0051214; P:RNA virus induced gene silencing; IGI:TAIR.
DR   GO; GO:0010050; P:vegetative phase change; IMP:TAIR.
DR   GO; GO:0009616; P:virus induced gene silencing; IGI:TAIR.
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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003100; PAZ_dom.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF00270; DEAD; 1.
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; SM00487; DEXDc; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00949; PAZ; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF69065; SSF69065; 2.
DR   PROSITE; PS51327; DICER_DSRBF; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 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   3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW   Endonuclease; Helicase; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Nucleotide-binding; Nucleus; Plant defense; Reference proteome;
KW   Repeat; RNA-binding; RNA-mediated gene silencing.
FT   CHAIN         1   1702       Dicer-like protein 4.
FT                                /FTId=PRO_0000180475.
FT   DOMAIN      131    307       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      475    629       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      656    748       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      927   1054       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN     1083   1251       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1292   1436       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1462   1528       DRBM 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00266}.
FT   DOMAIN     1621   1697       DRBM 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00266}.
FT   NP_BIND     144    151       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       251    254       DECH box.
FT   COMPBIAS     89    102       Poly-Ser.
FT   METAL      1330   1330       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1422   1422       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1425   1425       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1418   1418       Important for activity. {ECO:0000250}.
FT   HELIX       655    664       {ECO:0000244|PDB:2KOU}.
FT   STRAND      667    669       {ECO:0000244|PDB:2KOU}.
FT   STRAND      678    683       {ECO:0000244|PDB:2KOU}.
FT   HELIX       686    688       {ECO:0000244|PDB:2KOU}.
FT   STRAND      690    695       {ECO:0000244|PDB:2KOU}.
FT   STRAND      705    708       {ECO:0000244|PDB:2KOU}.
FT   HELIX       713    731       {ECO:0000244|PDB:2KOU}.
FT   TURN        735    737       {ECO:0000244|PDB:2KOU}.
FT   HELIX       741    744       {ECO:0000244|PDB:2KOU}.
FT   TURN        748    750       {ECO:0000244|PDB:2KOU}.
SQ   SEQUENCE   1702 AA;  191279 MW;  7AA7647A6BA7F24D CRC64;
     MRDEVDLSLT IPSKLLGKRD REQKNCEEEK NKNKKAKKQQ KDPILLHTSA ATHKFLPPPL
     TMPYSEIGDD LRSLDFDHAD VSSDLHLTSS SSVSSFSSSS SSLFSAAGTD DPSPKMEKDP
     RKIARRYQVE LCKKATEENV IVYLGTGCGK THIAVMLIYE LGHLVLSPKK SVCIFLAPTV
     ALVEQQAKVI ADSVNFKVAI HCGGKRIVKS HSEWEREIAA NEVLVMTPQI LLHNLQHCFI
     KMECISLLIF DECHHAQQQS NHPYAEIMKV FYKSESLQRP RIFGMTASPV VGKGSFQSEN
     LSKSINSLEN LLNAKVYSVE SNVQLDGFVS SPLVKVYYYR SALSDASQST IRYENMLEDI
     KQRCLASLKL LIDTHQTQTL LSMKRLLKRS HDNLIYTLLN LGLWGAIQAA KIQLNSDHNV
     QDEPVGKNPK SKICDTYLSM AAEALSSGVA KDENASDLLS LAALKEPLFS RKLVQLIKIL
     SVFRLEPHMK CIIFVNRIVT ARTLSCILNN LELLRSWKSD FLVGLSSGLK SMSRRSMETI
     LKRFQSKELN LLVATKVGEE GLDIQTCCLV IRYDLPETVT SFIQSRGRAR MPQSEYAFLV
     DSGNEKEMDL IENFKVNEDR MNLEITYRSS EETCPRLDEE LYKVHETGAC ISGGSSISLL
     YKYCSRLPHD EFFQPKPEFQ FKPVDEFGGT ICRITLPANA PISEIESSLL PSTEAAKKDA
     CLKAVHELHN LGVLNDFLLP DSKDEIEDEL SDDEFDFDNI KGEGCSRGDL YEMRVPVLFK
     QKWDPSTSCV NLHSYYIMFV PHPADRIYKK FGFFMKSPLP VEAETMDIDL HLAHQRSVSV
     KIFPSGVTEF DNDEIRLAEL FQEIALKVLF ERGELIPDFV PLELQDSSRT SKSTFYLLLP
     LCLHDGESVI SVDWVTIRNC LSSPIFKTPS VLVEDIFPPS GSHLKLANGC WNIDDVKNSL
     VFTTYSKQFY FVADICHGRN GFSPVKESST KSHVESIYKL YGVELKHPAQ PLLRVKPLCH
     VRNLLHNRMQ TNLEPQELDE YFIEIPPELS HLKIKGLSKD IGSSLSLLPS IMHRMENLLV
     AIELKHVLSA SIPEIAEVSG HRVLEALTTE KCHERLSLER LEVLGDAFLK FAVSRHLFLH
     HDSLDEGELT RRRSNVVNNS NLCRLAIKKN LQVYIRDQAL DPTQFFAFGH PCRVTCDEVA
     SKEVHSLNRD LGILESNTGE IRCSKGHHWL YKKTIADVVE ALVGAFLVDS GFKGAVKFLK
     WIGVNVDFES LQVQDACIAS RRYLPLTTRN NLETLENQLD YKFLHKGLLV QAFIHPSYNR
     HGGGCYQRLE FLGDAVLDYL MTSYFFTVFP KLKPGQLTDL RSLSVNNEAL ANVAVSFSLK
     RFLFCESIYL HEVIEDYTNF LASSPLASGQ SEGPRCPKVL GDLVESCLGA LFLDCGFNLN
     HVWTMMLSFL DPVKNLSNLQ ISPIKELIEL CQSYKWDREI SATKKDGAFT VELKVTKNGC
     CLTVSATGRN KREGTKKAAQ LMITNLKAHE NITTSHPLED VLKNGIRNEA KLIGYNEDPI
     DVVDLVGLDV ENLNILETFG GNSERSSSYV IRRGLPQAPS KTEDRLPQKA IIKAGGPSSK
     TAKSLLHETC VANCWKPPHF ECCEEEGPGH LKSFVYKVIL EVEDAPNMTL ECYGEARATK
     KGAAEHAAQA AIWCLKHSGF LC
//
DBGET integrated database retrieval system