GenomeNet

Database: UniProt
Entry: Q9SP32
LinkDB: Q9SP32
Original site: Q9SP32 
ID   DCL1_ARATH              Reviewed;        1909 AA.
AC   Q9SP32; Q9FDY6; Q9MAN0;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   13-NOV-2019, entry version 156.
DE   RecName: Full=Endoribonuclease Dicer homolog 1;
DE            EC=3.1.26.-;
DE   AltName: Full=Dicer-like protein 1;
DE            Short=AtDCL1;
DE   AltName: Full=Protein ABNORMAL SUSPENSOR 1;
DE   AltName: Full=Protein CARPEL FACTORY;
DE   AltName: Full=Protein SHORT INTEGUMENTS 1;
DE   AltName: Full=Protein SUSPENSOR 1;
GN   Name=DCL1; Synonyms=ASU1, CAF SIN1, SUS1; OrderedLocusNames=At1g01040;
GN   ORFNames=T25K16.4;
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], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF 1837-ASN--LYS-1843 AND 1844-ASN--SER-1909.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=10556049;
RA   Jacobsen S.E., Running M.P., Meyerowitz E.M.;
RT   "Disruption of an RNA helicase/RNase III gene in Arabidopsis causes
RT   unregulated cell division in floral meristems.";
RL   Development 126:5231-5243(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-415
RP   AND ILE-431.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=12376646; DOI=10.1104/pp.003491;
RA   Golden T.A., Schauer S.E., Lang J.D., Pien S., Mushegian A.R.,
RA   Grossniklaus U., Meinke D.W., Ray A.;
RT   "SHORT INTEGUMENTS1/SUSPENSOR1/CARPEL FACTORY, a Dicer homolog, is a
RT   maternal effect gene required for embryo development in Arabidopsis.";
RL   Plant Physiol. 130:808-822(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
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   [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, SUBCELLULAR LOCATION, AND INTERACTION WITH DRB1; DRB2 AND
RP   DRB5.
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   [7]
RP   FUNCTION, AND INTERACTION WITH DRB1.
RX   PubMed=16428603; DOI=10.1261/rna.2146906;
RA   Kurihara Y., Takashi Y., Watanabe Y.;
RT   "The interaction between DCL1 and HYL1 is important for efficient and
RT   precise processing of pri-miRNA in plant microRNA biogenesis.";
RL   RNA 12:206-212(2006).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17442570; DOI=10.1016/j.cub.2007.04.005;
RA   Fang Y., Spector D.L.;
RT   "Identification of nuclear dicing bodies containing proteins for
RT   microRNA biogenesis in living Arabidopsis plants.";
RL   Curr. Biol. 17:818-823(2007).
RN   [9]
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   [10]
RP   FUNCTION.
RX   PubMed=17579240; DOI=10.1534/genetics.107.070649;
RA   Schmitz R.J., Hong L., Fitzpatrick K.E., Amasino R.M.;
RT   "DICER-LIKE 1 and DICER-LIKE 3 redundantly act to promote flowering
RT   via repression of FLOWERING LOCUS C in Arabidopsis thaliana.";
RL   Genetics 176:1359-1362(2007).
RN   [11]
RP   FUNCTION.
RX   PubMed=18632569; DOI=10.1073/pnas.0803356105;
RA   Dong Z., Han M.-H., Fedoroff N.;
RT   "The RNA-binding proteins HYL1 and SE promote accurate in vitro
RT   processing of pri-miRNA by DCL1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9970-9975(2008).
RN   [12]
RP   INTERACTION WITH DDL.
RX   PubMed=18632581; DOI=10.1073/pnas.0804218105;
RA   Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M.,
RA   Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.;
RT   "The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act
RT   in small RNA biogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008).
RN   [13]
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   [14]
RP   MUTAGENESIS OF GLU-395.
RX   PubMed=19155326; DOI=10.1261/rna.1297109;
RA   Tagami Y., Motose H., Watanabe Y.;
RT   "A dominant mutation in DCL1 suppresses the hyl1 mutant phenotype by
RT   promoting the processing of miRNA.";
RL   RNA 15:450-458(2009).
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).
CC   -!- FUNCTION: Ribonuclease (RNase) III involved in RNA-mediated post-
CC       transcriptional gene silencing (PTGS). Functions in the microRNAs
CC       (miRNAs) biogenesis pathway by cleaving primary miRNAs (pri-
CC       miRNAs) and precursor miRNAs (pre-miRNAs). Functions with
CC       DRB1/HYL1 and SERRATE proteins for accurate pri-miRNAs to miRNAs
CC       processing. Indirectly involved in the production of trans-acting
CC       small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or
CC       TAS3 endogenous transcripts by participating in the production of
CC       their initiating miRNAs. Involved in the processing of natural
CC       siRNAs (nat-siRNAs, derived from cis-natural antisense
CC       transcripts) by cleaving 24 nucleotide nat-siRNAs into 21
CC       nucleotide nat-siRNAs. Can produce RDR6-dependent endogenous ta-
CC       siRNAs derived from TAS1 and TAS2. Required for the production of
CC       30-40 nucleotide bacterial-induced long siRNAs (lsiRNA). Acts
CC       redundantly with DICER-LIKE 3 (DCL3) to promote flowering via
CC       repression of FLOWERING LOCUS C (FLC). Represses antiviral RNA
CC       silencing through negative regulation of the expression of DCL4
CC       and DCL3. {ECO:0000269|PubMed:15821876,
CC       ECO:0000269|PubMed:16040244, ECO:0000269|PubMed:16428603,
CC       ECO:0000269|PubMed:17579240, ECO:0000269|PubMed:18003861,
CC       ECO:0000269|PubMed:18632569, 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 (via N-terminus) with DDL. Interacts (via DRBM
CC       domains) with DRB1, DRB2 and DRB5. May interact with AGO1 or AGO10
CC       through their common PAZ domains (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8W4D8:DDL; NbExp=2; IntAct=EBI-632627, EBI-2015534;
CC       O04492:DRB1; NbExp=3; IntAct=EBI-632627, EBI-632620;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15821876,
CC       ECO:0000269|PubMed:17442570}. Note=Localizes to nuclear dicing
CC       body (also named D body), a nuclear body distributed throughout
CC       the nucleoplasm and involved in miRNA processing.
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=Q9SP32-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Highly expressed in flowers and seeds and
CC       detected in leaves and stems. Found in ovule integuments,
CC       inflorescence and floral meristems, stigma of flowers until just
CC       before pollination, vasculature of the funiculus, and embryo.
CC       {ECO:0000269|PubMed:10556049, ECO:0000269|PubMed:12376646}.
CC   -!- DEVELOPMENTAL STAGE: Detected in the embryo, but not in the
CC       suspensor, up to the globular stage.
CC       {ECO:0000269|PubMed:12376646}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality in sus-1 mutant. Weaker
CC       mutant (caf-1) also exists. Mutant caf-1 produces extra whorls of
CC       stamens, indefinite number of carpels and show an absence of
CC       axillary inflorescence meristems and abnormally shaped leaves and
CC       floral organs. {ECO:0000269|PubMed:10556049,
CC       ECO:0000269|PubMed:12376646}.
CC   -!- MISCELLANEOUS: Expression in the early embryo is from the
CC       maternally contributed genome.
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF26461.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF187317; AAF03534.1; -; mRNA.
DR   EMBL; AF292940; AAG38019.1; -; mRNA.
DR   EMBL; AF292941; AAG38020.1; -; Genomic_DNA.
DR   EMBL; AC007323; AAF26461.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27220.1; -; Genomic_DNA.
DR   RefSeq; NP_171612.1; NM_099986.4. [Q9SP32-1]
DR   PDB; 2LRS; NMR; -; A=1837-1907.
DR   PDBsum; 2LRS; -.
DR   SMR; Q9SP32; -.
DR   BioGrid; 24809; 10.
DR   DIP; DIP-33454N; -.
DR   IntAct; Q9SP32; 6.
DR   STRING; 3702.AT1G01040.2; -.
DR   PaxDb; Q9SP32; -.
DR   EnsemblPlants; AT1G01040.1; AT1G01040.1; AT1G01040. [Q9SP32-1]
DR   GeneID; 839574; -.
DR   Gramene; AT1G01040.1; AT1G01040.1; AT1G01040. [Q9SP32-1]
DR   KEGG; ath:AT1G01040; -.
DR   Araport; AT1G01040; -.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   eggNOG; COG1111; LUCA.
DR   HOGENOM; HOG000239675; -.
DR   InParanoid; Q9SP32; -.
DR   KO; K11592; -.
DR   PhylomeDB; Q9SP32; -.
DR   PRO; PR:Q9SP32; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SP32; baseline and differential.
DR   Genevisible; Q9SP32; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
DR   CDD; cd00048; DSRM; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   DisProt; DP01467; -.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   Gene3D; 3.30.160.380; -; 1.
DR   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR014720; dsRBD_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; IPR003100; PAZ_dom.
DR   InterPro; IPR036085; PAZ_dom_sf.
DR   InterPro; IPR011907; RNase_III.
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; PF04851; ResIII; 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; SSF101690; SSF101690; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF69065; SSF69065; 2.
DR   PROSITE; PS51327; DICER_DSRBF; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
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; Manganese;
KW   Metal-binding; Nuclease; Nucleotide-binding; Nucleus;
KW   Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing.
FT   CHAIN         1   1909       Endoribonuclease Dicer homolog 1.
FT                                /FTId=PRO_0000180472.
FT   DOMAIN      256    433       Helicase ATP-binding.
FT   DOMAIN      651    812       Helicase C-terminal.
FT   DOMAIN      840    935       Dicer dsRNA-binding fold.
FT   DOMAIN     1180   1318       PAZ.
FT   DOMAIN     1342   1518       RNase III 1.
FT   DOMAIN     1559   1707       RNase III 2.
FT   DOMAIN     1733   1796       DRBM 1.
FT   DOMAIN     1831   1906       DRBM 2.
FT   NP_BIND     269    276       ATP. {ECO:0000255}.
FT   MOTIF       378    381       DECH box.
FT   METAL      1597   1597       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1693   1693       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1696   1696       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1689   1689       Important for activity. {ECO:0000250}.
FT   MUTAGEN     395    395       E->K: In dcl1-13; early-flowering and
FT                                decreased number of leaves. Suppresses
FT                                hyl1 mutant phenotype.
FT                                {ECO:0000269|PubMed:19155326}.
FT   MUTAGEN     415    415       P->S: In sin1-1; impaired reproductive
FT                                development.
FT                                {ECO:0000269|PubMed:12376646}.
FT   MUTAGEN     431    431       I->K: In sin1-2; impaired reproductive
FT                                development.
FT                                {ECO:0000269|PubMed:12376646}.
FT   MUTAGEN    1837   1843       NDICLRK->IAEIDPG: In caf-1; converts the
FT                                floral meristem to an indeterminate
FT                                state. {ECO:0000269|PubMed:10556049}.
FT   MUTAGEN    1844   1909       Missing: In caf-1; converts the floral
FT                                meristem to an indeterminate state.
FT                                {ECO:0000269|PubMed:10556049}.
FT   CONFLICT    148    148       S -> F (in Ref. 1; AAF03534).
FT                                {ECO:0000305}.
FT   CONFLICT    988    988       Y -> H (in Ref. 1; AAF03534).
FT                                {ECO:0000305}.
FT   HELIX      1838   1842       {ECO:0000244|PDB:2LRS}.
FT   STRAND     1849   1854       {ECO:0000244|PDB:2LRS}.
FT   STRAND     1864   1869       {ECO:0000244|PDB:2LRS}.
FT   TURN       1873   1875       {ECO:0000244|PDB:2LRS}.
FT   STRAND     1886   1888       {ECO:0000244|PDB:2LRS}.
FT   HELIX      1889   1903       {ECO:0000244|PDB:2LRS}.
FT   HELIX      1904   1906       {ECO:0000244|PDB:2LRS}.
SQ   SEQUENCE   1909 AA;  213574 MW;  EAA944F0C0C81D4C CRC64;
     MVMEDEPREA TIKPSYWLDA CEDISCDLID DLVSEFDPSS VAVNESTDEN GVINDFFGGI
     DHILDSIKNG GGLPNNGVSD TNSQINEVTV TPQVIAKETV KENGLQKNGG KRDEFSKEEG
     DKDRKRARVC SYQSERSNLS GRGHVNNSRE GDRFMNRKRT RNWDEAGNNK KKRECNNYRR
     DGRDREVRGY WERDKVGSNE LVYRSGTWEA DHERDVKKVS GGNRECDVKA EENKSKPEER
     KEKVVEEQAR RYQLDVLEQA KAKNTIAFLE TGAGKTLIAI LLIKSVHKDL MSQNRKMLSV
     FLVPKVPLVY QQAEVIRNQT CFQVGHYCGE MGQDFWDSRR WQREFESKQV LVMTAQILLN
     ILRHSIIRME TIDLLILDEC HHAVKKHPYS LVMSEFYHTT PKDKRPAIFG MTASPVNLKG
     VSSQVDCAIK IRNLETKLDS TVCTIKDRKE LEKHVPMPSE IVVEYDKAAT MWSLHETIKQ
     MIAAVEEAAQ ASSRKSKWQF MGARDAGAKD ELRQVYGVSE RTESDGAANL IHKLRAINYT
     LAELGQWCAY KVGQSFLSAL QSDERVNFQV DVKFQESYLS EVVSLLQCEL LEGAAAEKVA
     AEVGKPENGN AHDEMEEGEL PDDPVVSGGE HVDEVIGAAV ADGKVTPKVQ SLIKLLLKYQ
     HTADFRAIVF VERVVAALVL PKVFAELPSL SFIRCASMIG HNNSQEMKSS QMQDTISKFR
     DGHVTLLVAT SVAEEGLDIR QCNVVMRFDL AKTVLAYIQS RGRARKPGSD YILMVERGNV
     SHAAFLRNAR NSEETLRKEA IERTDLSHLK DTSRLISIDA VPGTVYKVEA TGAMVSLNSA
     VGLVHFYCSQ LPGDRYAILR PEFSMEKHEK PGGHTEYSCR LQLPCNAPFE ILEGPVCSSM
     RLAQQAVCLA ACKKLHEMGA FTDMLLPDKG SGQDAEKADQ DDEGEPVPGT ARHREFYPEG
     VADVLKGEWV SSGKEVCESS KLFHLYMYNV RCVDFGSSKD PFLSEVSEFA ILFGNELDAE
     VLSMSMDLYV ARAMITKASL AFKGSLDITE NQLSSLKKFH VRLMSIVLDV DVEPSTTPWD
     PAKAYLFVPV TDNTSMEPIK GINWELVEKI TKTTAWDNPL QRARPDVYLG TNERTLGGDR
     REYGFGKLRH NIVFGQKSHP TYGIRGAVAS FDVVRASGLL PVRDAFEKEV EEDLSKGKLM
     MADGCMVAED LIGKIVTAAH SGKRFYVDSI CYDMSAETSF PRKEGYLGPL EYNTYADYYK
     QKYGVDLNCK QQPLIKGRGV SYCKNLLSPR FEQSGESETV LDKTYYVFLP PELCVVHPLS
     GSLIRGAQRL PSIMRRVESM LLAVQLKNLI SYPIPTSKIL EALTAASCQE TFCYERAELL
     GDAYLKWVVS RFLFLKYPQK HEGQLTRMRQ QMVSNMVLYQ FALVKGLQSY IQADRFAPSR
     WSAPGVPPVF DEDTKDGGSS FFDEEQKPVS EENSDVFEDG EMEDGELEGD LSSYRVLSSK
     TLADVVEALI GVYYVEGGKI AANHLMKWIG IHVEDDPDEV DGTLKNVNVP ESVLKSIDFV
     GLERALKYEF KEKGLLVEAI THASRPSSGV SCYQRLEFVG DAVLDHLITR HLFFTYTSLP
     PGRLTDLRAA AVNNENFARV AVKHKLHLYL RHGSSALEKQ IREFVKEVQT ESSKPGFNSF
     GLGDCKAPKV LGDIVESIAG AIFLDSGKDT TAAWKVFQPL LQPMVTPETL PMHPVRELQE
     RCQQQAEGLE YKASRSGNTA TVEVFIDGVQ VGVAQNPQKK MAQKLAARNA LAALKEKEIA
     ESKEKHINNG NAGEDQGENE NGNKKNGHQP FTRQTLNDIC LRKNWPMPSY RCVKEGGPAH
     AKRFTFGVRV NTSDRGWTDE CIGEPMPSVK KAKDSAAVLL LELLNKTFS
//
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