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RDR6_ARATH
ID   RDR6_ARATH              Reviewed;        1196 AA.
AC   Q9SG02; A0A1I9LSW2; Q9LKP0;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=RNA-dependent RNA polymerase 6;
DE            Short=AtRDRP6;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein SILENCING DEFECTIVE 1;
DE   AltName: Full=Protein SUPPRESSOR OF GENE SILENCING 2;
DE   AltName: Full=RNA-directed RNA polymerase 6;
GN   Name=RDR6; Synonyms=RDRP6, SDE1, SGS2; OrderedLocusNames=At3g49500;
GN   ORFNames=T1G12.20, T9C5.95;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF GLU-429; GLU-453; GLY-825; ASP-826; SER-860 AND GLY-866.
RC   STRAIN=cv. Columbia;
RX   PubMed=10850495; DOI=10.1016/s0092-8674(00)80863-6;
RA   Mourrain P., Beclin C., Elmayan T., Feuerbach F., Godon C., Morel J.-B.,
RA   Jouette D., Lacombe A.-M., Nikic S., Picault N., Remoue K., Sanial M.,
RA   Vo T.-A., Vaucheret H.;
RT   "Arabidopsis SGS2 and SGS3 genes are required for posttranscriptional gene
RT   silencing and natural virus resistance.";
RL   Cell 101:533-542(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10850496; DOI=10.1016/s0092-8674(00)80864-8;
RA   Dalmay T., Hamilton A., Rudd S., Angell S., Baulcombe D.C.;
RT   "An RNA-dependent RNA polymerase gene in Arabidopsis is required for
RT   posttranscriptional gene silencing mediated by a transgene but not by a
RT   virus.";
RL   Cell 101:543-553(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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 reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-866.
RX   PubMed=15466488; DOI=10.1101/gad.1231804;
RA   Peragine A., Yoshikawa M., Wu G., Albrecht H.L., Poethig R.S.;
RT   "SGS3 and SGS2/SDE1/RDR6 are required for juvenile development and the
RT   production of trans-acting siRNAs in Arabidopsis.";
RL   Genes Dev. 18:2368-2379(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=15165191; DOI=10.1111/j.1365-313x.2004.02103.x;
RA   Muangsan N., Beclin C., Vaucheret H., Robertson D.;
RT   "Geminivirus VIGS of endogenous genes requires SGS2/SDE1 and SGS3 and
RT   defines a new branch in the genetic pathway for silencing in plants.";
RL   Plant J. 38:1004-1014(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=16377568; DOI=10.1016/j.cell.2005.11.035;
RA   Borsani O., Zhu J., Verslues P.E., Sunkar R., Zhu J.-K.;
RT   "Endogenous siRNAs derived from a pair of natural cis-antisense transcripts
RT   regulate salt tolerance in Arabidopsis.";
RL   Cell 123:1279-1291(2005).
RN   [8]
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   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16006579; DOI=10.1105/tpc.105.033449;
RA   Li H., Xu L., Wang H., Yuan Z., Cao X., Yang Z., Zhang D., Xu Y., Huang H.;
RT   "The Putative RNA-dependent RNA polymerase RDR6 acts synergistically with
RT   ASYMMETRIC LEAVES1 and 2 to repress BREVIPEDICELLUS and MicroRNA165/166 in
RT   Arabidopsis leaf development.";
RL   Plant Cell 17:2157-2171(2005).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF PRO-611 AND ASP-826.
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 through
RT   AGO7.";
RL   Curr. Biol. 16:927-932(2006).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17384170; DOI=10.1105/tpc.106.045724;
RA   Luo Z., Chen Z.;
RT   "Improperly terminated, unpolyadenylated mRNA of sense transgenes is
RT   targeted by RDR6-mediated RNA silencing in Arabidopsis.";
RL   Plant Cell 19:943-958(2007).
RN   [12]
RP   FUNCTION, AND MUTAGENESIS OF ASP-867.
RX   PubMed=18063577; DOI=10.1074/jbc.m708983200;
RA   Curaba J., Chen X.;
RT   "Biochemical activities of Arabidopsis RNA-dependent RNA polymerase 6.";
RL   J. Biol. Chem. 283:3059-3066(2008).
RN   [13]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH SGS3.
RX   PubMed=19332064; DOI=10.1016/j.febslet.2009.03.055;
RA   Kumakura N., Takeda A., Fujioka Y., Motose H., Takano R., Watanabe Y.;
RT   "SGS3 and RDR6 interact and colocalize in cytoplasmic SGS3/RDR6-bodies.";
RL   FEBS Lett. 583:1261-1266(2009).
RN   [14]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19308254; DOI=10.1371/journal.pone.0004971;
RA   Qi X., Bao F.S., Xie Z.;
RT   "Small RNA deep sequencing reveals role for Arabidopsis thaliana RNA-
RT   dependent RNA polymerases in viral siRNA biogenesis.";
RL   PLoS ONE 4:E4971-E4971(2009).
RN   [15]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20208518; DOI=10.1038/nature08828;
RA   Olmedo-Monfil V., Duran-Figueroa N., Arteaga-Vazquez M., Demesa-Arevalo E.,
RA   Autran D., Grimanelli D., Slotkin R.K., Martienssen R.A.,
RA   Vielle-Calzada J.P.;
RT   "Control of female gamete formation by a small RNA pathway in
RT   Arabidopsis.";
RL   Nature 464:628-632(2010).
RN   [16]
RP   FUNCTION.
RX   PubMed=20562854; DOI=10.1038/nsmb.1866;
RA   Cuperus J.T., Carbonell A., Fahlgren N., Garcia-Ruiz H., Burke R.T.,
RA   Takeda A., Sullivan C.M., Gilbert S.D., Montgomery T.A., Carrington J.C.;
RT   "Unique functionality of 22-nt miRNAs in triggering RDR6-dependent siRNA
RT   biogenesis from target transcripts in Arabidopsis.";
RL   Nat. Struct. Mol. Biol. 17:997-1003(2010).
CC   -!- FUNCTION: RNA-dependent RNA polymerase involved in post-transcriptional
CC       gene silencing (PTGS). Possesses ssRNA and ssDNA-dependent polymerase
CC       activity, but does not have priming activity. Possesses in vitro 3'
CC       nucleotidyltransferase activity in the presence of UTP as single
CC       nucleotide. Required for the production of 21 nucleotide trans-acting
CC       small interfering RNAs (ta-siRNAs) derived from TAS1, TAS2 and TAS3
CC       endogenous transcripts. Acts in the RDR6/SGS3/DCL4/AGO7 ta-siRNA
CC       pathway involved in leaf developmental timing. Required for the
CC       production of natural siRNAs (nat-siRNAs) derived from cis-natural
CC       antisense transcripts. Required for the production of 24 nucleotide
CC       nat-siRNAs derived from the stress-related P5CDH-SRO5 antisense gene
CC       pair. Required for PTGS induced by transgene direct repeats. Plays an
CC       essential role in transitive silencing of transgenes by processing
CC       secondary siRNAs. This pathway, which requires DCL2 and DCL4, amplifies
CC       silencing by using the target RNA as substrate to generate secondary
CC       siRNAs, providing an efficient mechanism for long-distance silencing.
CC       Involved in the biogenesis of secondary siRNAs which require 22
CC       nucleotide miRNAs associated to AGO1. Participates synergistically with
CC       AS1 and AS2 to proper plant development by repressing the miR165 and
CC       miR166 microRNAs (independently of AGO10) that may lead to mRNA
CC       degradation of genes in the class III HD-ZIP family. Required for the
CC       production of some small RNAs derived from the crucifer-infecting
CC       tobamovirus (TMV-cg). Required for sense virus-induced post-
CC       transcriptional gene silencing (S-PTGS). {ECO:0000269|PubMed:10850495,
CC       ECO:0000269|PubMed:10850496, ECO:0000269|PubMed:15165191,
CC       ECO:0000269|PubMed:15466488, ECO:0000269|PubMed:16006579,
CC       ECO:0000269|PubMed:16131612, ECO:0000269|PubMed:16377568,
CC       ECO:0000269|PubMed:16682354, ECO:0000269|PubMed:17384170,
CC       ECO:0000269|PubMed:18063577, ECO:0000269|PubMed:19308254,
CC       ECO:0000269|PubMed:20208518, ECO:0000269|PubMed:20562854}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48;
CC   -!- SUBUNIT: Interacts with SGS3. {ECO:0000269|PubMed:19332064}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC       {ECO:0000269|PubMed:19332064}. Nucleus {ECO:0000269|PubMed:17384170}.
CC       Note=Colocalize with SGS3 in cytoplasmic granules distinct from P-
CC       bodies. {ECO:0000269|PubMed:19332064}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16006579}.
CC   -!- DISRUPTION PHENOTYPE: First leaves are elongated and curl downward.
CC       Presence of stigmatic tissue in the middle of the septum at the apical
CC       end of the carpels. Altered post-transcriptional gene silencing (PTGS).
CC       Accumulation of ARF4 mRNA (targeted by TAS3-derived siRNAs). Upon
CC       infection, over-accumulation of CMV RNA and enhanced susceptibility to
CC       cucumber mosaic virus (CMV). Reduced levels of TMV-cg-derived small
CC       RNAs. {ECO:0000269|PubMed:10850495, ECO:0000269|PubMed:10850496,
CC       ECO:0000269|PubMed:15466488, ECO:0000269|PubMed:17384170,
CC       ECO:0000269|PubMed:19308254, ECO:0000269|PubMed:20208518}.
CC   -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000305}.
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DR   EMBL; AF239718; AAF73959.1; -; Genomic_DNA.
DR   EMBL; AF268093; AAF74208.1; -; Genomic_DNA.
DR   EMBL; AC012329; AAG52184.1; -; Genomic_DNA.
DR   EMBL; AL132964; CAB71285.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78550.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65667.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65668.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65669.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65670.1; -; Genomic_DNA.
DR   RefSeq; NP_001327617.1; NM_001339423.1.
DR   RefSeq; NP_001327618.1; NM_001339424.1.
DR   RefSeq; NP_001327619.1; NM_001339425.1.
DR   RefSeq; NP_001327620.1; NM_001339426.1.
DR   RefSeq; NP_190519.1; NM_114810.3.
DR   AlphaFoldDB; Q9SG02; -.
DR   SMR; Q9SG02; -.
DR   BioGRID; 9430; 1.
DR   IntAct; Q9SG02; 1.
DR   MINT; Q9SG02; -.
DR   STRING; 3702.AT3G49500.1; -.
DR   PaxDb; Q9SG02; -.
DR   PRIDE; Q9SG02; -.
DR   ProteomicsDB; 236991; -.
DR   EnsemblPlants; AT3G49500.1; AT3G49500.1; AT3G49500.
DR   EnsemblPlants; AT3G49500.2; AT3G49500.2; AT3G49500.
DR   EnsemblPlants; AT3G49500.3; AT3G49500.3; AT3G49500.
DR   EnsemblPlants; AT3G49500.4; AT3G49500.4; AT3G49500.
DR   EnsemblPlants; AT3G49500.5; AT3G49500.5; AT3G49500.
DR   GeneID; 824112; -.
DR   Gramene; AT3G49500.1; AT3G49500.1; AT3G49500.
DR   Gramene; AT3G49500.2; AT3G49500.2; AT3G49500.
DR   Gramene; AT3G49500.3; AT3G49500.3; AT3G49500.
DR   Gramene; AT3G49500.4; AT3G49500.4; AT3G49500.
DR   Gramene; AT3G49500.5; AT3G49500.5; AT3G49500.
DR   KEGG; ath:AT3G49500; -.
DR   Araport; AT3G49500; -.
DR   TAIR; locus:2114633; AT3G49500.
DR   eggNOG; KOG0988; Eukaryota.
DR   HOGENOM; CLU_001366_3_1_1; -.
DR   InParanoid; Q9SG02; -.
DR   OMA; HPKWVKK; -.
DR   OrthoDB; 63910at2759; -.
DR   PhylomeDB; Q9SG02; -.
DR   BRENDA; 2.7.7.48; 399.
DR   PRO; PR:Q9SG02; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SG02; baseline and differential.
DR   Genevisible; Q9SG02; AT.
DR   GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; ISS:TAIR.
DR   GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR   GO; GO:0031047; P:gene silencing by RNA; IMP:TAIR.
DR   GO; GO:0048467; P:gynoecium development; IMP:TAIR.
DR   GO; GO:0048366; P:leaf development; IGI:TAIR.
DR   GO; GO:0010492; P:maintenance of shoot apical meristem identity; IEA:EnsemblPlants.
DR   GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:TAIR.
DR   GO; GO:0048544; P:recognition of pollen; IMP:TAIR.
DR   GO; GO:0009616; P:RNAi-mediated antiviral immune response; IMP:TAIR.
DR   GO; GO:0030422; P:siRNA processing; IEP:TAIR.
DR   GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR   PANTHER; PTHR23079; PTHR23079; 1.
DR   Pfam; PF05183; RdRP; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   1: Evidence at protein level;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Nucleus;
KW   Plant defense; Reference proteome; RNA-binding;
KW   RNA-directed RNA polymerase; RNA-mediated gene silencing; Transferase.
FT   CHAIN           1..1196
FT                   /note="RNA-dependent RNA polymerase 6"
FT                   /id="PRO_0000404677"
FT   MUTAGEN         429
FT                   /note="E->K: Alters post-transcriptional gene silencing."
FT                   /evidence="ECO:0000269|PubMed:10850495"
FT   MUTAGEN         453
FT                   /note="E->K: Alters post-transcriptional gene silencing."
FT                   /evidence="ECO:0000269|PubMed:10850495"
FT   MUTAGEN         611
FT                   /note="P->L: Alters post-transcriptional gene silencing."
FT                   /evidence="ECO:0000269|PubMed:16682354"
FT   MUTAGEN         825
FT                   /note="G->E: Alters post-transcriptional gene silencing."
FT                   /evidence="ECO:0000269|PubMed:10850495"
FT   MUTAGEN         826
FT                   /note="D->N: Alters post-transcriptional gene silencing."
FT                   /evidence="ECO:0000269|PubMed:10850495,
FT                   ECO:0000269|PubMed:16682354"
FT   MUTAGEN         860
FT                   /note="S->F: Alters post-transcriptional gene silencing."
FT                   /evidence="ECO:0000269|PubMed:10850495"
FT   MUTAGEN         866
FT                   /note="G->E: In rdr6-13; alters post-transcriptional gene
FT                   silencing."
FT                   /evidence="ECO:0000269|PubMed:10850495,
FT                   ECO:0000269|PubMed:15466488"
FT   MUTAGEN         867
FT                   /note="D->A: Loss of polymerase activity."
FT                   /evidence="ECO:0000269|PubMed:18063577"
FT   CONFLICT        597
FT                   /note="D -> G (in Ref. 2; AAF74208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        646
FT                   /note="F -> I (in Ref. 2; AAF74208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        681
FT                   /note="D -> V (in Ref. 2; AAF74208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        696
FT                   /note="N -> D (in Ref. 2; AAF74208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        700
FT                   /note="D -> V (in Ref. 2; AAF74208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        805
FT                   /note="T -> K (in Ref. 2; AAF74208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        998
FT                   /note="R -> P (in Ref. 2; AAF74208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1044
FT                   /note="L -> S (in Ref. 2; AAF74208)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1196 AA;  136929 MW;  812DEB9CEDC82C8F CRC64;
     MGSEGNMKKS VVTQVSIGGF GESTTAKQLT DYLEDEVGIV WRCRLKTSWT PPGSYPNFEI
     ADTSNIPSID EYKKVEPHAF VHFAVFESAG RAMDAAGQCN LILDGQPLKV SLGPKNPYSL
     NQRRRTTVPY KLAGITLEIG TLVSRDDFFV SWRAEGVDFL VDPFDNTCKF CFRKSTAFSF
     KDAVMHAVIN CDYKLELLVR DIQTVRQYKT LHGFVLILQL ASSPRVWYRT ADDDIYDTVP
     GDLLDDDDPW IRTTDFTQVG AIGRCHSYRV LISPRYENKL RTALDYFRMR RVQEERVRWP
     PRIRNEPCFG EPVSDHFFCI HHKEGISFEI MFLVNSVLHR GVFNQFQLTE RFFDLLRNQP
     KDVNIASLKH LCTYKRPVFD AYKRLKLVQE WIQKNPKLLG SHEQSEDISE IRRLVITPTR
     AYCLPPEVEL SNRVLRRYKA VAERFLRVTF MDESMQTINS NVLSYFVAPI VKDLTSSSFS
     QKTYVFKRVK SILTDGFKLC GRKYSFLAFS ANQLRDRSAW FFAEDGKTRV SDIKTWMGKF
     KDKNVAKCAA RMGLCFSSTY ATVDVMPHEV DTEVPDIERN GYVFSDGIGT ITPDLADEVM
     EKLKLDVHYS PCAYQIRYAG FKGVVARWPS KSDGIRLALR DSMKKFFSKH TILEICSWTR
     FQPGFLNRQI ITLLSVLGVP DEIFWDMQES MLYKLNRILD DTDVAFEVLT ASCAEQGNTA
     AIMLSAGFKP KTEPHLRGML SSVRIAQLWG LREKSRIFVT SGRWLMGCLD EAGILEHGQC
     FIQVSKPSIE NCFSKHGSRF KETKTDLEVV KGYVAIAKNP CLHPGDVRIL EAVDVPQLHH
     MYDCLIFPQK GDRPHTNEAS GSDLDGDLYF VAWDQKLIPP NRKSYPAMHY DAAEEKSLGR
     AVNHQDIIDF FARNLANEQL GTICNAHVVH ADRSEYGAMD EECLLLAELA ATAVDFPKTG
     KIVSMPFHLK PKLYPDFMGK EDYQTYKSNK ILGRLYRRVK EVYDEDAEAS SEESTDPSAI
     PYDAVLEIPG FEDLIPEAWG HKCLYDGQLI GLLGQYKVQK EEEIVTGHIW SMPKYTSKKQ
     GELKERLKHS YNSLKKEFRK VFEETIPDHE NLSEEEKNIL YEKKASAWYH VTYHPEWVKK
     SLELQDPDES SHAAMLSFAW IAADYLARIK IRSREMGSID SAKPVDSLAK FLAQRL
 
 
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