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RPB6B_ARATH
ID   RPB6B_ARATH             Reviewed;         144 AA.
AC   Q9SJ96;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=DNA-directed RNA polymerases II and V subunit 6B;
GN   Name=NRPB6B; Synonyms=NRPE6B; OrderedLocusNames=At2g04630;
GN   ORFNames=F28I8.33;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND NOMENCLATURE.
RX   PubMed=19110459; DOI=10.1016/j.molcel.2008.12.015;
RA   Ream T.S., Haag J.R., Wierzbicki A.T., Nicora C.D., Norbeck A.D., Zhu J.K.,
RA   Hagen G., Guilfoyle T.J., Pasa-Tolic L., Pikaard C.S.;
RT   "Subunit compositions of the RNA-silencing enzymes Pol IV and Pol V reveal
RT   their origins as specialized forms of RNA polymerase II.";
RL   Mol. Cell 33:192-203(2009).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Component of RNA polymerase II which synthesizes mRNA precursors and
CC       many functional non-coding RNAs. Pol II is the central component of the
CC       basal RNA polymerase II transcription machinery. It is composed of
CC       mobile elements that move relative to each other. Component of RNA
CC       polymerase V which mediates RNA-directed DNA methylation-dependent
CC       (RdDM) transcriptional gene silencing (TGS) of endogenous repeated
CC       sequences, including transposable elements.
CC       {ECO:0000269|PubMed:19110459}.
CC   -!- SUBUNIT: Component of the RNA polymerase II and V complexes.
CC       {ECO:0000269|PubMed:19110459}.
CC   -!- INTERACTION:
CC       Q9SJ96; Q9LNC9: MYB13; NbExp=3; IntAct=EBI-4429205, EBI-25521688;
CC       Q9SJ96; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-4429205, EBI-4426557;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC       subunit family. {ECO:0000305}.
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DR   EMBL; AC006955; AAD22343.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05851.1; -; Genomic_DNA.
DR   EMBL; BT010184; AAQ22653.1; -; mRNA.
DR   EMBL; AK229481; BAF01339.1; -; mRNA.
DR   PIR; E84459; E84459.
DR   RefSeq; NP_178540.1; NM_126492.4.
DR   AlphaFoldDB; Q9SJ96; -.
DR   SMR; Q9SJ96; -.
DR   BioGRID; 407; 16.
DR   IntAct; Q9SJ96; 10.
DR   STRING; 3702.AT2G04630.1; -.
DR   PaxDb; Q9SJ96; -.
DR   PRIDE; Q9SJ96; -.
DR   ProteomicsDB; 227975; -.
DR   EnsemblPlants; AT2G04630.1; AT2G04630.1; AT2G04630.
DR   GeneID; 815006; -.
DR   Gramene; AT2G04630.1; AT2G04630.1; AT2G04630.
DR   KEGG; ath:AT2G04630; -.
DR   Araport; AT2G04630; -.
DR   TAIR; locus:2049213; AT2G04630.
DR   eggNOG; KOG3405; Eukaryota.
DR   HOGENOM; CLU_112527_1_0_1; -.
DR   InParanoid; Q9SJ96; -.
DR   OMA; ALIVICH; -.
DR   OrthoDB; 1488436at2759; -.
DR   PhylomeDB; Q9SJ96; -.
DR   PRO; PR:Q9SJ96; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJ96; baseline and differential.
DR   Genevisible; Q9SJ96; AT.
DR   GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
DR   GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR   GO; GO:0000419; C:RNA polymerase V complex; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.90.940.10; -; 1.
DR   HAMAP; MF_00192; RNApol_arch_Rpo6; 1.
DR   InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR   InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR   InterPro; IPR028363; RPB6.
DR   InterPro; IPR036161; RPB6/omega-like_sf.
DR   InterPro; IPR006111; Rpo6/Rpb6.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   PIRSF; PIRSF500154; RPB6; 1.
DR   PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR   SMART; SM01409; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; SSF63562; 1.
DR   PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE   1: Evidence at protein level;
KW   DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription.
FT   CHAIN           1..144
FT                   /note="DNA-directed RNA polymerases II and V subunit 6B"
FT                   /id="PRO_0000423323"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   144 AA;  16740 MW;  8210BE0CECE7DE9F CRC64;
     MADDDYNEVD DLGYEDEPAE PEIEEGVEED ADIKENDDVN VDPLETEDKV ETEPVQRPRK
     TSKFMTKYER ARILGTRALQ ISMNAPVMVE LEGETDPLEI AMKELRQRKI PFTIRRYLPD
     MSYEEWGVDE LIVEDSWKRQ VGGD
 
 
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