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RPB8B_ARATH
ID   RPB8B_ARATH             Reviewed;         146 AA.
AC   Q9M1A8;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=DNA-directed RNA polymerases II, IV and V subunit 8B;
DE   AltName: Full=RNA polymerase Rpb8;
GN   Name=NRPB8B; Synonyms=NRPD8B, NRPE8B; OrderedLocusNames=At3g59600;
GN   ORFNames=T16L24.150;
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=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   [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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH THE MEDIATOR
RP   COMPLEX.
RX   PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA   Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT   "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT   as the Med25 subunit.";
RL   Mol. Cell 26:717-729(2007).
RN   [7]
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       polymerases IV and V which mediate short-interfering RNAs (siRNA)
CC       accumulation and subsequent 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, IV and V complexes.
CC       Associates with the mediator complex. {ECO:0000269|PubMed:19110459}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RPB8 RNA polymerase subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AL138659; CAB75457.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79944.1; -; Genomic_DNA.
DR   EMBL; AK119016; BAC43592.1; -; mRNA.
DR   EMBL; BT008531; AAP40358.1; -; mRNA.
DR   EMBL; AY086002; AAM63211.1; -; mRNA.
DR   PIR; T49301; T49301.
DR   RefSeq; NP_191519.1; NM_115822.4.
DR   PDB; 7EU0; EM; 3.16 A; H=1-146.
DR   PDB; 7EU1; EM; 3.86 A; H=1-146.
DR   PDBsum; 7EU0; -.
DR   PDBsum; 7EU1; -.
DR   AlphaFoldDB; Q9M1A8; -.
DR   SMR; Q9M1A8; -.
DR   BioGRID; 10443; 25.
DR   IntAct; Q9M1A8; 1.
DR   STRING; 3702.AT3G59600.1; -.
DR   PaxDb; Q9M1A8; -.
DR   PRIDE; Q9M1A8; -.
DR   ProteomicsDB; 228223; -.
DR   EnsemblPlants; AT3G59600.1; AT3G59600.1; AT3G59600.
DR   GeneID; 825129; -.
DR   Gramene; AT3G59600.1; AT3G59600.1; AT3G59600.
DR   KEGG; ath:AT3G59600; -.
DR   Araport; AT3G59600; -.
DR   TAIR; locus:2097468; AT3G59600.
DR   eggNOG; KOG3400; Eukaryota.
DR   HOGENOM; CLU_103864_1_1_1; -.
DR   InParanoid; Q9M1A8; -.
DR   OMA; TINAYVS; -.
DR   OrthoDB; 1504067at2759; -.
DR   PhylomeDB; Q9M1A8; -.
DR   PRO; PR:Q9M1A8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M1A8; baseline and differential.
DR   Genevisible; Q9M1A8; 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:0000418; C:RNA polymerase IV complex; IDA:UniProtKB.
DR   GO; GO:0000419; C:RNA polymerase V complex; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR005570; RNA_pol_Rpb8.
DR   PANTHER; PTHR10917; PTHR10917; 1.
DR   Pfam; PF03870; RNA_pol_Rpb8; 1.
DR   PIRSF; PIRSF000779; RNA_pol_Rpb8; 1.
DR   SMART; SM00658; RPOL8c; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Reference proteome.
FT   CHAIN           1..146
FT                   /note="DNA-directed RNA polymerases II, IV and V subunit
FT                   8B"
FT                   /id="PRO_0000423325"
FT   STRAND          9..19
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   STRAND          28..34
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   STRAND          40..45
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   STRAND          93..99
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   STRAND          120..124
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   TURN            127..129
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   STRAND          135..144
FT                   /evidence="ECO:0007829|PDB:7EU0"
SQ   SEQUENCE   146 AA;  16603 MW;  230F6E9995E368B7 CRC64;
     MASNIIMFED IFVVDKLDPD GKKFDKVTRV EARSHNLEMF MHLDVNTEVY PLAVGDKFTL
     AMAPTLNLDG TPDTGYFTPG AKKTLADKYE YIMHGKLYKI SERDGKTPKA ELYVSFGGLL
     MLLQGDPAHI SHFELDQRLF LLMRKL
 
 
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