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NRPBA_ARATH
ID   NRPBA_ARATH             Reviewed;          71 AA.
AC   Q8LFJ6;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=DNA-directed RNA polymerases II, IV and V subunit 10;
DE   AltName: Full=DNA-directed RNA Polymerase II subunit L;
GN   Name=NRPB10; Synonyms=NRPD10, NRPE10; OrderedLocusNames=At1g11475;
GN   ORFNames=T23J18.30;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., 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., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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].
RA   Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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   [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).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NRPD1, AND SUBUNIT.
RX   PubMed=21811420; DOI=10.1371/journal.pgen.1002195;
RA   Law J.A., Vashisht A.A., Wohlschlegel J.A., Jacobsen S.E.;
RT   "SHH1, a homeodomain protein required for DNA methylation, as well as RDR2,
RT   RDM4, and chromatin remodeling factors, associate with RNA polymerase IV.";
RL   PLoS Genet. 7:E1002195-E1002195(2011).
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       Interacts with NRPD1. {ECO:0000269|PubMed:19110459,
CC       ECO:0000269|PubMed:21811420}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA
CC       polymerase subunit family. {ECO:0000305}.
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DR   EMBL; AC011661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002684; AEE28741.1; -; Genomic_DNA.
DR   EMBL; AK118363; BAC42977.1; -; mRNA.
DR   EMBL; BT025306; ABF47122.1; -; mRNA.
DR   EMBL; AK228397; BAF00334.1; -; mRNA.
DR   EMBL; AY084808; AAM61374.1; -; mRNA.
DR   RefSeq; NP_849640.1; NM_179309.3.
DR   PDB; 7EU0; EM; 3.16 A; J=1-71.
DR   PDB; 7EU1; EM; 3.86 A; J=1-71.
DR   PDBsum; 7EU0; -.
DR   PDBsum; 7EU1; -.
DR   AlphaFoldDB; Q8LFJ6; -.
DR   SMR; Q8LFJ6; -.
DR   BioGRID; 22930; 49.
DR   STRING; 3702.AT1G11475.1; -.
DR   PaxDb; Q8LFJ6; -.
DR   PRIDE; Q8LFJ6; -.
DR   ProteomicsDB; 249448; -.
DR   EnsemblPlants; AT1G11475.1; AT1G11475.1; AT1G11475.
DR   GeneID; 837690; -.
DR   Gramene; AT1G11475.1; AT1G11475.1; AT1G11475.
DR   KEGG; ath:AT1G11475; -.
DR   Araport; AT1G11475; -.
DR   TAIR; locus:2823924; AT1G11475.
DR   eggNOG; KOG3497; Eukaryota.
DR   HOGENOM; CLU_143122_2_1_1; -.
DR   InParanoid; Q8LFJ6; -.
DR   OMA; RCCMLLA; -.
DR   OrthoDB; 1639063at2759; -.
DR   PhylomeDB; Q8LFJ6; -.
DR   PRO; PR:Q8LFJ6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8LFJ6; baseline and differential.
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:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IBA:GO_Central.
DR   InterPro; IPR023580; RNA_pol_su_RPB10.
DR   InterPro; IPR020789; RNA_pol_suN_Zn-BS.
DR   InterPro; IPR000268; RPABC5/Rpb10.
DR   PANTHER; PTHR23431; PTHR23431; 1.
DR   Pfam; PF01194; RNA_pol_N; 1.
DR   PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1.
DR   SUPFAM; SSF46924; SSF46924; 1.
DR   PROSITE; PS01112; RNA_POL_N_8KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Zinc.
FT   CHAIN           1..71
FT                   /note="DNA-directed RNA polymerases II, IV and V subunit
FT                   10"
FT                   /id="PRO_0000423319"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   HELIX           18..26
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   HELIX           31..37
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   HELIX           43..51
FT                   /evidence="ECO:0007829|PDB:7EU0"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:7EU0"
SQ   SEQUENCE   71 AA;  8315 MW;  7129BA3099216AD4 CRC64;
     MIIPVRCFTC GKVIGNKWDQ YLDLLQLDYT EGDALDALQL VRYCCRRMLM THVDLIEKLL
     NYNTLEKSDN S
 
 
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