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NRPA2_ARATH
ID   NRPA2_ARATH             Reviewed;        1178 AA.
AC   F4I366; Q0WLL1; Q9C8S4; Q9FXG4;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=DNA-directed RNA polymerase I subunit 2 {ECO:0000305};
DE   AltName: Full=DNA-directed RNA polymerase I subunit RPA2 {ECO:0000305};
DE            Short=DNA polymerase I subunit A2 {ECO:0000305};
DE            EC=2.7.7.6 {ECO:0000305};
DE   AltName: Full=Nuclear RNA polymerase A2 {ECO:0000312|EMBL:AEE31152.1};
GN   Name=NRPA2 {ECO:0000312|EMBL:AEE31152.1}; Synonyms=RPA2 {ECO:0000305};
GN   OrderedLocusNames=At1g29940 {ECO:0000312|Araport:AT1G29940};
GN   ORFNames=F1N18.2 {ECO:0000312|EMBL:AAG10602.1},
GN   T1P2.15 {ECO:0000312|EMBL:AAG52049.1};
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=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] OF 601-1178.
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, AND DISRUPTION PHENOTYPE.
RX   PubMed=18723889; DOI=10.1534/genetics.108.090621;
RA   Onodera Y., Nakagawa K., Haag J.R., Pikaard D., Mikami T., Ream T., Ito Y.,
RA   Pikaard C.S.;
RT   "Sex-biased lethality or transmission of defective transcription machinery
RT   in Arabidopsis.";
RL   Genetics 180:207-218(2008).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Second largest core component of RNA polymerase I which synthesizes
CC       ribosomal RNA precursors. Proposed to contribute to the polymerase
CC       catalytic activity and forms the polymerase active center together with
CC       the largest subunit. Pol I is composed of mobile elements and NRPA2 is
CC       part of the core element with the central large cleft and probably a
CC       clamp element that moves to open and close the cleft.
CC       {ECO:0000250|UniProtKB:P22138}.
CC   -!- FUNCTION: Essential for the completion of the three rounds of mitosis
CC       in female megaspores required for the development of mature
CC       gametophytes. {ECO:0000269|PubMed:18723889}.
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=2.7.7.6; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC       of at least 13 subunits. {ECO:0000250|UniProtKB:P22138}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22138}.
CC   -!- DISRUPTION PHENOTYPE: Defect in seed production due to female
CC       gametophyte developmental arrest. {ECO:0000269|PubMed:18723889}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG10602.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG52049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AY075644; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC008030; AAG10602.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC022455; AAG52049.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31152.1; -; Genomic_DNA.
DR   EMBL; AY075644; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK230187; BAF01996.1; -; mRNA.
DR   PIR; B86423; B86423.
DR   RefSeq; NP_564341.2; NM_102734.5.
DR   AlphaFoldDB; F4I366; -.
DR   SMR; F4I366; -.
DR   IntAct; F4I366; 1.
DR   STRING; 3702.AT1G29940.1; -.
DR   iPTMnet; F4I366; -.
DR   PaxDb; F4I366; -.
DR   PRIDE; F4I366; -.
DR   ProteomicsDB; 250601; -.
DR   EnsemblPlants; AT1G29940.1; AT1G29940.1; AT1G29940.
DR   GeneID; 839872; -.
DR   Gramene; AT1G29940.1; AT1G29940.1; AT1G29940.
DR   KEGG; ath:AT1G29940; -.
DR   Araport; AT1G29940; -.
DR   TAIR; locus:2019272; AT1G29940.
DR   eggNOG; KOG0216; Eukaryota.
DR   HOGENOM; CLU_000524_5_1_1; -.
DR   InParanoid; F4I366; -.
DR   OMA; FFGVVHY; -.
DR   OrthoDB; 42570at2759; -.
DR   PRO; PR:F4I366; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4I366; baseline and differential.
DR   Genevisible; F4I366; AT.
DR   GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0009561; P:megagametogenesis; IMP:UniProtKB.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   InterPro; IPR009674; Rpa2_dom_4.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF06883; RNA_pol_Rpa2_4; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   2: Evidence at transcript level;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Nucleus; Reference proteome; Ribosome biogenesis; Transcription;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1178
FT                   /note="DNA-directed RNA polymerase I subunit 2"
FT                   /id="PRO_0000434009"
FT   ZN_FING         1097..1137
FT                   /note="C4-type"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1002
FT                   /note="G -> D (in Ref. 4; BAF01996)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1178 AA;  132381 MW;  9660FCAEF8FD6086 CRC64;
     MVVNAKDSTV PTMEDFKELH NLVTHHIESF DYMTLKGLDV MFNRIKPVSV YDPNTENELS
     IWLENPLVFA PQKESFKSTS RKEPLLPFEC RQAKISYTGT FMADVCFKYN DGVVVRDKFD
     FGQFPIMLMS KLCSLKGADC RKLLKCKEST SEMGGYFILN GIERVFRCVI APKRNHPTSM
     IRNSFRDRKE GYSSKAVVTR CVRDDQSSVT VKLYYLRNGS ARVGFWIVGR EYLLPVGLVL
     KALTNSCDEE IYESLNCCYS EHYGRGDGAI GTQLVRERAK IILDEVRDLG LFTREQCRKH
     LGQHFQPVLD GVKKESLSIV AEAVLRDYLF VHLDNDHDKF NLLIFIIQKL YSLVDQTSLP
     DNPDSLQNQE ILVPGHVITI YLKEKLEEWL RKCKSLLKDE LDNTNSKFSF ESLADVKKLI
     NKNPPRSIGT SIETLLKTGA LKTQSGLDLQ QRAGYTVQAE RLNFLRFLSF FRAVHRGASF
     AGLRTTTVRK LLPESWGFLC PVHTPDGTPC GLLNHMTRTS RITSQFDSKG NIRDFLKIRK
     SVVDVLTGAG MVPSLPKLVR AGPPKVIHVL LDGQVVGTLS SNLVTKVVSY IRRLKVEAPS
     VIPEDLEVGY VPTSMGGSYP GLYLASCPAR FIRPVKNISI PSDNIELIGP FEQVFMEISC
     PDGGNGGRNN SSLATHEEIH PTGMISVVAN LTPWSDHNQS PRNMYQCQMA KQTMAYSTQA
     LQFRADQKIY HLQTPQSPVV RTKTYTTYSI DENPTGTNAI VAVLAHTGFD MEDAMILNKS
     SVERGMCHGQ IYQTENIDLS DQNSRFDSGS KSFRRSTNKA EHFRIDADGL PSVGQKLYPD
     EPYCSIYDEV TNKTRHMKRK GTDPVIVDFV SVDMKSKKHP QRANIRFRHA RNPIIGDKFS
     SRHGQKGVCS QLWPDIDMPF NGVTGMRPDL IINPHAFPSR MTIAMLLESI AAKGGSLHGK
     FVDATPFRDA VKKTNGEEES KSSLLVDDLG SMLKEKGFNH YGTETLYSGY LGVELKCEIF
     MGPVYYQRLR HMVSDKFQVR STGQVDQLTH QPIKGRKRGG GIRFGEMERD SLLAHGASYL
     LHDRLHTSSD HHIADVCSLC GSLLTSSVVN VQQKKLIQEI GKLPPGRTPK KVTCYSCKTS
     KGMETVAMPY VFRYLAAELA SMNIKMTLQL SDREGVTD
 
 
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