ID   NRPC2_ARATH             Reviewed;        1161 AA.
AC   F4KD38; Q9FKF1;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=DNA-directed RNA polymerase III subunit 2 {ECO:0000305};
DE   AltName: Full=DNA-directed RNA polymerase III subunit RPC2 {ECO:0000305};
DE            Short=DNA polymerase I subunit C2 {ECO:0000305};
DE            EC=2.7.7.6 {ECO:0000305};
DE   AltName: Full=Nuclear RNA polymerase C2 {ECO:0000312|EMBL:AED95209.1};
GN   Name=NRPC2 {ECO:0000312|EMBL:AED95209.1}; Synonyms=RPC2 {ECO:0000305};
GN   OrderedLocusNames=At5g45140 {ECO:0000312|Araport:AT5G45140};
GN   ORFNames=K18C1.1 {ECO:0000312|EMBL:BAB11387.1};
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=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
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   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 III which synthesizes
CC       small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the
CC       polymerase catalytic activity and forms the polymerase active center
CC       together with the largest subunit. Pol III is composed of mobile
CC       elements and NRPC2 is part of the core element with the central large
CC       cleft and probably a clamp element that moves to open and close the
CC       cleft. {ECO:0000250|UniProtKB:P22276}.
CC   -!- FUNCTION: Essential for the completion of the three rounds of mitosis
CC       in female megaspores required for the development of mature
CC       gametophytes (PubMed:18723889). {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 III (Pol III) complex
CC       consisting of 17 subunits. {ECO:0000250|UniProtKB:P22276}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22276}.
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=BAB11387.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB012240; BAB11387.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED95209.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70451.1; -; Genomic_DNA.
DR   EMBL; AY123987; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001332060.1; NM_001344590.1.
DR   RefSeq; NP_199327.4; NM_123882.5.
DR   AlphaFoldDB; F4KD38; -.
DR   SMR; F4KD38; -.
DR   STRING; 3702.AT5G45140.1; -.
DR   PaxDb; F4KD38; -.
DR   PRIDE; F4KD38; -.
DR   ProteomicsDB; 250568; -.
DR   EnsemblPlants; AT5G45140.1; AT5G45140.1; AT5G45140.
DR   EnsemblPlants; AT5G45140.2; AT5G45140.2; AT5G45140.
DR   GeneID; 834550; -.
DR   Gramene; AT5G45140.1; AT5G45140.1; AT5G45140.
DR   Gramene; AT5G45140.2; AT5G45140.2; AT5G45140.
DR   KEGG; ath:AT5G45140; -.
DR   Araport; AT5G45140; -.
DR   TAIR; locus:2153323; AT5G45140.
DR   eggNOG; KOG0215; Eukaryota.
DR   HOGENOM; CLU_000524_5_1_1; -.
DR   InParanoid; F4KD38; -.
DR   OMA; CIKYIIR; -.
DR   OrthoDB; 42570at2759; -.
DR   PRO; PR:F4KD38; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KD38; baseline and differential.
DR   Genevisible; F4KD38; AT.
DR   GO; GO:0005666; C:RNA polymerase III 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: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; IPR007646; RNA_pol_Rpb2_4.
DR   InterPro; IPR007647; RNA_pol_Rpb2_5.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 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; PF04566; RNA_pol_Rpb2_4; 1.
DR   Pfam; PF04567; RNA_pol_Rpb2_5; 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; Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1161
FT                   /note="DNA-directed RNA polymerase III subunit 2"
FT                   /id="PRO_0000434011"
FT   ZN_FING         1104..1125
FT                   /note="C4-type"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1161 AA;  130212 MW;  9A19AAD8E9E44DA9 CRC64;
     MGLDQEDLDL TNDDHFIDKE KLSAPIKSTA DKFQLVPEFL KVRGLVKQHL DSFNYFINVG
     IHKIVKANSR ITSTVDPSIY LRFKKVRVGE PSIINVNTVE NINPHMCRLA DMTYAAPIFV
     NIEYVHGSHG NKAKSAKDNV IIGRMPIMLR SCRCVLHGKD EEELARLGEC PLDPGGYFII
     KGTEKVLLIQ EQLSKNRIII DSDKKGNINA SVTSSTEMTK SKTVIQMEKE KIYLFLHRFV
     KKIPIIIVLK AMGMESDQEI VQMVGRDPRF SASLLPSIEE CVSEGVNTQK QALDYLEAKV
     KKISYGTPPE KDGRALSILR DLFLAHVPVP DNNFRQKCFY VGVMLRRMIE AMLNKDAMDD
     KDYVGNKRLE LSGQLISLLF EDLFKTMLSE AIKNVDHILN KPIRASRFDF SQCLNKDSRY
     SISLGLERTL STGNFDIKRF RMHRKGMTQV LTRLSFIGSM GFITKISPQF EKSRKVSGPR
     SLQPSQWGML CPCDTPEGES CGLVKNLALM THVTTDEEEG PLVAMCYKLG VTDLEVLSAE
     ELHTPDSFLV ILNGLILGKH SRPQYFANSL RRLRRAGKIG EFVSVFTNEK QHCVYVASDV
     GRVCRPLVIA DKGISRVKQH HMKELQDGVR TFDDFIRDGL IEYLDVNEEN NALIALYESD
     GTTELDEGAE AAKADTTHIE IEPFTILGVV AGLIPYPHHN QSPRNTYQCA MGKQAMGNIA
     YNQLNRMDTL LYLLVYPQRP LLTTRTIELV GYDKLGAGQN ATVAVMSFSG YDIEDAIVMN
     KSSLDRGFGR CIVMKKIVAM SQKYDNCTAD RILIPQRTGP DAEKMQILDD DGLATPGEII
     RPNDIYINKQ VPVDTVTKFT SALSDSQYRP AREYFKGPEG ETQVVDRVAL CSDKKGQLCI
     KYIIRHTRRP ELGDKFSSRH GQKGVCGIII QQEDFPFSEL GICPDLIMNP HGFPSRMTVG
     KMIELLGSKA GVSCGRFHYG SAFGERSGHA DKVETISATL VEKGFSYSGK DLLYSGISGE
     PVEAYIFMGP IYYQKLKHMV LDKMHARGSG PRVMMTRQPT EGKSKNGGLR VGEMERDCLI
     AYGASMLIYE RLMISSDPFE VQVCRACGLL GYYNYKLKKA VCTTCKNGDN IATMKLPYAC
     KLLFQELQSM NVVPRLKLTE A