ID   RPOT2_ARATH             Reviewed;        1011 AA.
AC   Q9LFV6; O23644;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=DNA-directed RNA polymerase 2, chloroplastic/mitochondrial;
DE            EC=2.7.7.6;
DE   Flags: Precursor;
GN   Name=RPOT2; OrderedLocusNames=At5g15700; ORFNames=F14F8_80;
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 [MRNA], GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=11258484; DOI=10.1093/embo-reports/kvd086;
RA   Hedtke B., Boerner T., Weihe A.;
RT   "One RNA polymerase serving two genomes.";
RL   EMBO Rep. 1:435-440(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sanchez H., Schuster W.;
RT   "Cloning of three single-subunit RNA polymerases from Arabidopsis
RT   thaliana.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
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   [5]
RP   INTERACTION WITH NIP1 AND NIP2.
RX   PubMed=18567673; DOI=10.1073/pnas.0800909105;
RA   Azevedo J., Courtois F., Hakimi M.A., Demarsy E., Lagrange T.,
RA   Alcaraz J.P., Jaiswal P., Marechal-Drouard L., Lerbs-Mache S.;
RT   "Intraplastidial trafficking of a phage-type RNA polymerase is mediated by
RT   a thylakoid RING-H2 protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9123-9128(2008).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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:0000255|PROSITE-ProRule:PRU10031,
CC         ECO:0000255|PROSITE-ProRule:PRU10032};
CC   -!- SUBUNIT: Interacts with NIP1 and NIP2. {ECO:0000269|PubMed:18567673}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:11258484}. Mitochondrion
CC       {ECO:0000269|PubMed:11258484}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9LFV6-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ278248; CAC17120.1; -; mRNA.
DR   EMBL; AJ001037; CAA04491.1; -; Genomic_DNA.
DR   EMBL; AL391144; CAC01769.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92193.1; -; Genomic_DNA.
DR   PIR; T51399; T51399.
DR   RefSeq; NP_197074.1; NM_121574.3. [Q9LFV6-1]
DR   AlphaFoldDB; Q9LFV6; -.
DR   SMR; Q9LFV6; -.
DR   BioGRID; 16700; 2.
DR   STRING; 3702.AT5G15700.2; -.
DR   iPTMnet; Q9LFV6; -.
DR   PaxDb; Q9LFV6; -.
DR   PRIDE; Q9LFV6; -.
DR   ProteomicsDB; 228240; -. [Q9LFV6-1]
DR   EnsemblPlants; AT5G15700.1; AT5G15700.1; AT5G15700. [Q9LFV6-1]
DR   GeneID; 831424; -.
DR   Gramene; AT5G15700.1; AT5G15700.1; AT5G15700. [Q9LFV6-1]
DR   KEGG; ath:AT5G15700; -.
DR   Araport; AT5G15700; -.
DR   eggNOG; KOG1038; Eukaryota.
DR   HOGENOM; CLU_003364_4_0_1; -.
DR   InParanoid; Q9LFV6; -.
DR   OMA; KERDMIC; -.
DR   PhylomeDB; Q9LFV6; -.
DR   PRO; PR:Q9LFV6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFV6; baseline and differential.
DR   Genevisible; Q9LFV6; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase 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; IBA:GO_Central.
DR   GO; GO:0006390; P:mitochondrial transcription; IBA:GO_Central.
DR   Gene3D; 1.10.1320.10; -; 1.
DR   Gene3D; 1.10.287.260; -; 1.
DR   InterPro; IPR024075; DNA-dir_RNA_pol_helix_hairp_sf.
DR   InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR037159; RNA_POL_N_sf.
DR   InterPro; IPR029262; RPOL_N.
DR   PANTHER; PTHR10102; PTHR10102; 1.
DR   Pfam; PF00940; RNA_pol; 1.
DR   Pfam; PF14700; RPOL_N; 1.
DR   SMART; SM01311; RPOL_N; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR   PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chloroplast; DNA-directed RNA polymerase;
KW   Mitochondrion; Nucleotidyltransferase; Plastid; Reference proteome;
KW   Transcription; Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast and mitochondrion"
FT   CHAIN           ?..1011
FT                   /note="DNA-directed RNA polymerase 2,
FT                   chloroplastic/mitochondrial"
FT                   /id="PRO_0000046032"
FT   REGION          307..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        712
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        787
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        944
FT                   /evidence="ECO:0000250"
FT   CONFLICT        466
FT                   /note="K -> R (in Ref. 2; CAA04491)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        748
FT                   /note="G -> E (in Ref. 2; CAA04491)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1011 AA;  114521 MW;  6CAF27FB160FE1B2 CRC64;
     MSSAQTPLFL ANQTKVFDHL IPLHKPFISS PNPVSQSFPM WRNIAKQAIS RSAARLNVSS
     QTRGLLVSSP ESIFSKNLSF RFPVLGSPCH GKGFRCLSGI TRREEFSKSE RCLSGTLARG
     YTSVAEEEVL STDVEEEPEV DELLKEMKKE KKRESHRSWR MKKQDQFGMG RTKFQNLWRR
     QVKIETEEWE RAAAEYMELL TDMCEQKLAP NLPYVKSLFL GWFEPLRDAI AKDQELYRLG
     KSKATYAHYL DQLPADKISV ITMHKLMGHL MTGGDNGCVK VVHAACTVGD AIEQEIRICT
     FLDKKKKGDD NEESGGVENE TSMKEQDKLR KKVNELIKKQ KLSAVRKILQ SHDYTKPWIA
     DVRAKVGSRL IELLVRTAYI QSPADQQDND LPDVRPAFVH TFKVAKGSMN SGRKYGVIEC
     DPLVRKGLEK SGRYAVMPYM PMLVPPLKWS GYDKGAYLFL TSYIMKTHGA KQQREALKSA
     PKGQLQPVFE ALDTLGSTKW RVNKRVLTVV DRIWSSGGCV ADMVDRSDVP LPEKPDTEDE
     GILKKWKWEV KSAKKVNSER HSQRCDTELK LSVARKMKDE EAFYYPHNMD FRGRAYPMPP
     HLNHLGSDLC RGVLEFAEGR PMGISGLRWL KIHLANLYAG GVDKLSLDGR LAFTENHLDD
     IFDSADRPLE GSRWWLQAED PFQCLAVCIS LTEALRSPSP ETVLSHIPIH QDGSCNGLQH
     YAALGRDTLG AEAVNLVAGE KPADVYSGIA TRVLDIMRRD ADRDPEVFPE ALRARKLLNQ
     VDRKLVKQTV MTSVYGVTYI GARDQIKRRL KERSDFGDEK EVFGAACYAA KVTLAAIDEM
     FQAARAIMRW FGECAKIIAS ENETVRWTTP LGLPVVQPYH QMGTKLVKTS LQTLSLQHET
     DQVIVRRQRT AFPPNFIHSL DGSHMMMTAV ACKRAGVCFA GVHDSFWTHA CDVDKLNIIL
     REKFVELYSQ PILENLLESF EQSFPHLDFP PLPERGDLDL KVVLDSPYFF N