RPOT1_ARATH
ID RPOT1_ARATH Reviewed; 976 AA.
AC P92969; O23698;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=DNA-directed RNA polymerase 1, mitochondrial;
DE EC=2.7.7.6;
DE Flags: Precursor;
GN Name=RPOT1; Synonyms=RPOMT; OrderedLocusNames=At1g68990; ORFNames=T6L1.17;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9242608; DOI=10.1126/science.277.5327.809;
RA Hedtke B., Boerner T., Weihe A.;
RT "Mitochondrial and chloroplast phage-type RNA polymerases in Arabidopsis.";
RL Science 277:809-811(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Schuster W.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 SUBCELLULAR LOCATION.
RX PubMed=10205908; DOI=10.1046/j.1365-313x.1999.00393.x;
RA Hedtke B., Meixner M., Gillandt S., Richter E., Boerner T., Weihe A.;
RT "Green fluorescent protein as a marker to investigate targeting of
RT organellar RNA polymerases of higher plants in vivo.";
RL Plant J. 17:557-561(1999).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
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).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10205908}.
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=P92969-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC family. {ECO:0000305}.
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DR EMBL; Y08137; CAA69331.1; -; mRNA.
DR EMBL; Y09006; CAA70210.1; -; Genomic_DNA.
DR EMBL; Y09432; CAA70583.1; -; Genomic_DNA.
DR EMBL; AC011665; AAG51592.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34873.1; -; Genomic_DNA.
DR PIR; D96714; D96714.
DR RefSeq; NP_177063.1; NM_105571.4. [P92969-1]
DR AlphaFoldDB; P92969; -.
DR SMR; P92969; -.
DR STRING; 3702.AT1G68990.2; -.
DR PaxDb; P92969; -.
DR PRIDE; P92969; -.
DR ProteomicsDB; 228233; -. [P92969-1]
DR EnsemblPlants; AT1G68990.1; AT1G68990.1; AT1G68990. [P92969-1]
DR GeneID; 843232; -.
DR Gramene; AT1G68990.1; AT1G68990.1; AT1G68990. [P92969-1]
DR KEGG; ath:AT1G68990; -.
DR Araport; AT1G68990; -.
DR eggNOG; KOG1038; Eukaryota.
DR HOGENOM; CLU_003364_4_0_1; -.
DR InParanoid; P92969; -.
DR OMA; FAESHLE; -.
DR PhylomeDB; P92969; -.
DR PRO; PR:P92969; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92969; baseline and differential.
DR Genevisible; P92969; AT.
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 2: Evidence at transcript level;
KW Alternative splicing; DNA-directed RNA polymerase; Mitochondrion;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..976
FT /note="DNA-directed RNA polymerase 1, mitochondrial"
FT /id="PRO_0000031070"
FT ACT_SITE 677
FT /evidence="ECO:0000250"
FT ACT_SITE 752
FT /evidence="ECO:0000250"
FT ACT_SITE 909
FT /evidence="ECO:0000250"
FT CONFLICT 498
FT /note="E -> V (in Ref. 1; CAA69331)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="G -> S (in Ref. 1; CAA69331)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="V -> I (in Ref. 1; CAA69331)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="I -> V (in Ref. 1; CAA69331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 976 AA; 110930 MW; 75DFCF64465450D7 CRC64;
MWRNILGRAS LRKVKFLSDS SSSGTHYPVN RVRGILSSVN LSGVRNGLSI NPVNEMGGLS
SFRHGQCYVF EGYATAAQAI DSTDPEDESS GSDEVNELIT EMEKETERIR KKARLAAIPP
KRVIAGMGAQ KFYMLKQRQV KMETEEWERA ARECREILAD MCEQKLAPNL PYMKSLFLGW
FEPVRNAIQD DLDTFKIKKG KIPYAPFMEQ LPADKMAVIT MHKMMGLLMT NAEGVGIVKL
VNAATQIGEA VEQEVRINSF LQKKNKKNAT DKTINTEAEN VSEEIVAKET EKARKQVTVL
MEKNKLRQVK ALVRKHDSFK PWGQEAQVKV GARLIQLLME NAYIQPPAEQ FDDGPPDIRP
AFKQNFRTVT LENTKTSRRY GCIECDPLVL KGLDKSARHM VIPYLPMLIP PQNWTGYDQG
AHFFLPSYVM RTHGAKQQRT VMKRTPKEQL EPVYEALDTL GNTKWKINKK VLSLVDRIWA
NGGRIGGLVD REDVPIPEEP EREDQEKFKN WRWESKKAIK QNNERHSQRC DIELKLEVAR
KMKDEEGFYY PHNVDFRGRA YPIHPYLNHL GSDLCRGILE FCEGKPLGKS GLRWLKIHIA
NLYAGGVDKL AYEDRIAFTE SHLEDIFDSS DRPLEGKRWW LNAEDPFQCL AACINLSEAL
RSPFPEAAIS HIPIHQDGSC NGLQHYAALG RDKLGADAVN LVTGEKPADV YTEIAARVLK
IMQQDAEEDP ETFPNATYAK LMLDQVDRKL VKQTVMTSVY GVTYSGARDQ IKKRLKERGT
FEDDSLTFHA SCYAAKITLK ALEEMFEAAR AIKSWFGDCA KIIASENNAV CWTTPLGLPV
VQPYRKPGRH LVKTTLQVLT LSRETDKVMA RRQMTAFAPN FIHSLDGSHM MMTAVACNRA
GLSFAGVHDS FWTHACDVDV MNTILREKFV ELYEKPILEN LLESFQKSFP DISFPPLPER
GDFDLRKVLE STYFFN
