RPO2B_TOBAC
ID RPO2B_TOBAC Reviewed; 1021 AA.
AC Q8L6J3; Q8L6J7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=DNA-directed RNA polymerase 2B, chloroplastic/mitochondrial;
DE EC=2.7.7.6;
DE AltName: Full=NictaRpoT2-tom;
DE AltName: Full=T7 bacteriophage-type single subunit RNA polymerase 2B;
DE Flags: Precursor;
GN Name=RPOT2-TOM;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=12061895; DOI=10.1046/j.1365-313x.2002.01318.x;
RA Hedtke B., Legen J., Weihe A., Herrmann R.G., Boerner T.;
RT "Six active phage-type RNA polymerase genes in Nicotiana tabacum.";
RL Plant J. 30:625-637(2002).
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: Plastid, chloroplast
CC {ECO:0000269|PubMed:12061895}. Mitochondrion
CC {ECO:0000269|PubMed:12061895}.
CC -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC family. {ECO:0000305}.
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DR EMBL; AJ416569; CAC95020.1; -; mRNA.
DR EMBL; AJ416573; CAC95024.1; -; Genomic_DNA.
DR RefSeq; NP_001311818.1; NM_001324889.1.
DR AlphaFoldDB; Q8L6J3; -.
DR SMR; Q8L6J3; -.
DR GeneID; 107765810; -.
DR KEGG; nta:107765810; -.
DR Proteomes; UP000084051; Unplaced.
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 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Mitochondrion;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT CHAIN ?..1021
FT /note="DNA-directed RNA polymerase 2B,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000046034"
FT REGION 315..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 722
FT /evidence="ECO:0000250"
FT ACT_SITE 797
FT /evidence="ECO:0000250"
FT ACT_SITE 954
FT /evidence="ECO:0000250"
SQ SEQUENCE 1021 AA; 116163 MW; D4F0CC22CD0AE6C1 CRC64;
MSSTKTPISL TIKLNQFTDK PTGLDINRYH NSPIMWRNII KQLSSRTPQK LLFSSKNRTY
SFLGFGQDSV FKDNTKFRSL IPISCSNIVM GFQNLGEYLP GDEFLSRPLL KNQVNSNDFC
CRKSYASVAE AVAVSSTDAE EDVSVVDEVQ ELLTELKKEE KKQFAFRRRK QRMLTSGMGH
RKYQTLKRRQ VKVETEAWEQ AAKEYKELLF DMCEQKLAPN LPYVKSLFLG WFEPLRDKIA
EEQELCSQGK SKAAYAKYLY QLPADMMAVI TMHKLMGLLM TGGDHGTARV VQAALVIGDA
IEQEVRIHNF LEKTKKQKAE KDKQKEDGEH VTQEQEKLRK KVTNLMKKQK LRAVGQIVRR
QDDSKPWGQD AKAKVGSRLI ELLLQTAYIQ PPANQLAVDP PDIRPAFLHS VRTVAKETKS
ASRRYGIIQC DELVFKGLER TARHMVIPYM PMLVPPVKWT GYDKGGHLYL PSYVMRTHGA
RQQREAVKRA SRNQLQPVFE ALDTLGSTKW RINKRVLSVI DRIWAGGGRL ADLVDRDDAP
LPEEPDTEDE ALRTKWRWKV KSVKKENRER HSQRCDIELK LAVARKMKDE EGFFYPHNVD
FRGRAYPMHP HLNHLGSDIC RGVLVFAEGR PLGESGLRWL KIHLANLFAG GVEKLSLEGR
IAFTENHMDD IFDSADKPLE GRRWWLNAED PFQCLAVCIN LSEAVRSSSP ETSISHIPVH
QDGSCNGLQH YAALGRDELG AAAVNLVAGE KPADVYSGIA ARVLDIMKRD AQRDPAEFPD
AVRARALVNQ VDRKLVKQTV MTSVYGVTYI GARDQIKRRL KERGAIADDS ELFGAACYAA
KVTLTALGEM FEAARSIMTW LGECAKIIAS ENEPVRWTTP LGLPVVQPYR KIGRHLIKTS
LQILTLQQET EKVMVKRQRT AFPPNFIHSL DGSHMMMTAV ACRRAGLNFA GVHDSYWTHA
CDVDKLNRIL REKFVELYET PILEKLLESF QTSYPTLLFP PLPERGDFDL RDVLESPYFF
N