RPOA_CUSRE
ID RPOA_CUSRE Reviewed; 335 AA.
AC Q8SKY1; A7M995;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE Short=PEP {ECO:0000255|HAMAP-Rule:MF_00059};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059};
DE AltName: Full=Plastid-encoded RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE Short=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059};
OS Cuscuta reflexa (Southern Asian dodder).
OG Plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Monogynella.
OX NCBI_TaxID=4129;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Berg S.;
RT "Sequence analysis and coding potential of the holoparasitic flowering
RT plant genus Cuscuta.";
RL Thesis (2002), Christian-Albrechts University, Germany.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL BMC Plant Biol. 7:45-45(2007).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
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|HAMAP-Rule:MF_00059};
CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
CC -!- SUBCELLULAR LOCATION: Plastid.
CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC transcription, whereas the C-terminal domain is involved in interaction
CC with transcriptional regulators and with upstream promoter elements.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
CC -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC some thylakoids, although the photosynthetic activity does not exceed
CC the light compensation point. {ECO:0000305}.
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DR EMBL; AJ439611; CAD28795.1; -; Genomic_DNA.
DR EMBL; AM711640; CAM98423.1; -; Genomic_DNA.
DR RefSeq; YP_001430136.1; NC_009766.1.
DR AlphaFoldDB; Q8SKY1; -.
DR SMR; Q8SKY1; -.
DR PRIDE; Q8SKY1; -.
DR GeneID; 5536609; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR011773; DNA-dir_RpoA.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR011260; RNAP_asu_C.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR32108; PTHR32108; 1.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF03118; RNA_pol_A_CTD; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR TIGRFAMs; TIGR02027; rpoA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Transcription; Transferase.
FT CHAIN 1..335
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175449"
FT REGION 1..231
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 262..335
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT CONFLICT 27
FT /note="L -> P (in Ref. 1; CAD28795)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="F -> L (in Ref. 1; CAD28795)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="L -> S (in Ref. 1; CAD28795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38382 MW; 1F1EB5E2A011534F CRC64;
MVREKVTVST RTLQWKCVES RTDSKRLYYG RFILSPLTKG QADTIGIAMR RALLAEIEGT
RITRVKFANT SHEYSTIAGI QESVHEILMN LKEIVLRSNL YGTCDASISI KGPGYVTAED
IILPPHVEIV DSTQHIAWLT EPINFFIGLK IERNHGYFIK THANFEDGSY PIDALFMPVR
NANHSINSYG NEKQEILFLE IWTNGSLTPK EALHEASRNL IDLFIPFLHM EEENLHLEDA
DHTIPLSPFT VYDKVAKLRK NKKKLSLESI FIDQLEFPPK IYNCLKKSNI FTLLDLLNNS
QEDLIKIEHF HLEDVKQILG ILGKHFALDL PKNLN
