ID   RPOA_PHAAO              Reviewed;         337 AA.
AC   Q3BAK5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
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   Phalaenopsis aphrodite subsp. formosana (Moth orchid).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Vandeae; Aeridinae; Phalaenopsis.
OX   NCBI_TaxID=308872;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Taisugar TS-97;
RX   PubMed=16207935; DOI=10.1093/molbev/msj029;
RA   Chang C.-C., Lin H.-C., Lin I.-P., Chow T.-Y., Chen H.-H., Chen W.-H.,
RA   Cheng C.-H., Lin C.-Y., Liu S.-M., Chang C.-C., Chaw S.-M.;
RT   "The chloroplast genome of Phalaenopsis aphrodite (Orchidaceae):
RT   comparative analysis of evolutionary rate with that of grasses and its
RT   phylogenetic implications.";
RL   Mol. Biol. Evol. 23:279-291(2006).
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, chloroplast.
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}.
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DR   EMBL; AY916449; AAW82531.1; -; Genomic_DNA.
DR   RefSeq; YP_358613.1; NC_007499.1.
DR   AlphaFoldDB; Q3BAK5; -.
DR   SMR; Q3BAK5; -.
DR   GeneID; 3741712; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..337
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000225925"
FT   REGION          1..233
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          265..337
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   337 AA;  38647 MW;  F63A3B76A99EFFBE CRC64;
     MVREDVVGST RTLQWKCVES RVDSKRLYYG RFVLSPLMKG QADTIGIAIR RALLGEIEGT
     CITRATSENV LHEYSTIAGI EESVHEILLN LKDIVLRSNL YGVRNASICV RGPKYITAQD
     IISPPSVEIV DTTQHIANLT EPINLCIELQ IKRDRGYRMK STNDSHDGSY PIDIVSMPVR
     NANHSIHSYG NGNEKQEILF IEIWTNGSLT PKEALYEASR NLIDLLIPFL HAEEEDMNFK
     ENENRWNLPP FSFQDKFTNF KKNKKGIPLT CIFIDQSELS SRTYNCLKRS NIHTLLDLLS
     HSQEDLMKME YFRTEDVKQI LSTVQKHFAI NLLNKKL