ID   A0A0H3V898_9ORYZ        Unreviewed;       337 AA.
AC   A0A0H3V898;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-SEP-2017, entry version 12.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE            Short=PEP {ECO:0000256|HAMAP-Rule:MF_00059};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00059};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE            Short=RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
GN   Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059,
GN   ECO:0000313|EMBL:AJP34391.1};
OS   Oryza officinalis.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AJP34391.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4535 {ECO:0000313|EMBL:AJP34391.1};
RN   [1] {ECO:0000313|EMBL:AGY93924.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pilkington S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AJP34391.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26355750; DOI=10.1038/srep13957;
RA   Wambugu P.W., Brozynska M., Furtado A., Waters D.L., Henry R.J.;
RT   "Relationships of wild and domesticated rices (Oryza AA genome
RT   species) based upon whole chloroplast genome sequences.";
RL   Sci. Rep. 5:13957-13957(2015).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1). {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core
CC       is composed of four subunits: alpha, beta, beta', and beta''. When
CC       a (nuclear-encoded) sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_00059}.
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and
CC       basal transcription, whereas the C-terminal domain is involved in
CC       interaction with transcriptional regulators and with upstream
CC       promoter elements. {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00059}.
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DR   EMBL; KF359910; AGY93924.1; -; Genomic_DNA.
DR   EMBL; KM881643; AJP34391.1; -; Genomic_DNA.
DR   RefSeq; YP_009155820.1; NC_027463.1.
DR   GeneID; 25016145; -.
DR   GO; GO:0009507; C:chloroplast; 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   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; IPR009025; RBP11-like_dimer.
DR   InterPro; IPR011260; RNAP_asu_C.
DR   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF03118; RNA_pol_A_CTD; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   ProDom; PD001179; RNAP_asu_C; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF55257; SSF55257; 2.
DR   SUPFAM; SSF56553; SSF56553; 1.
DR   TIGRFAMs; TIGR02027; rpoA; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:AJP34391.1};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Plastid {ECO:0000313|EMBL:AJP34391.1};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   DOMAIN       29    232       RPOLD. {ECO:0000259|SMART:SM00662}.
FT   REGION        1    232       Alpha N-terminal domain (alpha-NTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   REGION      251    337       Alpha C-terminal domain (alpha-CTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
SQ   SEQUENCE   337 AA;  38696 MW;  E2E33C2EEA3527CD CRC64;
     MVREEVAGST QTLQWKCVES RVDSKRLYYG RFILSPLRKG QADTVGIALR RALLGETEGT
     CITHAKFGSV PHEYSTIAGI EESVQEILLN LKEIVLRSNL YGVRNASICV KGPRYITAQD
     IILPPSVEIV DTAQPIANLT EPTDFRIELR IKRDRGYHTE VRKNTQDGSY PIDAVSMPVR
     NVNYSIFSCG NGNAKYEILF LEIWTNGSLT PKEALYEASR NLIDLFLPFL HTEEEGTRFQ
     ENKNRFTSPL LSFQKRLTNL KKNKKRIPLN CIFIDQLELP SRTYNCLKRA NIHTLLDLLS
     KTEEDLMRID SFRMQDGKQI WDTLEKHLPM DLPKNKF
//