RPOA_MAIZE
ID RPOA_MAIZE Reviewed; 339 AA.
AC P09562;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 145.
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 Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Inrakorn;
RX PubMed=3399379; DOI=10.1093/nar/16.13.5741;
RA Ruf M., Koessel H.;
RT "Structure and expression of the gene coding for the alpha-subunit of DNA-
RT dependent RNA polymerase from the chloroplast genome of Zea mays.";
RL Nucleic Acids Res. 16:5741-5754(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [3]
RP PROTEIN SEQUENCE OF 1-18.
RX PubMed=2304916; DOI=10.1073/pnas.87.4.1531;
RA Hu J., Bogorad L.;
RT "Maize chloroplast RNA polymerase: the 180-, 120-, and 38-kilodalton
RT polypeptides are encoded in chloroplast genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1531-1535(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX PubMed=3149198;
RA Markmann-Mulisch U., Subramanian A.R.;
RT "Nucleotide sequence of maize chloroplast rpS11 with conserved amino acid
RT sequence between eukaryotes, bacteria and plastids.";
RL Biochem. Int. 17:655-664(1988).
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|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; X07810; CAA30670.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60317.1; -; Genomic_DNA.
DR EMBL; M35831; AAA84495.1; -; Genomic_DNA.
DR PIR; S00977; RNZMA.
DR PIR; S58583; S58583.
DR RefSeq; NP_043055.1; NC_001666.2.
DR AlphaFoldDB; P09562; -.
DR SMR; P09562; -.
DR STRING; 4577.GRMZM5G879235_P01; -.
DR PaxDb; P09562; -.
DR PRIDE; P09562; -.
DR GeneID; 845224; -.
DR KEGG; zma:845224; -.
DR MaizeGDB; 67212; -.
DR eggNOG; ENOG502QRS7; Eukaryota.
DR HOGENOM; CLU_053084_2_0_1; -.
DR OMA; LMKFRNF; -.
DR OrthoDB; 990306at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR Genevisible; P09562; ZM.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase.
FT CHAIN 1..339
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175468"
FT REGION 1..233
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 264..339
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT CONFLICT 130
FT /note="V -> D (in Ref. 1; CAA30670)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="S -> K (in Ref. 1; CAA30670)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..215
FT /note="AL -> GGI (in Ref. 1; CAA30670)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..294
FT /note="HT -> PSA (in Ref. 1; CAA30670)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="S -> V (in Ref. 1; CAA30670)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..308
FT /note="MQ -> IK (in Ref. 1; CAA30670)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="R -> G (in Ref. 1; CAA30670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 38947 MW; EA46E76F92ECA20D CRC64;
MVREEITGST QTLEWKCVES RVDSKRLYYG RFILSPLRKG QADTVGIALR RALLGEIEGT
CITRAKFGNV PHEYSTIVGI EESIQEILLN LKEIVLRSNL YGVRDASICV KGPRYITAQD
IILPPSVEIV DTTQPIANLR EPVDFCIELQ IKRDRAYHTE LRKNSQDGSY PIDAVFMPVR
NVNYSIFSCG NGNEKHEILF LEIWTNGSLT PKEALYEASR NLIDLFLPFL HTEEEGTSFE
ENKNRLTPPL LTFQKRFTNL KKNKKGIPLN CIFIDQLELP SRTYNCLKRA NIHTLLDLLS
KTEEDLMQIN SFRMEDGKLI WDTLEKHLPI DLPKNKFSL
