ID D3WC13_9MAGN Unreviewed; 337 AA.
AC D3WC13;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
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:ADD31217.1};
GN ORFNames=MecuCp054 {ECO:0000313|EMBL:AMD08390.1};
OS Meliosma aff. cuneifolia Moore 333.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADD31217.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Sabiaceae; Meliosma.
OX NCBI_TaxID=723415 {ECO:0000313|EMBL:ADD31217.1};
RN [1] {ECO:0000313|EMBL:ADD31217.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20176954; DOI=10.1073/pnas.0907801107;
RA Moore M.J., Soltis P.S., Bell C.D., Burleigh J.G., Soltis D.E.;
RT "Phylogenetic analysis of 83 plastid genes further resolves the early
RT diversification of eudicots.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4623-4628(2010).
RN [2] {ECO:0000313|EMBL:AMD08390.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26724406;
RA Sun Y., Moore M.J., Zhang S., Soltis P.S., Soltis D.E., Zhao T., Meng A.,
RA Li X., Li J., Wang H.;
RT "Phylogenomic and structural analyses of 18 complete plastomes across
RT nearly all families of early-diverging eudicots, including an angiosperm-
RT wide analysis of IR gene content evolution.";
RL Mol. Phylogenet. Evol. 96:93-101(2015).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|ARBA:ARBA00004026, ECO:0000256|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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|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: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 basal
CC transcription, whereas the C-terminal domain is involved in interaction
CC with transcriptional regulators and with upstream promoter elements.
CC {ECO:0000256|HAMAP-Rule:MF_00059}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000256|ARBA:ARBA00007123, ECO:0000256|HAMAP-Rule:MF_00059}.
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DR EMBL; GQ997523; ADD31217.1; -; Genomic_DNA.
DR EMBL; KU204901; AMD08390.1; -; Genomic_DNA.
DR RefSeq; YP_009234672.1; NC_029430.1.
DR AlphaFoldDB; D3WC13; -.
DR GeneID; 26895203; -.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd06928; RNAP_alpha_NTD; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1.
DR Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 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 NCBIfam; TIGR02027; rpoA; 1.
DR PANTHER; PTHR32108; DNA-DIRECTED RNA POLYMERASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32108:SF0; DNA-DIRECTED RNA POLYMERASE SUBUNIT ALPHA; 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; SSF47789; C-terminal domain of RNA polymerase alpha subunit; 1.
DR SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1.
DR SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:ADD31217.1};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00059};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00059}; Plastid {ECO:0000313|EMBL:ADD31217.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00059}.
FT DOMAIN 29..232
FT /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT /evidence="ECO:0000259|SMART:SM00662"
FT REGION 1..232
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
FT REGION 260..337
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ SEQUENCE 337 AA; 38740 MW; EB9BC7C181169495 CRC64;
MVREEVAVST RTLQWKCVES RADSKRLYYG RFIMSPLMKG QADTIGIAMR RALLGEIEGT
CITRAKSETI PHEYSTIVGI EESVHEILMN LKEIVLRSNL YGTRDASICV RGPGYVTAQD
IISPSSVEIV DTTQHIASLT EPINLCIGLQ IERNHGYRMK TPKNSQDGSY PIDAVFMPVR
NANHSIHSYG NGNEKQEILF LEIWTNGSLT PKEALHEASR NLIDLFIPFL HTEEEDIIIE
DNQNRFTVPF FTFHDRLAKL RKNKKEIALK FIFIDQSELP PRTYNCLKRS NIHTLLDLLN
KSQEDLMRIE HFRIEDVKHI LGILQKHFEI NLPKNKL
//
