ID M9YU34_9ASPA Unreviewed; 339 AA.
AC M9YU34;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:AGK25262.1};
OS Cymbidium aloifolium.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AGK25262.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Cymbidieae; Cymbidiinae; Cymbidium.
OX NCBI_TaxID=112603 {ECO:0000313|EMBL:AGK25262.1};
RN [1] {ECO:0000313|EMBL:AGK25262.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23597078;
RA Yang J.B., Tang M., Li H.T., Zhang Z.R., Li D.Z.;
RT "Complete chloroplast genome of the genus Cymbidium: lights into the
RT species identification, phylogenetic implications and population genetic
RT analyses.";
RL BMC Evol. Biol. 13:84-84(2013).
RN [2] {ECO:0000313|EMBL:AGK25262.1}
RP NUCLEOTIDE SEQUENCE.
RA Yang J.-B., Tang M., Zhang Z.-R., Li H.-T., Li D.-Z.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QIA92529.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen J., Chen M.-K., Zheng Q.-D., Ma S.-H., Liu Z.-J., Ai Y.;
RT "Chloroplast characterization and phylogenetic relationship of Cymbidium
RT aloifolium (Orchidaceae).";
RL Mitochondrial DNA Part B Resour 5:478-479(2020).
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; KC876122; AGK25262.1; -; Genomic_DNA.
DR EMBL; MN641752; QIA92529.1; -; Genomic_DNA.
DR RefSeq; YP_008081604.1; NC_021429.1.
DR AlphaFoldDB; M9YU34; -.
DR GeneID; 15823227; -.
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:AGK25262.1};
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:AGK25262.1};
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 251..339
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ SEQUENCE 339 AA; 38965 MW; CE6B05591CC7E958 CRC64;
MVREEVAGST RKLKWKCVES RVDSKRLYYG RFVLSPLMKG QADTIGIAMR RALLGEIEGT
CITRATSENV LHEYSTIAGI EESVHEILIN LKEIVLKSNL YGVRDASICV RGPKYITAQD
IISPPSVQIV DTTQHIANLT EPIDLCIELQ IKRGRGYHMK STNESHEGSY PIDIVSMPVR
NANHSIHSYG NGNEKQEILF LEIWTNGSLT PKEALYEASR NLIDLLIPFL HAEEEYMNLE
ENENRWNLPF FSFQDRFTNL KKNKKGIPLT CIFIDQSELS SRTYNCLKRS NIHTLLDLLN
HSQEDLMKME YFRIEDIKQI LGTLQKHFAI NLPKKNFSF
//