ID M5DDG3_CHOCR Unreviewed; 310 AA.
AC M5DDG3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE Short=RNAP subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00059};
DE AltName: Full=RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
DE AltName: Full=Transcriptase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059};
GN Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059,
GN ECO:0000313|EMBL:CCP38114.1};
GN ORFNames=CHC_490 {ECO:0000313|EMBL:CCP38114.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OG Plastid {ECO:0000313|EMBL:CCP38114.1}.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:CCP38114.1, ECO:0000313|Proteomes:UP000012073};
RN [1] {ECO:0000313|EMBL:CCP38114.1, ECO:0000313|Proteomes:UP000012073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX PubMed=23536846; DOI=10.1371/journal.pone.0059001;
RA Janouskovec J., Liu S.-L., Martone P.T., Carre W., Leblanc C., Collen J.,
RA Keeling P.J.;
RT "Evolution of red algal plastid genomes: ancient architectures, introns,
RT horizontal gene transfer, and taxonomic utility of plastid markers.";
RL PLoS ONE 8:e59001-e59001(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {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: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
CC beta, 1 beta' and 1 omega subunit. When a sigma factor is associated
CC with the core the holoenzyme is formed, which can initiate
CC transcription. {ECO:0000256|HAMAP-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; HF562234; CCP38114.1; -; Genomic_DNA.
DR RefSeq; YP_007627367.1; NC_020795.1.
DR AlphaFoldDB; M5DDG3; -.
DR STRING; 2769.M5DDG3; -.
DR EnsemblPlants; CCP38114; CCP38114; CHC_490.
DR GeneID; 14971115; -.
DR Gramene; CCP38114; CCP38114; CHC_490.
DR KEGG; ccp:CHC_490; -.
DR OMA; PIKNVKY; -.
DR OrthoDB; 162at2759; -.
DR PhylomeDB; M5DDG3; -.
DR Proteomes; UP000012073; Plastid.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; 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 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 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:CCP38114.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012073};
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 20..226
FT /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT /evidence="ECO:0000259|SMART:SM00662"
FT REGION 1..234
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
FT REGION 241..310
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ SEQUENCE 310 AA; 34878 MW; 136E6C660EBB38DC CRC64;
MTHFELECIE SKTEGAREQY GHFILEPLKQ GQGITVGNSL RRTILSDLQG TAIVAVRIAG
INHEFSTITG VREDVLEILL NLKEVVLKSY TKEPQIGRIR IQGPAIVTAG LFDVPTEIQI
IDPKQYIATI CNNTIFEMEF RIEQGSGYRI VDKGIDHQSI DFLQVDAVFM PAKKFNYVVE
EKRISSTLVQ EKLSLEIWTN GSLSPQEAIS EGANVLTNLF HPLTNINFQP AVNNQIQEEQ
AINQVLIEEL QLSVRAYNCL KRAQIHSISD LLDYSQEELL EIKNFGQKSA EEVIDALQKK
LGISLPKEKS
//
