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Database: UniProt
Entry: RPOA_DRIGR
LinkDB: RPOA_DRIGR
Original site: RPOA_DRIGR 
ID   RPOA_DRIGR              Reviewed;         339 AA.
AC   Q06GW5;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   Drimys granadensis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Canellales; Winteraceae; Drimys.
OX   NCBI_TaxID=224735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17020608; DOI=10.1186/1471-2148-6-77;
RA   Cai Z., Penaflor C., Kuehl J.V., Leebens-Mack J., Carlson J.E.,
RA   dePamphilis C.W., Boore J.L., Jansen R.K.;
RT   "Complete plastid genome sequences of Drimys, Liriodendron, and Piper:
RT   implications for the phylogenetic relationships of magnoliids.";
RL   BMC Evol. Biol. 6:77-77(2006).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|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: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; DQ887676; ABH88328.1; -; Genomic_DNA.
DR   RefSeq; YP_784418.1; NC_008456.1.
DR   AlphaFoldDB; Q06GW5; -.
DR   SMR; Q06GW5; -.
DR   GeneID; 4363604; -.
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; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..339
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000275688"
FT   REGION          1..235
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          267..339
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   339 AA;  38650 MW;  9BA390FE191D27AA CRC64;
     MVREEVAVST RTLQWKCVES RTDSKRLSYG RFILSPLMKG QADMIGIAMR RALLGEIEGT
     CITRAKSDKI PHEYSTIVGI EESVHQILMN LKEIVLRSNL YGTCDASIFV RGPRCVTAQD
     IISPPSVKMV DTTQHIASLT EPIDLCIGLQ IERDRGYRMK TPNNDQDGSY PIPIEAVSMP
     VRNANHSIHS YGNGNEKQEI LFLEIWTNGS LTPKEALHEA SHNLIDLFIP FLHGEEEDIN
     LEDSLNRGTL PFFTFQDKLA NLRKNKKAIA LECIFIDQSE LPPRTYNCLK RSNIHTLLDL
     LSNSQEDLMR IEHLRIEDVK RILDILQKHF TIDLPKNKF
//
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