ID RPOA_CUCSA Reviewed; 333 AA.
AC Q4VZK3; A5J1W6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 77.
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}; OrderedLocusNames=CsCp074;
OS Cucumis sativus (Cucumber).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekmibaekdadagi;
RX PubMed=16362300; DOI=10.1007/s00299-005-0097-y;
RA Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J.,
RA Choi D.-W., Liu J.R., Cho K.Y.;
RT "Complete sequence and organization of the cucumber (Cucumis sativus L. cv.
RT Baekmibaekdadagi) chloroplast genome.";
RL Plant Cell Rep. 25:334-340(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Borszczagowski;
RX PubMed=17607527; DOI=10.2478/s11658-007-0029-7;
RA Plader W.W., Yukawa Y., Sugiura M., Malepszy S.;
RT "The complete structure of the cucumber (Cucumis sativus L.) chloroplast
RT genome: its composition and comparative analysis.";
RL Cell. Mol. Biol. Lett. 12:584-594(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chipper, and cv. Gy14;
RX PubMed=17546086; DOI=10.1139/g07-003;
RA Chung S.-M., Gordon V.S., Staub J.E.;
RT "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies
RT differences between chilling-tolerant and -susceptible cucumber lines.";
RL Genome 50:215-225(2007).
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; DQ119058; AAZ94682.1; -; Genomic_DNA.
DR EMBL; AJ970307; CAJ00791.1; -; Genomic_DNA.
DR EMBL; DQ865975; ABI97448.1; -; Genomic_DNA.
DR EMBL; DQ865976; ABI98777.1; -; Genomic_DNA.
DR RefSeq; YP_247632.1; NC_007144.1.
DR AlphaFoldDB; Q4VZK3; -.
DR SMR; Q4VZK3; -.
DR GeneID; 3429301; -.
DR KEGG; csv:3429301; -.
DR eggNOG; KOG0408; Eukaryota.
DR OrthoDB; 1200455at2759; -.
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..333
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000225918"
FT REGION 1..233
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 269..333
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ SEQUENCE 333 AA; 38560 MW; A8733FA0570F95FB CRC64;
MVREKIRVST RTLKWKCVES RADSKRLYYG RFILSPLMKG QGDTIGIAMR KALLGEIEGT
CITRAKSEKI PHEYSTIVGI QESVHEILMN LKEIVLRSNL YGTRDASICV KGPGCVTAQD
IILPPSVEIV DNTQHIANLM EPINLCIELK IERNRGYHIQ TPNNFQDASY PMDAIFMPVR
NVNHSIHSYV NGNEKQEILF LEIWTNGSLT PKEALHEASR NLIDLFIPFL HAEEEKENFH
LKNNKKKVTL PLFTFHEKLA KLRKKKKEIA LKYIFIDQSE LPPRIYNCLK RCNIHTLFDL
LNNSPDELMK IKHFRIEDVK HILDILEMEK NFA
//
