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Database: UniProt
Entry: E3W0M5_PRUPE
LinkDB: E3W0M5_PRUPE
Original site: E3W0M5_PRUPE 
ID   E3W0M5_PRUPE            Unreviewed;       326 AA.
AC   E3W0M5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
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:ADO65007.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ADO65007.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ADO65007.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=20935065; DOI=10.1093/molbev/msq261;
RA   Jansen R.K., Saski C., Lee S.B., Hansen A.K., Daniell H.;
RT   "Complete plastid genome sequences of three Rosids (Castanea, Prunus,
RT   Theobroma): evidence for at least two independent transfers of rpl22 to the
RT   nucleus.";
RL   Mol. Biol. Evol. 28:835-847(2011).
RN   [2] {ECO:0000313|EMBL:AZZ71088.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Magdy M.;
RT   "Comparative Plastogeniomic analysis in Peach.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QQO80883.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xin L., Fei R.;
RL   Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:QYJ09200.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sharko F., Rastorguev S., Gladysheva-Azgari M., Tsygankova S.,
RA   Mitrofanova I., Boulygina E., Slobodova N., Nedoluzhko A.;
RT   "The complete chloroplast genome sequence of cultivated peach Prunus cv.
RT   Sovetskiy.";
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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; HQ336405; ADO65007.1; -; Genomic_DNA.
DR   EMBL; MH169125; AZZ71088.1; -; Genomic_DNA.
DR   EMBL; MH169126; AZZ71170.1; -; Genomic_DNA.
DR   EMBL; MW042696; QQO80883.1; -; Genomic_DNA.
DR   EMBL; MZ065355; QYJ09200.1; -; Genomic_DNA.
DR   RefSeq; YP_004021697.1; NC_014697.1.
DR   AlphaFoldDB; E3W0M5; -.
DR   STRING; 3760.E3W0M5; -.
DR   GeneID; 9978759; -.
DR   KEGG; pper:9978759; -.
DR   OrthoDB; 1200455at2759; -.
DR   Proteomes; UP000006882; Chloroplast.
DR   Proteomes; UP000829242; Chloroplast Pltd.
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:ADO65007.1};
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:ADO65007.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
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..234
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
FT   REGION          269..326
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   326 AA;  37579 MW;  ABDB2D860CEC41E3 CRC64;
     MVREKVTVST RTLQWKCVES RADSKRLYYG RFILAPLMKG QADTIGIAMR RALLGEIEGT
     CITRAKSEKI PHEYSTIIGI QESVHEILMN LKEIVLRSNL YGTRNASICI KGPGYVTAQD
     IILPPSVEIV DNTQHIANLT EPINLCIELQ IERNRGYRIK TPNNFQDGSY PIDAVFMPVR
     NANHSIHSYV NGNEKQEILF LEIWTNGSLT PKEALHDASR NLIDLFIPFL HAEEENLQLE
     NNQHKVTLPL FTFHGRLAKQ RKNKKEIALQ YIFIDQSELF PRVYNCLKRS NIHTLLDLLN
     NSQEDLMKIK HFRIEDVKHI LNILEI
//
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