ID   A0A8F2YHI8_9ROSA        Unreviewed;       326 AA.
AC   A0A8F2YHI8;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   25-MAY-2022, entry version 2.
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:QWX21092.1};
OS   Prunus mandshurica.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:QWX21092.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=122122 {ECO:0000313|EMBL:QWX21092.1};
RN   [1] {ECO:0000313|EMBL:QWX21092.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yi M.;
RT   "The complete chloroplast genome of Prunus mandshurica.";
RL   Submitted (FEB-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; MW599985; QWX21092.1; -; Genomic_DNA.
DR   Gene3D; 2.170.120.12; -; 1.
DR   Gene3D; 3.30.1360.10; -; 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   PANTHER; PTHR32108; PTHR32108; 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; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
DR   TIGRFAMs; TIGR02027; rpoA; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:QWX21092.1};
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};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:QWX21092.1};
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="RPOLD"
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;  37510 MW;  4A9F939DED525A43 CRC64;
     MVREKVTVST RTLQWKCVES RADSKRLYYG RFILAPLMKG QADTIGIAMR RALLGEIEGT
     CITRAKSEKI PHEYSTIIGI QESVHEILMN LKEIVLRSNL YGTSNASICI KGPGYVTAQD
     IILPPSVEIV DNTQHIANLT EPINLCIELQ IERNRGYRIK TPNNFQDGSY PIDAVFMPVR
     NANHSIHSYV NGNEKQEILF LEIWTNGSLT PKEALHDASR NLIDLFIPFL HAEEENLQLE
     NNQHKVTLPL FTFHGRLAKQ RKNKKEIALQ YIFIDQSELF PRVYNCLKRS NIHTLLDLLN
     NSQEDLMKIK HFRIEDVKHI LNILEI
//