ID   A0A4P8JBL5_9LILI        Unreviewed;       342 AA.
AC   A0A4P8JBL5;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   16-OCT-2019, entry version 3.
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:QCP68187.1};
OS   Lanxangia paratsaoko.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:QCP68187.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Lanxangia.
OX   NCBI_TaxID=252857 {ECO:0000313|EMBL:QCP68187.1};
RN   [1] {ECO:0000313|EMBL:QCP68187.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gao Y., Li G., Zhang Y., Qian Z.;
RT   "Characterization of the complete chloroplast genome of Amomum para-
RT   tsaoko S. Q. Tong et Y. M. Xia(Zingiberaceae).";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00059};
CC   -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core
CC       is composed of four subunits: alpha, beta, beta', and beta''. When
CC       a (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
CC       basal transcription, whereas the C-terminal domain is involved in
CC       interaction with transcriptional regulators and with upstream
CC       promoter elements. {ECO:0000256|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_00059}.
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DR   EMBL; MH423780; QCP68187.1; -; Genomic_DNA.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
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   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:QCP68187.1};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Plastid {ECO:0000313|EMBL:QCP68187.1};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   DOMAIN       29    232       RPOLD. {ECO:0000259|SMART:SM00662}.
FT   REGION        1    240       Alpha N-terminal domain (alpha-NTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   REGION      269    342       Alpha C-terminal domain (alpha-CTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
SQ   SEQUENCE   342 AA;  39540 MW;  B795936F13D1FF51 CRC64;
     MVREEVVGST RTLQWRCVES RIDSNRLYYG RFILCPLMKG QADTIGIAMR RALLGEIEGT
     CITCAKSEKV PHEYSTIVGI EESVHEILLN LKEIVLRSNI HGVRDASICV KGPKYVTAQD
     IISPPFVEIV DTTQHIANLT EPIDLCIGLQ IRRDRGYRTK LTINSQDGSY PIDAVSMPVR
     NANHSIHSFG NGKEKEEILF LEIWTNGSLT PKEALYEASR NLIDLFIPFL HGEEEDINFK
     LKENKNRFTL PIFTFQDRLT NLKKNKKEIP LKCIFIDQSE LPYRTYNCLK RSNIHTLLEL
     LSKSQEDLMR IEYFRIEDVK EISDTLRKHF EIDLPKNKFS FF
//