ID W5VNT7_9POAL Unreviewed; 339 AA.
AC W5VNT7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:AHH83977.1};
OS Paspalum candidum.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AHH83977.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Paspaleae; Paspalinae; Paspalum.
OX NCBI_TaxID=1424518 {ECO:0000313|EMBL:AHH83977.1};
RN [1] {ECO:0000313|EMBL:AHH83977.1}
RP NUCLEOTIDE SEQUENCE.
RA Scataglini M.A., Zuloaga F.O., Giussani L.M., Denham S.S., Morrone O.;
RT "Phylogeny of New World Paspalum (Poaceae, Panicoideae, Paspaleae) based on
RT plastid and nuclear markers.";
RL Plant Syst. Evol. 300:1051-1070(2014).
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
CC {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|HAMAP-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; KF810548; AHH83977.1; -; Genomic_DNA.
DR AlphaFoldDB; W5VNT7; -.
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:SF9; 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:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:AHH83977.1};
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:AHH83977.1};
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="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT /evidence="ECO:0000259|SMART:SM00662"
FT REGION 1..232
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
FT REGION 246..339
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ SEQUENCE 339 AA; 39128 MW; 509BEAF7CF3103CC CRC64;
MVREEVTGST QTLEWKCVES RVDSKRLYYG RFILSPLRKG QADTVGIALR RALLGEIEGT
CITRAKFWNV PHEYSTIVGI EESIQEILLN LKEIVLRSNL YGVRDASICV KGPRYITAQD
IILPPSVEIV DTTQPIANLR ESIDFCIELQ IKRDRGYHTE LRKNSQDGSY PIDAVSMPVR
NVNYSIFSCG NGNEKHEILF LEIWTNGSLT PKEALYEASR NLIDLFLPFL HAEEERASFE
ENKNRFSPPL LTFQKRFTNL KKNKKGIPLN CIFIDQLELP SRTYNCLKRA NIHTLLDLLS
KTEEDLMRID SFRMEDGKLI WDTLEKHLTM DLPKNKFLL
//
