RPOA_TAKLE
ID RPOA_TAKLE Reviewed; 341 AA.
AC Q60F88; Q1HAE5; Q5EGG9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 78.
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};
OS Takakia lepidozioides (Moss).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Takakiophytina; Takakiopsida; Takakiales; Takakiaceae; Takakia.
OX NCBI_TaxID=37425;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sugita M., Sugiura C., Arikawa T., Higuchi M.;
RT "Molecular evidence of an rpoA gene in the basal moss chloroplast genomes:
RT rpoA is a useful molecular marker for phylogenetic analysis of mosses.";
RL Hikobia 14:171-175(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RX PubMed=16960353; DOI=10.1271/bbb.60204;
RA Sugita M., Miyata Y., Maruyama K., Sugiura C., Arikawa T., Higuchi M.;
RT "Extensive RNA editing in transcripts from the psbB operon and rpoA gene of
RT plastids from the enigmatic moss Takakia lepidozioides.";
RL Biosci. Biotechnol. Biochem. 70:2268-2274(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Goffinet B., Wickett N.J., Shaw J.A., Cox C.J.;
RT "Phylogenetic significance of the rpoA loss in the chloroplast genome of
RT mosses.";
RL Submitted (JAN-2005) 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 -!- 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 -!- RNA EDITING: Modified_positions=35 {ECO:0000269|PubMed:16960353}, 53
CC {ECO:0000269|PubMed:16960353}, 67 {ECO:0000269|PubMed:16960353}, 88
CC {ECO:0000269|PubMed:16960353}, 91 {ECO:0000269|PubMed:16960353}, 123
CC {ECO:0000269|PubMed:16960353}, 136 {ECO:0000269|PubMed:16960353}, 145
CC {ECO:0000269|PubMed:16960353}, 170 {ECO:0000269|PubMed:16960353}, 172
CC {ECO:0000269|PubMed:16960353}, 182 {ECO:0000269|PubMed:16960353}, 288
CC {ECO:0000269|PubMed:16960353}, 299 {ECO:0000269|PubMed:16960353}, 325
CC {ECO:0000269|PubMed:16960353};
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR EMBL; AB193121; BAD60944.2; -; Genomic_DNA.
DR EMBL; AB254140; BAE94567.1; -; mRNA.
DR EMBL; AY884000; AAW82426.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q60F88; -.
DR SMR; Q60F88; -.
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: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 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 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW RNA editing; Transcription; Transferase.
FT CHAIN 1..341
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175500"
FT REGION 1..233
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 265..341
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ SEQUENCE 341 AA; 38787 MW; A5CC3B800D243DD8 CRC64;
MIRDEIPISA QVLQWRCVES RVDSARLHYS RFAISPFRSG QASTVGIAMR RALLGEVEGT
CITCAEFKRV THEYSTILGI QESVHDVLIN LGEIVLRSDS YETQKAFISI LGPKKVTAQD
IILPPSVKII DTTQYIATVT KAIHLDIELK IEKDFGYRIE DPIKSADGNF PVDAVFMPIR
NVNYSVHSFE NGNETQEILF LEIWTNGSVT PKEALYEASR SLINLFIPFL HAEKKEFIYG
LKNTYESNMS YFSSPSLSAD IDEMTKGVTF KHIFIDQLEL PARAYNCLKR VNAHTISDLL
NYSQDDLMKI KNFGKKSVEQ VLEALQKRFS INLPKNKLHF H
