ID   RPOA_PHYPA              Reviewed;         450 AA.
AC   P60315; A9T5L6;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha, chloroplastic;
DE            EC=2.7.7.6;
DE   AltName: Full=Plastid-encoded RNA polymerase subunit alpha;
DE            Short=PEP;
DE            Short=RNA polymerase subunit alpha;
DE   Flags: Precursor;
GN   Name=rpoA; ORFNames=PHYPADRAFT_168194;
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBCELLULAR LOCATION.
RC   TISSUE=Protonema;
RX   PubMed=15002671; DOI=10.1078/0176-1617-01220;
RA   Miyata Y., Sugita M.;
RT   "Tissue- and stage-specific RNA editing of rps14 transcripts in moss
RT   (Physcomitrella patens) chloroplasts.";
RL   J. Plant Physiol. 161:113-115(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
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;
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:15002671}.
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:0000250}.
CC   -!- MISCELLANEOUS: Unlike most plants, the gene for this protein is encoded
CC       in the nucleus, thus the protein is synthesized as a precursor and
CC       imported into the chloroplast.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000305}.
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DR   EMBL; AB110071; BAC85012.1; -; Genomic_DNA.
DR   EMBL; AB110072; BAC85013.1; -; mRNA.
DR   EMBL; DS545058; EDQ61285.1; -; Genomic_DNA.
DR   RefSeq; XP_001773937.1; XM_001773885.1.
DR   AlphaFoldDB; P60315; -.
DR   SMR; P60315; -.
DR   STRING; 3218.PP1S169_65V6.1; -.
DR   EnsemblPlants; Pp3c5_15590V3.1; Pp3c5_15590V3.1; Pp3c5_15590.
DR   EnsemblPlants; Pp3c5_15590V3.2; Pp3c5_15590V3.2; Pp3c5_15590.
DR   Gramene; Pp3c5_15590V3.1; Pp3c5_15590V3.1; Pp3c5_15590.
DR   Gramene; Pp3c5_15590V3.2; Pp3c5_15590V3.2; Pp3c5_15590.
DR   eggNOG; ENOG502QRS7; Eukaryota.
DR   HOGENOM; CLU_608895_0_0_1; -.
DR   InParanoid; P60315; -.
DR   OMA; LMKFRNF; -.
DR   OrthoDB; 990306at2759; -.
DR   Proteomes; UP000006727; Chromosome 5.
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:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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   Reference proteome; Transcription; Transferase; Transit peptide.
FT   TRANSIT         1..77
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           78..450
FT                   /note="DNA-directed RNA polymerase subunit alpha,
FT                   chloroplastic"
FT                   /id="PRO_0000031057"
FT   REGION          78..346
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000250"
FT   REGION          374..450
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  49469 MW;  1F8D7648398F3937 CRC64;
     MAAVMSAQAM ADAVRVVRAS ISELGKSAKK SDAFSARDLK SRSGFTESVD RLGLVNLQVQ
     ARKKRVRGLR LVPTRVVSAI EGSNSTTADA PVDEDVLAWT KAYRAENSTA ITRDETLKSN
     AQSALQWKCV ETQVEGERLH YGRFAVSPFR SGQANTVGVS MQKALLGEVE GAAVSCATFK
     NVKSEYAAMK GVEETPMDIL VNLKELVIRS DSDEPQKAII SAIGPGPVTA GDIVLPPSLE
     VTDPTQHIAY LTKEVSLDIE LDVEKGCGYR MGDHTKSGDG RFYIDSVFMP VRNANYSVHS
     YESEPDVTQE ILFLEIWTNG SITPEEALHE AARCLIDLFL PFLHPKKKEV TNSATKMHKS
     FTMSQFNSSA EMSAKEVDLR HVYVDQLRIP SKAYNSLKRA NINTVSDLLD YTQDDLLSIP
     NFGRKSVDDI LEALQAQFSI DLPENNPLCN