RPOC2_ADICA
ID RPOC2_ADICA Reviewed; 1420 AA.
AC Q85FM9; Q9MW06;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS Adiantum capillus-veneris (Maidenhair fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT "Complete nucleotide sequence of the chloroplast genome from a
RT leptosporangiate fern, Adiantum capillus-veneris L.";
RL DNA Res. 10:59-65(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC TISSUE=Frond;
RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA Wolf P.G., Rowe C.A., Hasebe M.;
RT "High levels of RNA editing in a vascular plant chloroplast genome:
RT analysis of transcripts from the fern Adiantum capillus-veneris.";
RL Gene 339:89-97(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-317.
RX PubMed=10474899; DOI=10.1093/oxfordjournals.molbev.a026192;
RA Nishiyama T., Kato M.;
RT "Molecular phylogenetic analysis among bryophytes and tracheophytes based
RT on combined data of plastid coded genes and the 18S rRNA gene.";
RL Mol. Biol. Evol. 16:1027-1036(1999).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01324}.
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_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
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_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01324}.
CC -!- RNA EDITING: Modified_positions=39 {ECO:0000269|PubMed:15363849}, 57
CC {ECO:0000269|PubMed:15363849}, 78 {ECO:0000269|PubMed:15363849}, 182
CC {ECO:0000269|PubMed:15363849}, 300 {ECO:0000269|PubMed:15363849}, 339
CC {ECO:0000269|PubMed:15363849}, 659 {ECO:0000269|PubMed:15363849}, 768
CC {ECO:0000269|PubMed:15363849}, 1099 {ECO:0000269|PubMed:15363849}, 1253
CC {ECO:0000269|PubMed:15363849}; Note=The nonsense codon at position 78
CC is modified to a sense codon.;
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; AY178864; AAP29382.2; -; Genomic_DNA.
DR EMBL; AB013683; BAA83459.1; -; Genomic_DNA.
DR RefSeq; NP_848050.1; NC_004766.1.
DR AlphaFoldDB; Q85FM9; -.
DR PRIDE; Q85FM9; -.
DR GeneID; 807355; -.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; RNA editing; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1420
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067911"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1420 AA; 159869 MW; 69F9396F8389A90B CRC64;
MMDRNELPFC NKTIDRAAMK RLIGKLVVCF GIASTTNILD QVKVLGFQQA TEASISLGID
DLSAVPTRGW LVRDAEKQGY VSEGHYRCGS LHAIEKLRQS IEAWYATSEC LKREMSPSFK
MIDPLNPVHM MSVSGARGTI SQVHQLLGMR GLMADPRGQV IDLPIRRNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIAVRRRDC ETPRSLAFLT SNTGERRRGF
LGTMPHQGLV GRVLADHVYW DVRCIATRNQ DISDGLASNL MASSQPIHVR SPLTCKSIFW
ICQFCYGWSL AHCNLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG DIAEYVRIPF
NGLIKFDERL LHPTRTRHGH PAWMCRNDLP LFIGNSVGTQ NSLIPAQSLL MIRTGQYVES
QQVIAEVRAK EFPPKECIRK PIYPNSRGEI HWSKFVWHVR DSICNIARLV REASHIWILS
GSPSKFDGNS FFHKDQDRVR IKPHPIKRIR SHSEGIFEAQ ASASNCVDRR KGIQEFGTDS
KYFSNWSKRP RSNYILSNVW LERAELENSV SLLMERCQKN IKKLDFVSIN VQLNNGSDQD
HIFATYENFE YQTIVSGIIK YGTVEIKPVN PKRLQLDGGT GNKSSRPWCR VVRKGNFFLI
PEEVYLTHEP SSSILVTNNA IVKKGAQITN NIITKSGGLI RMRKRSRDAT TIRILPGYIY
NPEKQINISK RGNTLLAPGN RISDDIEVKN WIYLQPFTFR RKGKTFVLMT PVSEYNLSSD
SLAQVASRFD KPKTQRRAKA KTLSFICCKN GEKIEVINDV PTQLVRLCLI IEWQKYLHET
LPRKRNYFSL ISVKISYLFK TFLQVNPMVS PPTQRGVRVD EIFRTSTPLG KPSPPQLDLA
NSCCKSAVNC QGIIHLTLEP ATSFLILSPF NLSRNNSVTD TRDGGCGGEI GKYFYGSEDG
FFCIGENKKK ISLSSKCISE NYANPNVEEG WIKARRASSN LGQRKAEEVG LVGTLSPISC
SSIPHHLSLG GKNLSTRKGF VDYSIDKSEH QDFYLIDESK LLLKCPINFY VKKGFLDKPS
YLPTRVFSRE IMLISLGLLI SESRYLHRDR TCFQSGQVMA IHQDYSLVRT GKTFLATRGA
NPHKSSGDIL EEGDTLITLP YDRLKSGDIT QGLPKVEQLL ESRSIASISA GIGDLFEKWC
QNITKLIGNP WSHLLGAGRS MEHCQLILID QIRKVYESQG VRICDKHLEI IVRQLTSRVV
ASEDGVTNVF LPGELVELSQ AERINRVLKK SIFYEPIVLG MTRASLSTTS FLAEASFQET
TRVLAKAALR GRIDWLKGLK ENVVIGDSVP VGTGSPEIYC QLNINKEKES RLASGGSKKL
TKWETGSSLS GYHKKRDFNP SFFIRKELNR SFTRLHLDMW
