RPOC2_ANTAG
ID RPOC2_ANTAG Reviewed; 1445 AA.
AC Q85C71;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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=42 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 49 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 66 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 94 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 111 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 113 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 137 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 138 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 139 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 142 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 144 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 156 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 157 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 195 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 197 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 204 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 224 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 277 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 327 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 328 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 341 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 347 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 356 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 432 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 608 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 621 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 665 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 673 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 679 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 794 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 831 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 922 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1179 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1201 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1206 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1259 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1260 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1293 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1311 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 1340 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 49,
CC 113, 137, 138, 156, 195, 224, 328, 356, 831, 922, 1201 and 1260 are
CC modified to sense codons.;
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; AB086179; BAC55328.1; -; Genomic_DNA.
DR EMBL; AB087420; BAC55419.1; -; mRNA.
DR RefSeq; NP_777392.1; NC_004543.1.
DR AlphaFoldDB; Q85C71; -.
DR GeneID; 2553425; -.
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; 2.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 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..1445
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067913"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1445 AA; 165855 MW; 35B3BEE41700283F CRC64;
MAESAKLLFY NKVIDGTAIK QFIGRLVAHF GITYTAHILD QLKTLGFQQA TYAATSLGID
DLLTAPSKGW LIQDAEHHSY TLEKHHRYGN VHAVEKLRQL IETWYATSEY LKQEMNPNFR
MTDPLNPVHM MSFSGARGSA SQVHQLVGMR GLVSDPQGQI IDLPIKSNFR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRKTDC NTFRGISLNS TEDKKKNLQI
FTQQKLVGRV LADNLYINAR CLAIRNQDIN TNLIEKLITL KTPLISIRSP LTCKSMLWIC
QLCYGWSLTH YGDLVELGEA VGIIAGQSIG EPGTQLTLRT FHTGGVFTGD IAEHVRTPFN
GTIEFDTDLV YPTRTRHGHP AWVCRTDLAV TIKSQNKIHN LIIPSQSLLL IQNNQYVESK
QLIAEVHAKV SPFKEKVQKY IYCNIEGEMH WSKRVRHASK YLHSNVHLIF NTGHLWILSG
SSHEDKTSSM FFKNQDQINT KFFISPRKIL FMKKTNQVNS KNLDPYLEKE METLNYSNLY
LGILNKSRNF VYPSIILHDY EVKRIYDEKK GENFLLLEER HGEKKTQIFR RFVLNIPKSG
ILENKDIFAI SNDPGYGIQS PGIIKYGTIK VNPIKGKGET FKNRETKILR LRPRYQVIEP
GNFFPIPEEV HILYESFPPI LVRNDSLIKK NTQITSDIRS QVGGLVRIRR KMNDSYEVKV
LPGRVYHPEE RRNISKQNDI LVPPGEEISN KFQSENWLYL EWITPPKEKP FIFIRPAIEF
IVPEETDLAE TFTLNSQKKQ EILKVKKIRY LLYEDGEEVE VTNKTGIQLI QTGLVLDWKE
DSSIKKVYAS LTEIETNGLS KKFLQISLIE HPIFEIEKKK NNVNLKYLFT NEINYSSHSF
NYENGLFNGY RGIIRISSNE NQEDKSLPIL SPFDFVQIFL SKNSEEYTPE MKDEGNFNLD
TNSIFYAKSF VKKFNQNSIT SSQNSSGTFI NKEFYNHNNI NQEFNSRKII RNFFLSIERN
FMEILLLRKL GLLGNSHSLP SPFQFSCWAN THNQPIINRY SILENLRDVF QVPKWYFFDE
NKKTHKLDLS KNSIYHLLTW SFSIALSYEE GAIHLVGLGQ FICENISISS KYQTISESGQ
IIAIHPEFLV VRLAKPSLAT GGATIHSHYG QIIKKGDVLI TLVYERLKSG DIIQGLPKVE
QLLEARPINS TSINLENGFE NWNRDMTKSL GSLWGFLLSA KTTMNQSQIN LVDQIQEVYQ
SQGVYISDKH IEIVVRQMTS KVLTLEDGMA NGFLPGELIE SSRAQRMNRV LEESVLYKPI
LLGITKASLN TQSFISEASF QETTRVLAKA ALRGRIDWLK GLKENVIFGG VISAGTGCQE
VVWQVILEKR KETYSKRKKN KLFSGRVRDV FSYYQRILFF PTMKIIHKTL KKPLSEINLD
PNYRK
