RPOC2_CHLAT
ID RPOC2_CHLAT Reviewed; 1396 AA.
AC Q19VA0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 56.
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 Chlorokybus atmophyticus (Soil alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; Chlorokybales;
OC Chlorokybaceae; Chlorokybus.
OX NCBI_TaxID=3144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.80;
RX PubMed=17222354; DOI=10.1186/1741-7007-5-2;
RA Lemieux C., Otis C., Turmel M.;
RT "A clade uniting the green algae Mesostigma viride and Chlorokybus
RT atmophyticus represents the deepest branch of the Streptophyta in
RT chloroplast genome-based phylogenies.";
RL BMC Biol. 5:2-2(2007).
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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ422812; ABD62242.2; -; Genomic_DNA.
DR RefSeq; YP_001019102.1; NC_008822.1.
DR AlphaFoldDB; Q19VA0; -.
DR SMR; Q19VA0; -.
DR GeneID; 4783312; -.
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; 4.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1396
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353553"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 297
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"
SQ SEQUENCE 1396 AA; 157831 MW; 0A388E717EE79269 CRC64;
MNLFFCNRTI EKGEIRRFIA WFIFHHGTAR TTQMVERLKV LGFRHATKAG VSLSVDDLKI
PPSKRWLLED AEEEIQFTER QYQKGKITAV ERFQKVIDTW HSTSETLKDE VVQHFLQTDT
LNPVYMMAFS GARGNISQVR QLVGMRGLMS DPQGQIIDLP IRSNFREGLT VTEYVISCYG
ARKGLVDTAL RTADSGYLTR RLVDVAQHVI IRETDCGTLS GISLMPMKDQ DKIIFSLEER
LIGRVLAESI YSIQEKKYVA RRNQDISANL ATQIVRVKKN NIFVRSPLTC KANRSVCQLC
YGWSLAHGSL VDLGEAVGII AAQSIGEPGT QLTMRTFHTG GVFTGNVAKQ IRSPIDGIVH
FPTILQNQMT TTRTRHGEEA LLTNIDVEIL IQTNAEKSVQ LKLPQYTVLF IKDGQFVRSK
QLIAEVSSKN KKLQSVEIAS KYVTSDLYGE VYFDNLVLQE RKGGYGNRMN RVGQHGGLLW
VLSGRIYELG IELPIMFQAG DLVLFGCILA EQDIATTFGG ILKIDFFEKD SFARENIDSK
RIHLTDSISS YNKKPINATT RAAENSSLND KNVDIKIFNS LFTLQDVKVY HFDSFRIKED
FIKEKVKDYY LLKSLNPAIS KKKRFENTSE KKKTHIDSTL KRETNDQGVS YNGHAAVATT
NEIKDYLFSN SCNPWNLELS SDLKVKRDQV IGKLVTEAYL TSTGGIVKYS GILVERYDPI
KKGYKVLKGG ILLWIPEETH KVKRSTVRLF IEDGDYIPKG TKLLPNVVSK HAGLVNISQT
NDLYDEITIK PGEIYTPKDG KQALEKHQCF VQVGEEIVDG LIAKELVYLE VINKPVITNR
FVDKKNDVVR ETQEDFIKGS ENKEVVLLIR PVVQYLVPDN RDVPIPPGIH NIRNNINLKA
IQFIRYQDGE TVSSFEPVEL VQVSLAIDLK ESGQKTAAIE LIPIQDNDMV TTSSKHINKS
KKPYDKNLSV KEKNRNRVTQ ILSLDKGKLF EFQIGLFESL FIRSNEYIES NSQKNICRLL
AKNGQYVVPE DSIAIKEVIG KYSGEVRQSE KASEEERSFL IMNESDHITL SLKDSSKNLK
LGDLLHKEDF IAPGVRLPQS GQIIQLQSDQ VTIRIARPYL VSSEAVLHVN HGDLVKSGDT
LVMLIFEQAK TGDIVQGLPR IEELLEARRT KGLKPLPNNL HDRLESLFFQ CRKKYGNHRA
ARKSLEEIQL FLVNEIQSVY KSQGVSISDK HIEVIVRQMT SKVVIEEGGD TTLLPGELIE
LHRIENINKN VSIHAQYKPV VLGITKASLN TESFISAASF QETTRVLTKA AIEGKTDWLK
GLKENVIIGR LIPAGTGFNE HERISSNMSN IYNDLGYVIN PIYEKEKNKV EEADFEDIIF
EDNRTPKGFR LKDEAS
