RPOC2_ZYGCR
ID RPOC2_ZYGCR Reviewed; 1095 AA.
AC Q32RG2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 Zygnema circumcarinatum (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC Zygnematales; Zygnemataceae; Zygnema.
OX NCBI_TaxID=35869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16236178; DOI=10.1186/1741-7007-3-22;
RA Turmel M., Otis C., Lemieux C.;
RT "The complete chloroplast DNA sequences of the charophycean green algae
RT Staurastrum and Zygnema reveal that the chloroplast genome underwent
RT extensive changes during the evolution of the Zygnematales.";
RL BMC Biol. 3:22-22(2005).
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; AY958086; AAX45864.1; -; Genomic_DNA.
DR RefSeq; YP_636564.1; NC_008117.1.
DR AlphaFoldDB; Q32RG2; -.
DR PRIDE; Q32RG2; -.
DR GeneID; 4108184; -.
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; 3.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
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..1095
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000277206"
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 1095 AA; 123770 MW; 3AAEAA876613ECA8 CRC64;
MAELKNRIFY NQVMDKSAIK QLIIRLVACL GRVCTAHILD QLKTLGFQYS TQTGISLGID
DLLASPLKNW ILQDAENEAN VSQEYCRHGY IHAVERLRQI VETWHTTSEF LKREMTVSFN
ILDGFNPVHM MSFSGARGNV SQVHQLVGMR GLISDPQGNI IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAIRTADAG YLTRRLVEVA QHVVIRNVDC NTYEGIILRS IRTRQGNAYL
TQENRIIGRV LARPLYFGKR CIAVRNQDIG PDLAAKLSII SPQAILVRSP ITCKTTDWVC
QLCYGWGVNQ GKMVSLGEAI GVVAGQSIGE PGTQLTLRTF HTGGVFTGDI ANHLRAPFNG
IAHFETHNCK PTRNRHGRLV WKCLQDLTIT VIGQGKKHSL NVPSQSLLLI NNNQYVESKQ
VIAEVRASIA PIKEKVQRNI YSYLQGEVVH TRSALRLSNA FSGTILLIHH NPNTGHLWIW
SGKLYQLSGQ QASSIYTSED FIQTNITVAN KRYLKFDTHK ISNKKVLKSV LIGKFTRFKQ
VKSIQTGTVR SVLIQKPDTL RMVVLSSVDQ LEITMHKTPY IMEPLLTQKI SNNILNLTSY
PKSSTLISKQ KNTVSSFASI HIKRPTIGFQ FQLPIVPKIR CYSLGLLGKL QRPLQYNLVL
SSPTQPIFID RYYNTFTNWC YLNEHGNSYN LYGLQMIVLD KKLYNNNSIS GLFNTYRNIP
KIGQLICKGT FVQQTTQLSE SGKIVSIFKH KIVLRLSQPY LLAPGTFIHP DCYDVINRGD
IVITMMYEQL RTTDIIQGLP KAEQLLEARS FNEVVLKLEN DFVMLTERIA RQLRSLSRSY
MLSTKESTKH SQIDLVNRIQ TVYLSQGVRI VDKHIEIIVR QMSSKVMLVE NGDPLAVSSG
GLICLPLPPI GSFLPENWIE IPLSYVIDNH TFLPRELVEL TRAQKINYVI QNPVAYKPVL
LGITKASLNT NSFISEASFQ QTARVLSKSA IKNRVDWIRG LQENVLFGRM IPAGTGCREI
SSQLQYGNIF QKKWAQHTKW KLFVNSFGLN LSCLQIYLHF QAYCLESTNE QPQSNLHVHN
SRIFPFTTIC SILKS
