RPOC2_NEPOL
ID RPOC2_NEPOL Reviewed; 1463 AA.
AC Q9TL04;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Nephroselmis olivacea (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX NCBI_TaxID=31312;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-484 / S-N-5-8;
RX PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA Turmel M., Otis C., Lemieux C.;
RT "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT olivacea: insights into the architecture of ancestral chloroplast
RT genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; AF137379; AAD54812.1; -; Genomic_DNA.
DR RefSeq; NP_050841.1; NC_000927.1.
DR AlphaFoldDB; Q9TL04; -.
DR SMR; Q9TL04; -.
DR PRIDE; Q9TL04; -.
DR GeneID; 802013; -.
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; 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..1463
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067932"
FT REGION 836..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1463 AA; 165153 MW; FCA0921315859E10 CRC64;
MNTQEKHQFE PVLPQAHDDP TLSKPPIFFN RTADKGMIKR LIAWFLVHYG LADTVSMIED
LKQVGFQYAT RAGISLGIED LRIPPTKPRL LQEAHREINR MEFRYQQGYV SLVERFQKVI
DTWNGTSELL KDDVVENFLA TDPLNPVYMM AFSGARGNLS QVRQLVGMRG LMSNPQGEII
DLPIRSNFRE GLTVTEYIIS CYGARKGLVD TALRTANSGY LTRRLVDVAQ DIVIRMTSCS
PSAYPLISFT KSGKEVVYPL EERLLGRVLA IGAFNQEGEL ISGPDTAISQ EIAVQLMDCD
PKEILVRSVL LCKSKRGLCR LCYGWNLGTG TIVSIGEAVG IIAAQSIGEP GTQLTMRTFH
TGGVFAGGVT NEIRAPHAGL VHYPRPIHPK WVRTRHGQFG ILISEKIEII FEHESKKTIQ
VFDAGTVLTI HEGEKVHTNQ LIGEIPAHGT LVTGWRSLKS GVDGEVRFDE LELLKQRPRS
DRTSPVRLDP RVCNKAHLWI LQGHVNTFEM PIQLVANIGD KVEKDSIVST TKQVVSEEGR
IIYRYDEKRG KEQTIITHAF GSVQFDGVDA WLPTKSQGIK QSIRTTGGKL SISSQGMTLS
ATKIKQEGIG SFDWPALAEP SIEEDEELEE AYKKTKDPII QPTPYPLQYC VLPEQKYVIQ
AQEGWIISVL GGQSVGASQS LATYVDSQWE VEQGQLSIRS IEYRVHDQSW IQVITPSLVE
IESGRGSYHL MAKAGWIIPI STKIRCKDYR LISGSILLGK WSLPISRFAV EQAASYPAIL
IRPIHTYPVY PTTIWDETIN WQRGIASIGS NDWHPRCIAP TYQAPSYVES FKGRQTFTGE
EKQEGNKPVE ITSKNRRKSA ANSSHETRMT QNRTWPIVLA DTRIQKGASP IQIEWTWPHA
KNPWISPNHG AIAGHIRFVN MTILDSSSIS TKQELDHREA QVIPTTQTVS GVHRLTPLLE
KTVFSQDDGE IQRMLPFSRA LVKPVRTNRS KTRRNASGKT QVKAQARSQA KARSVRLKLK
ETVKTRSQEK FTNEMKKQLA KSSEGNKGFQ IRQALFPKKL IRLMVVLRPV DIMTFATYGA
RVCIPLGAMI YQGEELFEGA STPISGQLIE IRRDRVTLRI GQPYRVGWQS RLMVTRDQIV
KAEKVLAHLL YFKTKTGDIV QGLPKIEEIL EARRKKGNEI IRSNLQDFVQ QFYQDNLDEG
FSRKYASTRT MRAMQVLILR RVQLVYRSQG VQISDKHLEI ISLRMTSRVL VEKAYGTGIL
PGEIIEKRRA DMLNQGRTRI RYCPIVLGIT KASLTTKGFI SSASFQETTR VLTQAVLQGK
SDWLLGLKEN VILGRLIPAG VGIYGHWVGP HEFNIKQMLK LWVLPPIITG QSTMRAMFHS
TTRYWQDLEA VMESPNKLYP VTPYKCYPDT QHLAGLSIWM PEFEFRRFET FTEEEMVAAE
SLFTAHPNCH ARRINNKQLN SLI
