RPOC2_CRYJA
ID RPOC2_CRYJA Reviewed; 1212 AA.
AC B1VKH5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 52.
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 Cryptomeria japonica (Japanese cedar) (Cupressus japonica).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Cryptomeria.
OX NCBI_TaxID=3369;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18570682; DOI=10.1186/1471-2229-8-70;
RA Hirao T., Watanabe A., Kurita M., Kondo T., Takata K.;
RT "Complete nucleotide sequence of the Cryptomeria japonica D. Don.
RT chloroplast genome and comparative chloroplast genomics: diversified
RT genomic structure of coniferous species.";
RL BMC Plant Biol. 8:70-70(2008).
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; AP009377; BAG16686.1; -; Genomic_DNA.
DR RefSeq; YP_001806688.1; NC_010548.1.
DR AlphaFoldDB; B1VKH5; -.
DR PRIDE; B1VKH5; -.
DR GeneID; 6166560; -.
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; 2.
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..1212
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353555"
FT REGION 1162..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 229
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 309
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"
SQ SEQUENCE 1212 AA; 138888 MW; 3A3FD476652850EC CRC64;
MTQNPVKFVH PFPFEVPFFN KGMDKFVMKH LIRRFVNQFG MTYTSHILDQ LKILGFQQAT
DAAISLGIDD LLTTPSKAWL IQDAQQRGFA SERHHDYGNV HAVEKLRQLI EVWHATSEYL
RREMNPNFRM TDPLNPVHMM SFSGARGSTS QVHQLVGMRG LMSDPRGKIV DLPIQGNFRE
GLSLTEYIIS CYGARKGVVD TSIRTADAGY LTRRLVEVVQ HLVVRKVDCG TIQGLFVNLI
QDRETIKNKF VLQTLIGRVL ADDVYIHGRC IATRNEDIGI KLANQLYYFQ VQPIYIRTPF
TCKSIYWICQ LCYGRNTTHS NLIELGEAVG IIAGQSIGEP GTQLTLRTFH TGGVFTGDIA
EHVRAPFTGK IEFNENLVYP TRTRHGHPAY ICYNSLDVTI NNQYEVQNLT IPPESLLFIQ
NNQLVESEQV IAEVRAKRSP FKEKVKKHIY SDLTGEMHRS IPMSNLILET THLWVLSGSI
YESVVVPFSS DQDQVDIPEL LLDKHKSLSN YSVDQVKHES VDSNCFEKGK KILNYFETDR
TIPNEHKDSI YSAILFENTH MSVKKEKNKL IVPLWCDKQW GKRRIPCPDF IFRIPRGQGI
LLNKKHIFAF LNDPRSKMIK YGNILGGYSI EKKRNSLENQ LDGGPRLKIK KTYASLISVG
TNEIIINMIQ ISLLKYPFFN IAKRENIASS PFLFHNKLGH TNLNDQSKLL SKGTIRSLPN
ENKKDESFTI LSPSDFLQIV LFHDLKCLNT VKKLDANKKR IELSGLLGHL HSIANRFPYS
HFMTYKKVLL TERSISNNDS NNFQLAKCYF MDEKREIYQF DSCRNIIFDF FNLNLYFCLS
NFFEKTFSVV SLGQFCSESI WISEDKQLQG SGQIVVVHEE SFVIRLAKPY LGARGATLNS
YYGKILSQGD TLITMLYERL KSDDIIQGLP KVEQLSEARS NTSISKNRKK RFQKLNRYLA
IFFGNFWGSF TSVRMTMEDS QNQLVDEIQK VYRSQGVQIS DKHIEIIVRQ ITSKVLVVDV
DRSENKNWEN GLGSLFLPGE LVGLSRVQRM DRALEKRINY RTILLGMTNA SLNTQSFLSE
ASFQETAQVL AKSALQGRID WLKGLKENVI LGGMIPVGTG FNRLVKRSKM NSRTSQKSLF
INKVEDFFFE HQDQALILSL KQKETSKNKK ETSKNKKETS KNKKETSKNK KETSKNKKET
SKNKKEASKN KK
