RPOC_CYAM1
ID RPOC_CYAM1 Reviewed; 1676 AA.
AC Q85FR6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'-beta'' {ECO:0000305};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01322};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit beta';
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta';
DE Short=RNA polymerase beta';
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit beta'';
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'';
DE Short=RNA polymerase subunit beta'';
GN Name=rpoC {ECO:0000305};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND DISCUSSION OF SEQUENCE.
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(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_01322}.
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_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
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. Beta' and
CC beta'' are fused in this algae. {ECO:0000255|HAMAP-Rule:MF_01322,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01322}.
CC -!- MISCELLANEOUS: In this algae the rpoC1 (beta') and rpoC2 (beta'') genes
CC are fused into one ORF. This seems to be the result of evolution acting
CC to reduce protein size rather than horizontal transfer from a bacteria.
CC Thus this is considered an atypical member of the bacterial RpoC
CC family. {ECO:0000303|PubMed:12755171}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the RNA polymerase
CC beta' chain family. RpoC1 subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the RNA polymerase
CC beta' chain family. RpoC2 subfamily. {ECO:0000305}.
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; AB002583; BAC76279.1; -; Genomic_DNA.
DR RefSeq; NP_849117.1; NC_004799.1.
DR AlphaFoldDB; Q85FR6; -.
DR SMR; Q85FR6; -.
DR STRING; 45157.CMV217CT; -.
DR PRIDE; Q85FR6; -.
DR EnsemblPlants; CMV217CT; CMV217CT; CMV217C.
DR GeneID; 844996; -.
DR Gramene; CMV217CT; CMV217CT; CMV217C.
DR KEGG; cme:CymeCp185; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR HOGENOM; CLU_000524_3_1_1; -.
DR Proteomes; UP000007014; Chloroplast.
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:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR InterPro; IPR012755; DNA-dir_RpoC1_gamma.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR034678; RNApol_RpoC1.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02387; rpoC1_cyan; 1.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1676
FT /note="DNA-directed RNA polymerase subunit beta'-beta''"
FT /id="PRO_0000067870"
FT REGION 1..582
FT /note="DNA-directed RNA polymerase subunit beta'"
FT REGION 583..1676
FT /note="DNA-directed RNA polymerase subunit beta''"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 859
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 866
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1676 AA; 188904 MW; 8478102CC68FF397 CRC64;
MCDAIQIRLA SPERIRSWAE RVLPNGQVVG EVTKPETINY RTLKPEMDGL FCERIFGPVK
DWECHCGKYK KVRYKGIVCE RCGVEVTESK VRRHRMGYID LAAVVSHVWY LKGPPSYLAL
FLNMSSSEVE QVIYFHSYVV LQSTTELVQP KQLLSEDELI ILEERLANQP FQVGIGAQAI
QYLLQQLDLD MEIRVLRNQL FHAKSSKREK LMKRLRILDN FASTGADPSW MILSVLPVIP
PDLRPMVQLD GGRFATSDLN DLYRRVINRN NRLKRLQEIL APEIIIRNEK RMLQEAVDAL
MDNGRRGRSV VGANNRALKS LSHILEGKQG RFRQNLLGKR VDYSGRSVIV VGPELKLYQC
GLPKEMALEL FQPFVIQRLM AQGLANNMKA AKKIIQRKEA IVDQILHQVV KAHPVLLNRA
PTLHRLGIQA FDPILVDGRA IQLHPLVCAA FNADFDGDQM AVHVPLSVEA QAEARLLMLS
VNNFLSPATG DAIIMPSQDM VIGCYYLTAN NPASQAKQSH YFADFEHVLM AFEQKQINLH
TWVWVHVNNN LNIILERSAL QEDWIQTRGE SLFLKTTPGR IIFYQQAAYH VGFYNLTINK
SHLKELVKTV YNLKGMACAT QLADDLKQLG FHYATTCGLS LGIEDLRVAP SKQKIFQWAQ
QAIEKTEQLW QRAQITHVEK FHKVVDTWSE ASETLKQEVV RYYEHTDPLN PVYMMAFSGA
RGNLSQVRQL VGMRGLMADP HGQLIDLPIL SNFREGLTVT EYLISSYGAR KGLVDTSLRT
ADSGYLTRRL VDVAQDVIIR QADCGTLRGI AVPVSKALIG RVLAQDVNEE CKRNQLITAD
MLVALRDTKQ VIVRSPLTCE ALRCICQLCY GGNLAYGHMV DLAEAVGIIA AQSIGEPGTQ
LTMRTFHTGG VFTSAQTASV RATLDGVVTY EGRCKSTRTR YGQEAWLLET STPLFLQNDG
QQHRYDFQAG TVLLVKSGQR VKFNTLLAYL PTSTRFEKAT KSVDAHNAGE VVFDQLKLEQ
NLVKKEGILW ILSGQMLHLP AGSELLVSNE QQIKPAQVLA QSYLRSRAKG IVQIHTNQVE
LILDRLSFEV KEPFHFHSGD GQIIAEKFEH QTPTGGQVFH RNGQIWLVPA AIYEVSSQKD
LVDIKHGQFI LANQRSICGV KNELSGWVQL VKQNEVIKEI RIRPGIYLPK VKTNQLGFVQ
SHLLLSSYGI NAYTRRFCYV ENYEQGILIS PVYVFAGVSP PKIVAKSRWL SLVMYQTCMF
QHQQWVKSYK KVYLMRCQLQ LKVAPQAPLN QVTVHKEKNR REWRLSYFSN IKLQAFQTIK
WLVKNHQRVE ADVPLALIQL VSAFNGIVRY HPMLNRLLVV SDQDVITYSI GKPHHFQIGD
VIRIGDQISH GLVAKTSGFV IARDANQIQV RIAQGYFLSR ETICYVKDGD LVNEGDHLAS
LVFEQVKTGD IIQGLPRIEE ILEARKPKNS CELAQFDGVI QEQSLVSDDG RVQAIKGTLI
VCEGTRVQAG EPLTDGAVNA HEWLQIHFNN AVPYRGMVEA ARESFAKLQA KLLHQVQQVY
KSQGVDIADK HIEVILRQMT SKVILDDPGD SDFLPGQLVY LNEIASYKHV IFHPVLLGIT
KAALNTESFI SAASFQETTR ILAQAAMEGQ IDQLRGLKEN VIMGRLIPAG TGAKYL
