RPOC1_CHLVU
ID RPOC1_CHLVU Reviewed; 836 AA.
AC P56300;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=DNA-directed RNA polymerase subunit beta';
DE EC=2.7.7.6;
DE AltName: Full=PEP;
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta';
DE Short=RNA polymerase subunit beta';
GN Name=rpoC1;
OS Chlorella vulgaris (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3077;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM C-27 / Tamiya;
RX PubMed=9159184; DOI=10.1073/pnas.94.11.5967;
RA Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S., Tsudzuki J.,
RA Nakashima K., Tsudzuki T., Suzuki Y., Hamada A., Ohta T., Inamura A.,
RA Yoshinaga K., Sugiura M.;
RT "Complete nucleotide sequence of the chloroplast genome from the green alga
RT Chlorella vulgaris: the existence of genes possibly involved in chloroplast
RT division.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5967-5972(1997).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250|UniProtKB:P0A8T7}.
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:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000305}.
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DR EMBL; AB001684; BAA57970.1; -; Genomic_DNA.
DR PIR; T07322; T07322.
DR RefSeq; NP_045894.1; NC_001865.1.
DR AlphaFoldDB; P56300; -.
DR PRIDE; P56300; -.
DR GeneID; 809115; -.
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; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..836
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067868"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 623
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 625
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 627
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
SQ SEQUENCE 836 AA; 96562 MW; FB50D65D2EA7A3DE CRC64;
MSTRKSPFFK KAEISLASPK AIEIWTERYF PNGQPINEVT SSETVNYKTL KPEPHGLFCQ
TIFGPVVDFT CACGKKATKL VKNKKFRGYC PKCGVERTSS RVRRYRLGLI KLKQPVAHSL
YVSHRPSPLR LCLGWSTKRL QAVLKAVEFC YLPLIFTTFQ SERECFSFFP KSFLLLRSQL
TQKNEVFLEP RSSGFNENLS SSFFFKEKKR SKRKTGKVFP LRTSPRLFHK KHQKNRPRLV
FNHGVIEARL YGIAYDATWP KVEEFQEFLF YLWEQSFFYE SSIPYYAFAK GVKSYKEEIP
KREQSYALQT GGLALQQILS HHDSSRFEYD LIYLSKKVSM ILEILKENMA SLNLDYEDDQ
KEYKKLLSKV KKLDLLLLKW KRQRELYRDF EVGKTQPAWM ILNNLPVLPP GLRPITSIGG
LVVASDINSF YRKIIIRNKR MSPRNNLGIF DTTLGGSWLS WCYNLRQVQE AVDELLRTGS
VDAGRPLKSL LDGLKGKKGR FRQHLLGKRV DYSGRSVIVV GPKLKLHQCG LPKEMAVELF
QPFIIQQLRL QGIVFTVTAA KVLIADRKPI VWSVLGEILK RHPVLLNRAP TLHRLGIQAF
LPRLVEGKAI LLHPLVCPAF NADFDGDQMA VHVPLSAKTR AEALSLLWSR NQLLAPSSGQ
PQHLPTQDMV LGFYYLTCSL EKTLKRVDSL VSSRKLFFQS SFFLKKKNEE TLKNSIPQNL
YFSEFSQVKT AYDIGNLTLH TPIWVKWTSC VQTFVPERHS RLKETLLETR LTFSGQRQTL
FIDTCQFFSP SFFFGKKVRF IRTTPGRIFM HWCFFEANAE MSSTPTSKEK KSLEKK
