RPC1A_CHLRE
ID RPC1A_CHLRE Reviewed; 603 AA.
AC Q8HUG9; B7U1L0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' N-terminal section;
DE EC=2.7.7.6;
DE AltName: Full=PEP;
DE AltName: Full=Plastid-encoded RNA polymerase beta' N-terminal section;
DE Short=RNA polymerase beta' N-terminal section;
GN Name=rpoC1A;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND COMPLETE
RP PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250}.
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=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 -!- MISCELLANEOUS: In C.reinhardtii the gene for this protein is split in
CC two.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACJ50157.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF541870; AAN17822.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50157.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK000554; DAA00970.1; -; Genomic_DNA.
DR RefSeq; NP_958426.1; NC_005353.1.
DR AlphaFoldDB; Q8HUG9; -.
DR STRING; 3055.DAA00970; -.
DR PaxDb; Q8HUG9; -.
DR PRIDE; Q8HUG9; -.
DR GeneID; 2717050; -.
DR KEGG; cre:ChreCp070; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR HOGENOM; CLU_452974_0_0_1; -.
DR OrthoDB; 1369830at2759; -.
DR Proteomes; UP000006906; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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:0006366; P:transcription by RNA polymerase II; IEA:GOC.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..603
FT /note="DNA-directed RNA polymerase subunit beta' N-terminal
FT section"
FT /id="PRO_0000067866"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
SQ SEQUENCE 603 AA; 68613 MW; 1E070C22CA86F373 CRC64;
MHYKKYAELL KNGTYFSHIH SPTLLYPKGK VMYAQYGNSP LQGLNSQVTN LNLIRKVVAA
SAEMDSFKKL PNLQNNKLPL NNLKARLNTK AIYISNEEAQ LTVSKIGTPN AIETDVPGTI
KNAPSNTLLT HRSFKFFVNK IYAKPLISLK KTKETKPLLL GKTGTTLTQK GLNPFQSLFL
NTKSSSPSTA RSFGTKNIVN TLQIKKIVHK FENSYSKLTE INLITINLAS ANRIRQWAEK
TLPNGKVVGE VINPETIHYK TLKPIKGGLF CERIFGPLKD HECACGKKFN IKNYLTKTVN
NSSIQPIAES RQTQPNTQLS LNLQKRYFCR ICDVEYTYSI IRRTQLGYIQ LASPTTHVWF
VKGIPSYISI LLDMKKKHLQ GITYNTETLT LENSFRGRQL LPVSPSSIFE SWQKIMKKQY
PEKYNLTNTM IKIKSTNTLP LRVSQPNSNT SYSYMPNIYI PEGEGEEKTK TKLKKTTPLN
AIAQKGVKYK KPKTKKALYK QYLKNYYARK PKNSNQAEAV SFGVNKVQLP LTAFQQRNKV
YFYKSEKRNW PVLTTVAKMQ YIVSKKGWFK LIQYVIKSAE SYGAATPTKM DGLQKMSLLT
KQA
