ID   RPOC1_PROHO             Reviewed;         203 AA.
AC   P42075;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=DNA-directed RNA polymerase subunit gamma;
DE            Short=RNAP subunit gamma;
DE            EC=2.7.7.6;
DE   AltName: Full=RNA polymerase subunit gamma;
DE   AltName: Full=Transcriptase subunit gamma;
DE   Flags: Fragment;
GN   Name=rpoC1;
OS   Prochlorothrix hollandica.
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Prochlorotrichaceae;
OC   Prochlorothrix.
OX   NCBI_TaxID=1223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1731224; DOI=10.1038/355265a0;
RA   Palenik B., Haselkorn R.;
RT   "Multiple evolutionary origins of prochlorophytes, the chlorophyll b-
RT   containing prokaryotes.";
RL   Nature 355:265-267(1992).
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 cyanobacteria the RNAP catalytic core is composed of 2
CC       alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC       factor is associated with the core the holoenzyme is formed, which can
CC       initiate transcription (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; Z11154; CAA77505.1; -; Genomic_DNA.
DR   PIR; S20584; S20584.
DR   AlphaFoldDB; P42075; -.
DR   SMR; P42075; -.
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; 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   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Transcription; Transferase; Zinc.
FT   CHAIN           <1..>203
FT                   /note="DNA-directed RNA polymerase subunit gamma"
FT                   /id="PRO_0000067844"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   NON_TER         1
FT   NON_TER         203
SQ   SEQUENCE   203 AA;  23442 MW;  85B2C9B17CA7304D CRC64;
     EVTKPETINY RTLKPEMDGL FCERIFGPAK DWECHCGKYK RVRHRGIVCE RCGVEVTESR
     VRRHRMGYIK LAAPVTHVWY LKGIPSYISI LLDMPLRDVE QIVYFNSYVV LDPGNHPELQ
     TKQLLTEDQS MELEDQIYAE DSTLEGIEVG IGAEALERLL QDLELEQDAE RLREEINSAK
     GQKRAKLIKR LRVVDNFVAT GSH