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RPOC1_SYNS3
ID   RPOC1_SYNS3             Reviewed;         634 AA.
AC   Q0I7L8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=DNA-directed RNA polymerase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE            Short=RNAP subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=RNA polymerase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=Transcriptase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
GN   Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323}; OrderedLocusNames=sync_2357;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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_01323}.
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_01323};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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. {ECO:0000255|HAMAP-Rule:MF_01323}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR   EMBL; CP000435; ABI45531.1; -; Genomic_DNA.
DR   RefSeq; WP_011620264.1; NC_008319.1.
DR   AlphaFoldDB; Q0I7L8; -.
DR   SMR; Q0I7L8; -.
DR   STRING; 64471.sync_2357; -.
DR   EnsemblBacteria; ABI45531; ABI45531; sync_2357.
DR   KEGG; syg:sync_2357; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_030022_2_0_3; -.
DR   OMA; WGERTLP; -.
DR   OrthoDB; 105573at2; -.
DR   Proteomes; UP000001961; Chromosome.
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:0000287; F:magnesium ion binding; 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; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR   InterPro; IPR012755; DNA-dir_RpoC1_gamma.
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; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR034678; RNApol_RpoC1.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   SMART; SM00663; RPOLA_N; 1.
DR   TIGRFAMs; TIGR02387; rpoC1_cyan; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..634
FT                   /note="DNA-directed RNA polymerase subunit gamma"
FT                   /id="PRO_1000051996"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         475
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ   SEQUENCE   634 AA;  72432 MW;  11588A74E169CD53 CRC64;
     MTNSNLRTEN HFDYVKITLA SPDRVMEWGQ RTLPNGQVVG EVTKPETINY RTLKPEMDGL
     FCEKIFGPSK DWECHCGKYK RVRHRGIVCE RCGVEVTESR VRRHRMGFIK LAAPVSHVWY
     LKGIPSYVAI LLDMPLRDVE QIVYFNCYVV LDAGDHKDLK YKQLLTEDEW LEIEDEIYAE
     DSEIENEPVV GIGAEALKQL LEDLQLNAVA EQLREEIAGS KGQKRAKLIK RLRVIDNFIA
     TNARPEWMVL DAIPVIPPDL RPMVQLDGGR FATSDLNDLY RRVINRNNRL ARLQEILAPE
     IIVRNEKRML QEAVDALIDN GRRGRTVVGA NNRPLKSLSD IIEGKQGRFR QNLLGKRVDY
     SGRSVIVVGP KLKMHQCGLP KEMAIELFQP FVIHRLIRQN IVNNIKAAKK LIQRADDEVM
     QVLQEVIDGH PIMLNRAPTL HRLGIQAFEP KLVDGRAIQL HPLVCPAFNA DFDGDQMAVH
     VPLAIEAQTE ARMLMLASNN ILSPATGDPI ITPSQDMVLG SYYLTALQPQ MHPIEFGDRS
     RTYSSLEDVI HAFEDNRITL HDWVWVRFNG EVEDEDEREE PITTETLSDG TRFEQWTYRR
     DRFDEDGALI SRYILTTVGR VVMNHTIIDA VAAT
 
 
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