RPOC1_SYNR3
ID RPOC1_SYNR3 Reviewed; 634 AA.
AC A5GVF1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=SynRCC307_1957;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT978603; CAK28860.1; -; Genomic_DNA.
DR RefSeq; WP_011936372.1; NC_009482.1.
DR AlphaFoldDB; A5GVF1; -.
DR SMR; A5GVF1; -.
DR STRING; 316278.SynRCC307_1957; -.
DR PRIDE; A5GVF1; -.
DR EnsemblBacteria; CAK28860; CAK28860; SynRCC307_1957.
DR KEGG; syr:SynRCC307_1957; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_030022_2_0_3; -.
DR OMA; WGERTLP; -.
DR OrthoDB; 105573at2; -.
DR Proteomes; UP000001115; 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_1000051995"
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; 72460 MW; F4BBFADC2BA21C2E CRC64;
MTNSNTRTES HFDYVKIKLA SPERIREWGQ RTLPNGQVVG EVTKPETINY RTLKPEMDGL
FCEKIFGPSK DWECHCGKYK RVRHRGIVCE RCGVEVTESR VRRHRMGFIK LAAPVSHVWY
LKGIPSYVAI LLDMPLRDVE QIVYFNCYVV LDPGDHKTLK YKQLLTEDEW LEIEDEIYAE
DSEIETEPEV GIGAEALKAL LEDLELTEIA EQLREDISGS KGQKRAKLIK RLRVIDNFIA
TDARPEWMVL DAIPVIPPDL RPMVQLDGGR FATSDLNDLY RRVINRNNRL ARLQEILAPE
IIVRNEKRML QEAVDALIDN GRRGRTVVGA NNRPLKSLSD IIEGKQGRFR QNLLGKRVDY
SGRSVIVVGP KLKMHQCGLP KEMAIELFQP FVIHRLIRQN IVNNIKAAKK LIQRADDEVM
QVLQEVIDGH PILLNRAPTL HRLGIQAFEP KLVDGRAIQL HPLVCPAFNA DFDGDQMAVH
VPLALEAQTE ARMLMLASNN ILSPATGQPI ITPSQDMVLG AYYLTATRQE RSKPEFGDRS
RTYANLEDVC HAFEEKRITL HDWVWVRFNG AVDDDDEAKE PIKSETLSDG TRVEQWQYRR
DRLDEDGALI SRYVLTTTGR VVMNRTIIDA VVTR
