ID K9QGW3_9NOSO Unreviewed; 625 AA.
AC K9QGW3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=DNA-directed RNA polymerase subunit gamma {ECO:0000256|HAMAP-Rule:MF_01323};
DE Short=RNAP subunit gamma {ECO:0000256|HAMAP-Rule:MF_01323};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01323};
DE AltName: Full=RNA polymerase subunit gamma {ECO:0000256|HAMAP-Rule:MF_01323};
DE AltName: Full=Transcriptase subunit gamma {ECO:0000256|HAMAP-Rule:MF_01323};
GN Name=rpoC1 {ECO:0000256|HAMAP-Rule:MF_01323};
GN ORFNames=Nos7107_4072 {ECO:0000313|EMBL:AFY44623.1};
OS Nostoc sp. PCC 7107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY44623.1, ECO:0000313|Proteomes:UP000010381};
RN [1] {ECO:0000313|EMBL:AFY44623.1, ECO:0000313|Proteomes:UP000010381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY44623.1,
RC ECO:0000313|Proteomes:UP000010381};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Nostoc sp. PCC 7107.";
RL Submitted (AUG-2012) 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:0000256|ARBA:ARBA00004026, ECO:0000256|HAMAP-Rule:MF_01323,
CC ECO:0000256|RuleBase:RU004279}.
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:0000256|HAMAP-Rule:MF_01323,
CC ECO:0000256|RuleBase:RU004279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00025825,
CC ECO:0000256|HAMAP-Rule:MF_01323}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000256|ARBA:ARBA00007207, ECO:0000256|HAMAP-
CC Rule:MF_01323}.
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DR EMBL; CP003548; AFY44623.1; -; Genomic_DNA.
DR RefSeq; WP_015114822.1; NC_019676.1.
DR AlphaFoldDB; K9QGW3; -.
DR STRING; 317936.Nos7107_4072; -.
DR KEGG; nos:Nos7107_4072; -.
DR PATRIC; fig|317936.3.peg.4414; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_030022_2_0_3; -.
DR InParanoid; K9QGW3; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000010381; 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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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 NCBIfam; TIGR02387; rpoC1_cyan; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01323};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01323};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01323};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01323}; Reference proteome {ECO:0000313|Proteomes:UP000010381};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01323};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01323}; Zinc {ECO:0000256|HAMAP-Rule:MF_01323}.
FT DOMAIN 242..521
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323"
SQ SEQUENCE 625 AA; 70667 MW; 68C3AF42043A7227 CRC64;
MRSAQTNQFD YVKIGLASPE RIRQWGERTL PNGQLVGEVT KPETINYRTL KPEMDGLFCE
RIFGPAKDWE CHCGKYKRVR HRGIVCERCG VEVTESRVRR HRMGYIKLAA PVAHVWYLKG
IPSYIAILLD MPLRDVEQIV YFNSYVVLSP GNAETLTYKQ LLSEDQWLEI EDQIYSEDST
LQGVEVGIGA EALLRLLADI NLEQEAESLR EEISTAKGQK RAKLIKRLRV IDNFIATGSK
PEWMVMTVIP VIPPDLRPMV QLDGGRFATS DLNDLYRRVI NRNNRLARLQ EILAPEIIVR
NEKRMLQEAV DALIDNGRRG RTVVGANNRP LKSLSDIIEG KQGRFRQNLL GKRVDYSGRS
VIVVGPKLHI HQCGLPREMA IELFQPFVIN RLIRSGMVNN IKAAKKLISR NDPSVWDVLE
EVIEGHPVML NRAPTLHRLG IQAFEPILVE GRAIQLHPLV CPAFNADFDG DQMAVHVPLS
LESQAEARLL MLASNNILSP ATGKPIITPS QDMVLGAYYL TAENPHATKG AGKYFASLED
VIMAFEQGQI DLHAYIYVRF DGELESDQPD TEPLEVTNND DGTRTLMYKF RRVREDSQGN
LISQYIRTTP GRVIYNNAIQ EALAS
//
