ID A0A252DEM1_9NOSO Unreviewed; 625 AA.
AC A0A252DEM1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BV372_27165 {ECO:0000313|EMBL:OUL26066.1};
OS Nostoc sp. T09.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1932621 {ECO:0000313|EMBL:OUL26066.1, ECO:0000313|Proteomes:UP000195076};
RN [1] {ECO:0000313|EMBL:OUL26066.1, ECO:0000313|Proteomes:UP000195076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T09 {ECO:0000313|EMBL:OUL26066.1};
RA Cruz-Morales P., Corona-Gomez J.A., Gutierrez-Garcia K.G., Barona-Gomez F.,
RA Cibrian-Jaramillo A.;
RT "Metagenomics of subcommunity co-cultures reveals the complexity of the
RT cycad coralloid root endophytic microbiome.";
RL Submitted (JAN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUL26066.1}.
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DR EMBL; MTAV01000153; OUL26066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252DEM1; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000195076; Unassembled WGS sequence.
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:UP000195076};
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; 70576 MW; 8E56A707477A970C CRC64;
MRNAQTNQFD YVKIGLASPE RIRQWGERTL PNGQVVGEVT KPETINYRTL KPEMDGLFCE
RIFGPAKDWE CHCGKYKRVR HRGIVCERCG VEVTESRVRR HRMGYIKLAA PVAHVWYLKG
IPSYISILLD MPLRDVEQIV YFNSYVVLSP GNAETLSYKQ LLSEDQWLEI EDQIYSEDSQ
LQGVEVGIGA EALLHLLADI NLEQEAESLR EEIGNAKGQK RAKLIKRLRV IDNFIATGSK
PEWMVMAVIP VIPPDLRPMV QLDGGRFATS DLNDLYRRVI NRNNRLARLQ EILAPEIIVR
NEKRMLQEAV DALIDNGRRG RTVVGANNRP LKSLSDIIEG KQGRFRQNLL GKRVDYSGRS
VIVVGPKLNI HQCGLPREMA IELFQPFVIN RLIRSGMVNN IKAAKKLISR NDPSVWDVLE
EVIEGHPVLL NRAPTLHRLG IQAFEPILVE GRAIQLHPLV CPAFNADFDG DQMAVHVPLS
LESQAEARLL MLASNNILSP ATGKPIITPS QDMVLGAYYL TAENPDATKG AGRYFASLED
VIMAFQQEQI DLHAYIYVRF DGEVESDGPD TEPLEVTENN DGSRTLLYKY RRVREDAKGN
LLSQYVRTTP GRVIYNKAIQ EALAS
//
