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Database: UniProt
Entry: K9X571_9NOST
LinkDB: K9X571_9NOST
Original site: K9X571_9NOST 
ID   K9X571_9NOST            Unreviewed;       625 AA.
AC   K9X571;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Cylst_5170 {ECO:0000313|EMBL:AFZ27211.1};
OS   Cylindrospermum stagnale PCC 7417.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ27211.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ27211.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ27211.1,
RC   ECO:0000313|Proteomes:UP000010475};
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., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL   Submitted (JUN-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; CP003642; AFZ27211.1; -; Genomic_DNA.
DR   RefSeq; WP_015210446.1; NC_019757.1.
DR   AlphaFoldDB; K9X571; -.
DR   STRING; 56107.Cylst_5170; -.
DR   KEGG; csg:Cylst_5170; -.
DR   PATRIC; fig|56107.3.peg.5674; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_030022_2_0_3; -.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000010475; 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:UP000010475};
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;  70538 MW;  1489FC8223E11610 CRC64;
     MRHAQTNQFD YVKIGLASPE RIRQWGERTL PNGQVVGEVT KPETINYRTL KPEMDGLFCE
     RIFGPAKDWE CHCGKYKRVR HRGIVCERCG VEVTESRVRR HRMGFIKLAA PVAHVWYLKG
     IPSYIAILLD MPLRDVEQIV YFNSYVVLGP GNAETLSYKQ LLSEDQWLEI EDQIYSEDSL
     LVGVEVGIGA EALLRLLADI NLEQEAESLR EEIGNAKGQK RAKLIKRLRV IDNFIATGSK
     PEWMVMAVIP VIPPDLRPMV QLDGGRFATS DLNDLYRRVI NRNNRLARLQ EILAPEIIVR
     NEKRMLQEAV DALIDNGRRG RTVVGANNRP LKSLSDIIEG KQGRFRQNLL GKRVDYSGRS
     VIVVGPKLKI HQCGLPREMA IELFQPFVIN RLIRSGMVNN IKAAKKLISR NDPSVWDVLE
     EVIEGHPVLL NRAPTLHRLG IQSFEPILVE GRAIQLHPLV CPAFNADFDG DQMAVHVPLS
     LESQAEARLL MLASNNILSP ATGKPIITPS QDMVLGAYYL TAENPGATKG AGGYYFSLDD
     VIMAYQQEQV DLHAYIYVRF DGEMETDQPD TEPVEVTENS DGSRTLLYKF RRVRQDAKGN
     LLSQYIRTTP GRVIYNKAIQ EALAS
//
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