RPOC2_MICAN
ID RPOC2_MICAN Reviewed; 1334 AA.
AC B0JGK8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324}; OrderedLocusNames=MAE_54520;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
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_01324}.
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_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
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_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; AP009552; BAG05274.1; -; Genomic_DNA.
DR RefSeq; WP_002796211.1; NC_010296.1.
DR AlphaFoldDB; B0JGK8; -.
DR SMR; B0JGK8; -.
DR STRING; 449447.MAE_54520; -.
DR PaxDb; B0JGK8; -.
DR EnsemblBacteria; BAG05274; BAG05274; MAE_54520.
DR KEGG; mar:MAE_54520; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR BioCyc; MAER449447:MAE_RS23685-MON; -.
DR Proteomes; UP000001510; 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:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR036566; PYNP-like_C_sf.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 4.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SUPFAM; SSF54680; SSF54680; 1.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..1334
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353522"
FT REGION 1299..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1334 AA; 146830 MW; 92F6C30B71FCABE9 CRC64;
MFYNQTVDKG KLKKLIAWAY QNYGSARCSQ MADELKNLGF RFATKAGVSI SVDDLTVPPA
KRQMIESAEQ EIRQTEQRYV RGEITEVERF QKVIDTWNST SESLKDEVIR NFQVTDPLNS
VYMMAFSGAR GNMSQVRQLV GMRGLMANPQ GEIIDLPIKT NFREGLTVTE YVISSYGARK
GLVDTALRTA DSGYLTRRLV DVSQDVIVRE ADCGTNRYVE LTAMTDGDRV LIPLSDRLLG
RSLAEDVVVN GEVIATRNQI IDDETAEKLG RLVDKIKVRS PLTCEAARSV CQTCYGWSLA
HGHPVDMGEA VGIIAAQSIG EPGTQLTMRT FHTGGVFTGE VARQVRSPFE GTVRFLPGLS
IRNVRTRHGD ERDQVEAPGE IKLTPKDKTK ETVTYSLTPG SLLFVTDGET VSEEQLLAEI
TSDKVQKSTE KATKDVTSDL AGEVLFSQLV PEEKTDRQGN TTRIAQRGGL LWILSGEVYN
LPPGAEPVVS NGDQVQVGDV LAETKLVSTN GGLVRLAPNS REIDIVTASV SLDQAEVKVE
SSAGREQFII HTGDGQSFLL KTTPGTKVQN HAIVAELIDD RYQTHTGGMI KYVDIEVAKG
SRKQGYEITK GGTILWIPEE THEVNKDISL LQVEDGQYVE AGEEVVKDIF CNSSGVVEVI
QKNDILREII VKPGLLFMDL EPESSGIAQE QLIYPGTQLT PEVTIEELRQ AEWVETNEGL
GLLLRPVQEF TVQDQSTSPT QGSANQEGGR HIELRSVQRI FFKDGERVKS VEGCQLISTQ
LVLEISSEEP ESVSHLTADI ELEPIEDRDC QRLQLVILES LVLRRDSDND PLGGNIQTRV
LVQDGDEIPP GAVVARTEIQ CKEAGEIRGI RKGSEAVRRL LIVSDRDEFI LPLAVAPTVK
ARDLVIAEAE IAAGVLAPNS GQVLAVDKTA TGYEIRLRKA RPYRVSAGAI LHIDEGDLVQ
RGDNLVLLVF ERSKTGDIIQ GLPRIEELLE ARKPKEACVL ARKPGVCQVE YQDSEIVDIK
VVEDDGTISE YPLLGSQNPL VSDNQRIDVG QALTDGQANP HEILEVFFNY YVDSLGSYEA
ALKALEKTQM FLVDQVQSVY QSQGIDIADK HIEVIVRQMT SKVRIDDGGD TSMLPGELLE
LRQVETVNEA MSITGGAAAK YTPVLLGITK ASLNTDSFIS AASFQETTRV LTEAAIEGKS
DWLRGLKENV IIGRLIPAGT GFNSHENTAG ISDYTPPEEE YNYNNRSYYA PPGGLGLPPR
PGFGDSSEDS DMILDDQTAR AYAEGDVVDL EDDEMAFLSS RGSSRFSRQP ISDRWSEADE
EGEEDDFEED YEEE
