ID A0A2T1E562_9CYAN Unreviewed; 1329 AA.
AC A0A2T1E562;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324};
GN ORFNames=C7B82_16090 {ECO:0000313|EMBL:PSB27893.1};
OS Stenomitos frigidus ULC18.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Stenomitos.
OX NCBI_TaxID=2107698 {ECO:0000313|EMBL:PSB27893.1, ECO:0000313|Proteomes:UP000239576};
RN [1] {ECO:0000313|Proteomes:UP000239576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC18 {ECO:0000313|Proteomes:UP000239576};
RA Moore K., Momper L.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB27893.1, ECO:0000313|Proteomes:UP000239576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC18 {ECO:0000313|EMBL:PSB27893.1,
RC ECO:0000313|Proteomes:UP000239576};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) 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_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:0000256|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00025825,
CC ECO:0000256|HAMAP-Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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:PSB27893.1}.
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DR EMBL; PVWK01000084; PSB27893.1; -; Genomic_DNA.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000239576; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 2.40.50.100; -; 3.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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; 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 NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
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; 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_01324};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Reference proteome {ECO:0000313|Proteomes:UP000239576};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Zinc {ECO:0000256|HAMAP-Rule:MF_01324}.
FT DOMAIN 9..63
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04983"
FT DOMAIN 92..170
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 173..626
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1094..1187
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT REGION 1306..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1329 AA; 145510 MW; 775EE4296065DE96 CRC64;
MVEQNNQPVF RNRVVDKGQL RKLISWAFTT YGSARTAQMA DQLKDLGFRY ATRAGVSISV
DDLQIPPSKR KLLEAAEETI RATEERYTRG EITEVERFQK VIDTWNGASE ELKDEVVRHF
RSNNPLNSVY MMAFSGARGN ISQVRQLVGM RGLMADPQGE IIDLPIKTNF REGLTVTEYI
ISSYGARKGL VDTALRTADS GYLTRRLVDV SQDVIIRELD CGTQRGIPVR SMMDGDRVLI
PLKNRLLGRV AAEPMVDPAT GEVIVERNQS ITDEMADHIG RAKLEEVIVR SPLTCEATRS
VCQHCYGWSL AHAHMVDIGE AVGIIAAQSI GEPGTQLTMR TFHTGGVFTG EMARQEKAQF
DGTLKFPKKL RIRPYRTRHG EDAYTVESVE ASSKLTLEAK DGRQQTFSVL QGATLLVKDG
QKVKEGQILA EVPLTGRARK TTEKAAKDVA SDMAGEVQFA DLVPEEKKDR QGNTTRIAQR
GGLVWIRSGE VYNLPPGAEP IVKNGDRIDA NGVIAETKLV TEHGGVVRLP ADADGKGGRE
VEIITASVLL DEAKVRAESF QGRDHYLIET NYNQLFSLKA TPGTKVTNNQ VVAELIDDHY
RTQTGGIIKY SGVEVAKRGK AKQGYEVVKG GTLLWIPEEA HEVNKDISLL MVEDGQYVEA
GTEVVKDIFC QSNGVVEVTQ KNDILREIVV KPGDLHMVDN LDDIITKESI LVNPGQTVMA
GLTVDELRYV EYVETPEGPA LLLRPVTEFT VPDEPSVPSQ ESANEESGRS IRLRAVQRLP
YKDGERVKSV EGLELLKIQL VLEIGQDAPQ LAADIELVPD ETDSETMRLQ LVILESLVIR
RDIAADPTQG PTKTRVLVKD GDQIAPGAVV ARTEILCKEA GEVQGIREAA EAIRRILVVR
PADMITVTTK GKPPTVKVGD LLVAGSDLAP GVALQESGQI VSVGDAEVTL RHARPYRVSP
GAVLHIDDGD LVQRGDNLVI LVFERTKTGD IIQGLPRIEE LLEARKPKEA CVLAARPGTA
QVVYGDDDSV KVKVIETDGV IAEYLIGPGQ NVIVSDGQEV LAAEPLTDGP ANPHEILEVF
FKYRRETDGV HDAALVSLQM VQTFLVNEVQ SVYQSQGVDI SDKHIEVVVR QMTSKARVDD
GGDTTMLPGE LVELYQVEQV NEAMAITGGA PAEYTPVLLG ITKASLNTDS FISAASFQET
TRVLTEAAIE GKSDWLRGLK ENVIIGRLIP AGTGFNAYEE QSSPDVDLSY DGIGVFDDDA
DLKDVVLDDR TARSYGLDSF DERPTYTFDN FGVPAVDAEP FSPILEDDDL ISDDVDEVDD
VDDIDVDDA
//
