ID A0A0G0MK82_9BACT Unreviewed; 1096 AA.
AC A0A0G0MK82;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
DE Flags: Fragment;
GN ORFNames=US96_C0041G0001 {ECO:0000313|EMBL:KKQ74094.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_38_5b.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618569 {ECO:0000313|EMBL:KKQ74094.1, ECO:0000313|Proteomes:UP000034181};
RN [1] {ECO:0000313|EMBL:KKQ74094.1, ECO:0000313|Proteomes:UP000034181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
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|RuleBase:RU004279};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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:KKQ74094.1}.
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DR EMBL; LBUZ01000041; KKQ74094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MK82; -.
DR Proteomes; UP000034181; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd01609; RNAP_beta'_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
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; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR NCBIfam; TIGR02386; rpoC_TIGR; 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 Pfam; PF04998; RNA_pol_Rpb1_5; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 330..610
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT COILED 154..228
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1096
FT /evidence="ECO:0000313|EMBL:KKQ74094.1"
SQ SEQUENCE 1096 AA; 121866 MW; 09FFB0ADC11D12BD CRC64;
MNTQIQPIDD LIKLADFTSL VIRLASPEDI RRWSRGEVLK PETINYRTLK PEKDGLFDER
IFGPTKDWEC YCGKYKRIRY KGVVCDKCGV EVTQSRVRRE RMGHISLATP VAHVWFFKGA
PSRLSLLLGV APRAIEQVIY FARYLAVDVK EEGRKEAMKS LEKTRAEREK EINDTFKEAK
ENLAHEAEKE KAKVEGKIKD KEQLALALNE VDLELRKKET SLNEEEGKTI EKTGQLFENL
ISLAKNVKPL TVLSEDEYDE LVDHNAGDFI TVKMGADAVL SAIEKVNLDE VSISLRKELE
ESKVGSSKYI KVSKRLKLID GLRRAKINPA SMILRVLPVL PPDLRPMVQL SGGRFATSDL
NDLYRRVINR NNRLKHLIGL GAPEIILRNE KRMLQEAVDS LIDASQRKAT RKGRGKQPLR
SLSDMLRGKQ GRFRQNLLGK RVDYSGRSVI VVGPELKLTQ CGLPKEMALE MFKPFVLREM
IVRGIAPNVK SAKNMLDRRP PEVFDILEEI IKDHPVLLNR APTLHKLSIQ AFYPVLIEGN
AIRLHPTVCS GFNADFDGDQ MAVHVPLSKK AIEEAKTLML PTSNLLKPSD GSPATTPASK
EMALGVYFLT SIDTDIKTPN SLFGDKNEVI LAYQSGRVEL RQIITVMTDS GIVDTTCGRI
LFNESLPEGF DFVNESVTSA VIKQLLAKAF NTQTNDRVAE MIDAIKDLGF WGGTLSGLSF
GISDAKVHPD KAKMLLEADK EVAKIEENFA QGLITNEEKK RLAQEVWINV SEDLVEKTWN
ALPESNPIKI VINAKVGRTS KDQVKQLAAM RGLIVDPMGK IVELPIKSNF REGLSEFEYV
TSSRGSRKGL TDTAIKTADA GYLTRRLVDV AHDVIVREED CGTKEKYIVR RSPRANVFYS
RILGRYLAED LTDNKGKVLF TKGTLLGEVD AKSVETNENV SEVAVRSPLT CGLRHGICVK
CYGLDISNKK VVALGTPVGV VAAESIGEPG TQLTLRTKHT GGAVGVDVTQ GLPRVEELFE
ARTPKVLSPL SEISGKVKID ETDGGWKVTV TSKEAKLKDE REYIIPKSIK LALADGDVIE
SGSALAQGSL DIKEIL
//