ID F9Q8R3_9PAST Unreviewed; 956 AA.
AC F9Q8R3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN Name=rpoC {ECO:0000313|EMBL:EGV06116.1};
GN ORFNames=HMPREF9952_1916 {ECO:0000313|EMBL:EGV06116.1};
OS Haemophilus pittmaniae HK 85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV06116.1, ECO:0000313|Proteomes:UP000006235};
RN [1] {ECO:0000313|EMBL:EGV06116.1, ECO:0000313|Proteomes:UP000006235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK 85 {ECO:0000313|EMBL:EGV06116.1,
RC ECO:0000313|Proteomes:UP000006235};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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|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:EGV06116.1}.
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DR EMBL; AFUV01000010; EGV06116.1; -; Genomic_DNA.
DR AlphaFoldDB; F9Q8R3; -.
DR STRING; 1035188.HMPREF9952_1916; -.
DR Proteomes; UP000006235; 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 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; -; 3.
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; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
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; PF05000; RNA_pol_Rpb1_4; 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 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 1..217
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 956 AA; 104627 MW; 33D13FE837E20FE3 CRC64;
MLQESVDALL DNGRRGRAIT GSNRRPLKSL ADMIKGKQGR FRQNLLGKRV DYSGRSVITV
GPYLHLHQCG LPKKMALELF RPFIYAKLES RGYATTIKAA KKMVEREDAI VWDILAEVIR
EHPILLNRAP TLHRLGIQAF EPLLIEGKAI QLHPLVCAAF NADFDGDQMA VHVPLTLEAQ
LEARALMMST NNVLSPANGD PIIVPSQDVV LGLYYMTREK VNGKGEGMLL QDPREAEKAY
RTGEAELHSR VKVRITEYVK NEAGGFEEKT TLTDTTIGRA ILWMIAPKGM PYSLFNQTLG
KKAISKLINE AYRRLGLKEA VMFADHIMYT GFAYAARSGS SVGIDDMVIP EKKYEIISAA
EAEVAEIQEQ FQSGLVTAGE RYNKVIDIWA AANERVAKAM MENLSQEEVI NREGNSEKQA
SFNSIFMMAD SGARGSAAQI RQLAGMRGLM ARPDGSIIET PITANFREGL NVLQYFISTH
GARKGLADTA LKTANSGYLT RRLVDVAQDL VIVEDDCGTH EGLVVTPLIE GGDEKVPLRE
LVLGRVAAED IYKPGTEEVL IARNTLLDEK LCDVLDANSV DSVKVRSVVT CDTDFGVCAK
CYGRDLARGH LINQGEAVGV IAAQSIGEPG TQLTMRTFHI GGAASAAAKE SSVQIKNNGT
LHLVNAKFVT NDEGKLVLTS RNTELTVTDA FGRTKEHYKV PYGTVLNKAD GQEVAAGETV
ANWDPHTMPV VSEVSGFVKF VDIVDGLTVT RQTDELTGLS SIVVQDVGER ATAGKDLRPT
IKLVDAKGND IFLPETDVIA QYFLPGKAIV SLDDGAEVKV GEPLARIPQE SVGTKDITGG
LPRVADLFEA RKPKEPAILA EISGIVSFGK ETKGKRRLLI TPTEGETYEE MIPKWRQLNV
FEGEMVQRGD VISDGAETPH DILRLRGVRA VTEYIVNEVQ EVYRLQGVKL TISTLK
//
