ID A0A286UMB1_9AGAM Unreviewed; 593 AA.
AC A0A286UMB1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=PNOK_0321200 {ECO:0000313|EMBL:PAV20585.1};
OS Pyrrhoderma noxium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV20585.1, ECO:0000313|Proteomes:UP000217199};
RN [1] {ECO:0000313|Proteomes:UP000217199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA Kikuchi T., Tsai I.J.;
RT "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT Hymenochaetales Members.";
RL bioRxiv 0:0-0(2017).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:PAV20585.1}.
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DR EMBL; NBII01000003; PAV20585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286UMB1; -.
DR STRING; 2282107.A0A286UMB1; -.
DR InParanoid; A0A286UMB1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000217199; Chromosome 3.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 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 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 PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
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|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000217199};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 244..546
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 593 AA; 66938 MW; AA8E6ED6AA6960A4 CRC64;
MKDTVSHNAP KVIKKIQFGL LNAQDVVKLS EFQVTHRDLY TAVDRAPVKD GVLDRRLGTS
VKNAFCETCG LASADCVGHY AYIKLALPVF HIGYLKHIVS ILQCICKTCS RVLLDEPERR
IYLKRFRRPN LENIQRMALI KAVNGLSRKV VYCPYCSATN GAVKKVGAIK IIHDKFRAKK
TTEELDKFKK SFATAIEAQK EIGIYISKAV HEDLNPLKVL DLFKRISDED CELLGLNPSH
GRPEEYIWQY ISVPPVCIRP SVAQDGASNE DDLTVKLTEI VFTSALIKQG LLKGAPTQQF
MEQWDFLQVS VAIYINSETP GIPIQMAQKP IRGFCQRLKG KQGRFRGNLS GKRVDFSGRT
VISPDPNLRI DEVAIPERVA KILTYPERVT SHNIDMLKRA VRNGCDVHPG ANFVTAGNSG
FKKFLKFGNR TAIADSLRVG DTVERHIIDG DIVLFNRQPS LHKLSIMCHR VKVRPWRSFR
LNECVCGPYG ADFDGDEMNI HVPQTEEART EALTLMSIKL NLVTPRNGEP VIAAIQDFIT
ASFLLSQRDR FFDRRQFTQI CSYLGDADLH IDIPLQQYLS HNVFGQESKF SMF
//
