ID Q2U3T5_ASPOR Unreviewed; 1447 AA.
AC Q2U3T5;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=AO090020000625 {ECO:0000313|EMBL:BAE63780.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE63780.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE63780.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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|ARBA:ARBA00024550,
CC 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}.
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DR EMBL; AP007167; BAE63780.1; -; Genomic_DNA.
DR RefSeq; XP_001824913.1; XM_001824861.2.
DR STRING; 510516.Q2U3T5; -.
DR EnsemblFungi; BAE63780; BAE63780; AO090020000625.
DR GeneID; 5996999; -.
DR KEGG; aor:AO090020000625; -.
DR VEuPathDB; FungiDB:AO090020000625; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OMA; AVCPPYN; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000006564; Chromosome 6.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005666; C:RNA polymerase III complex; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001056; F:RNA polymerase III activity; IEA:EnsemblFungi.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IEA:EnsemblFungi.
DR GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; IEA:EnsemblFungi.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IEA:EnsemblFungi.
DR CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 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; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
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 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 265..567
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 1447 AA; 162136 MW; FCCED1AF1CADB857 CRC64;
MQPPEGVQVD LGKAQVIDRA PKVIKELKFG VLSNDDIVSQ GVVEVSDRKF FDLDRDRSVV
AHGPLDSRMG VSSKTASCQT CGGALQVCNG HFGHVKLVLP SFHVGYFKRV ITILQEICKE
CSHILLPEGE RRAFLREMRR PGLDNLRRLQ IAKRINERCR KTRNCDRCGA TNGVVKKAGT
SALKITHDKF RAFNASTSMK KIPPPSKIVF DRSFEEARSH NPEVEKHHKK AQDDMNALRV
LNLFKRISDT DCELLGLDPK EARPEMFLWQ YIPAPPVCIR PSVGQDASST EDDLTAKLGD
IVQSNINLKN ALLKGAPVQT IMECWDYMQL QIAVYINSDV PGLNKADLGK PIRGFVQRLK
GKQGRFRGNL SGKRVDFSGR TVISPDPNLR VDEVAVPELV AKNMTYPEVV TRYNKEKLQQ
RVRNGTKKWP GANYLVKKGS TFKTFLKYGS LNMIADQLQE GDVVERHIED GDIVLFNRQP
SLHKLSILSH FAKVRPHRTF RLNECVCNPY NADFDGDEMN LHVPQTEEAR AEAMELMGVK
NNLATPKNGE PIISAIQDFI SAAYILSSKD NFFDRRSFTQ ICLYMLGPET RFDLPPPAVL
KPQMLWTGKQ VFNILMRPNK DDPVMVNLDA ACREYKPPKD GRPKDLDPKD GWLVIRNSEV
MCGVMDKATI GSGKKDNVFY VMLRDFGPPA AAEGMNRLSR LSARWFTNMG FSIGITDVYP
SEKLLQSKHD LVETAYAQCD EVIAQYKAGT LETFPGCDEL QTMENKLSGI LSKVRQQAGD
ECIAQLSKYN SPLIMATSGS KGSSINVSQM VALVGQQIIG GQRVQDGFQD RTLPHFPKNA
RQPPSKGFVR NSFFSGLEPY EFIFHAMSGR EGLVDTAVKT AETGYMSRRL MKSLEDLSSR
YDDTVRNSSG HIVQFQYGDD KLDPVDMEGK AKPVHFDRTF IHSEATTYDN DERSLQPAEI
MEVCEEMLSK ERAKLVRKDL LDVELGYMDR SNHGVDQFES ARDFLESIQQ YVSTKADKLI
SRGGDIDPSD ERSQQGLNHT GKLTEKTLRT FISACLMKYK KAQVEPGHAV GAVGAQSIGE
PGTQMTLKTF HFAGVAGMSI TQGVPRIKEI INASKEISTP VVSCELVTKD NVIAARIVKG
RIEKTYLRDI THYVRETWTG KEAYITVKIN WKTIQDLALE LKIQDILAAI KNHRRFKSDD
LKFRCQRSHI HIYMDVDPAS KLGLSKTEIA ATSADPFLRL KHLKRLLPDI QVLGHPQAYR
AIIRTDDTST TNTLLVEGYG LRACMNTIGV DGLRTSTNNV MEMREVLGIE AARTTIVREI
SEVMKDMDID PRHMQLLADV MTYKGEVLGI TRFGLAKMRD SVLQLASFEK TADHLFDAGG
AGRTDLVEGV SECIIMGKTV SLGTGAMEVV RRMNFFEGQI GARKTTFEDT WNNVCEAPLK
SKKRART
//
