ID B0XMU6_ASPFC Unreviewed; 1750 AA.
AC B0XMU6;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=AFUB_014220 {ECO:0000313|EMBL:EDP56703.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP56703.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP56703.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; DS499594; EDP56703.1; -; Genomic_DNA.
DR EnsemblFungi; EDP56703; EDP56703; AFUB_014220.
DR HOGENOM; CLU_000487_1_1_1; -.
DR PhylomeDB; B0XMU6; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_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; 3.30.1360.140; -; 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; 2.
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; IPR000684; RNA_pol_II_repeat_euk.
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; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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 Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 12.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 3.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 244..550
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 153..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1733..1750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1750 AA; 193513 MW; BE6EB05DC08928CE CRC64;
MSNVYFPYSK APLRTIKEIQ FGLFSPEEIK RMSVVHVEYP ETMDEQRMRP RTKGLNDPRL
GTIDRQWNCE TCEEGQKECP GHFGHIELAT PVFHIGFLTK VKKLLETVCH NCGKIKADTS
DSKFLEALRM RDPKRRFDHI WRLSKDVLIC EADPPPDEDE PFSKESSKPL RRHGGCGNAQ
PTIRKEGITL VGTWKPNKSM MDEDEMQQPE KKVITPQMAL NVFRNISHED VRIMGLSNDY
ARPEWMIITV LPVPPPPVRP SVLVGGSTSG QRGEDDLTYK LAEIIRANQN VQRCEQEGAP
EHVVREFESL LQYHVATYMD NDIAGQPKAM QKSNRPVKAI RSRLKGKEGR LRQNLMGKRV
DFSARTVITG DPNLSLDEVG VPRSIARTLT YPEVVTPYNI EKLQQLVANG PNEHPGARYI
VRDNGERIDL RHARRAGGQQ LLYGWKVERH LMDGDIILFN RQPSLHKESM MGHRVRVMPY
STFRLNLSVT TPYNADFDGD EMNLHVPQSE ESRAELKQLA LVPLNIVSPQ RNGPLMGIVQ
DTLCGIYKIC RRDVFLTKEQ VMNIMLWVPD WDGVIPPPAI LKPRPRWTGK QMISMALPSG
LNLLRVEKDN SSLAEKFSPL TDGGLLIHGG QLMYGMFSKK TVGASGGGVI HTIFNEYGPD
TAVAFFNGAQ TIVNYWLLHN GFSIGIGDTI PDAITIQRIE NCVRERKKEV EAITASATEN
TLEPLPGMNV RETFESKVSR ALNNARDEAG SETEKSLKDL NNAIQMARSG SKGSTINISQ
MTAVVGQQSV EGKRIPFGFK YRTLPHFTKD DYSPESRGFV ENSYLRGLTP TEFFFHAMAG
REGLIDTAVK TAETGYIQRK LVKALEEVMV KYDGTVRNSL GDVIQFIYGE DGLDGAHIEN
QRVDVIRCSD EKFRERFRVD LMDPERSLGP EVLEQANEIA GDVEVQRYLD EEWEQLLKDR
AFLRTVAKED DEMMQLPINV QRILETARST FRIREGAISD LHPAEVIPQV RSLLDRLLVV
RGDDPISREA QENATMLFKA QLRSRLAFRR LVTEYSMNKL AFQHVLGAIE SRFAKAAANP
GEMVGVLAAQ SIGEPATQMT LNTFHFAGVS SKNVTLGVPR LKEILNVATN IKTPSMTVYQ
LPHRCHDKES AKQLRSVVEH TSLRSVTEAT EIYYDPDIQT TVIENDRDMV ESYFIIPEDV
TDATSRQSKW LLRIILSRPK LLDKGLTVQD VAAKIKQAYP KDIAVIFSDN NADEQVIRIR
QIQDYKEDED DEDIEYDVTL KKLEQHLLDT LTLRGVQGVE RAFINEKSKV RVLEDGSLFA
SKTDPLCKEW VLETSGSSLG EVLAVPGVDA TRTYSNQFIE VFEVFGIEAA RTAVLRELTQ
VLAFDGSYVN HRHLALLVDV MTVRGYLTPV TRHGINRADN GALMRCSFEE TVEILLEAAA
FGELDDCRGV SENLILGQMA PAGTGEFDLY LDQNLLNTVV SNNARFGVMG TIGAKDAIIS
DGAATQYDTG SPMQESAFIG TPDPESAFSP IRQAGAESPG GFTEYQPTGG FGGGFSPAAT
SPAGYSPSSP FSANPTSPGY SPTSSYSPTS PGMGITSPRF MTSPGFSPAS PSFAPTSPAY
SPTSPAYGQA SPTSPSYSPT SPGFSPTSPN YSPTSPSFSP ASPAFSPTSP SYSPTSPAIG
GAGRHLSPTS PTSPKYTPTS PGWSPTSPQT YSPTSPNFAG SPTSPGGPTS PGYSPTSPAF
SPSYVPSSSA
//
