ID A0A0F0IAP5_ASPPU Unreviewed; 2612 AA.
AC A0A0F0IAP5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=P875_00010908 {ECO:0000313|EMBL:KJK64829.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK64829.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK64829.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) 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|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}.
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:KJK64829.1}.
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DR EMBL; JZEE01000383; KJK64829.1; -; Genomic_DNA.
DR STRING; 1403190.A0A0F0IAP5; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
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 InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_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; 11.
DR Pfam; PF08238; Sel1; 8.
DR SMART; SM00663; RPOLA_N; 1.
DR SMART; SM00671; SEL1; 10.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR SUPFAM; SSF81901; HCP-like; 3.
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}; Membrane {ECO:0000256|SAM:Phobius};
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 Reference proteome {ECO:0000313|Proteomes:UP000033540};
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 2545..2564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 244..550
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 152..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2570..2601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2612 AA; 289207 MW; 52C79EBD41062338 CRC64;
MSNVYFPYSK APLRTIKEIQ FGLFSPEEIK RMSVVHVEYP ETMDEQRQRP RTKGLNDPRL
GTIDRQWNCE TCEEGQKECP GHFGHIELAT PVFHIGFLTK IKKLLETVCH NCGKIKANTS
DSKFLEALRM RDPKRRFDHI WRLSKDVTIC EADPPPDEDE PYAKESSKPT RMHGGCGNAQ
PTIRKEGITL VGTWKPSKSM MDEMDMQQPE KKTITPQMAL TIFRNISHED VRIMGLSNDY
ARPEWMVLTV LPVPPPPVRP SVLVGGSTSG QRGEDDLTYK LAEIVRANQN VQRCEQEGAP
EHVVREFESL LQYHVATYMD NDIAGQPKAM QKSNRPVKAI RSRLKGKEGR LRQNLMGKRV
DFSARTVITG DPNLSLDEVG VPKSIARTLT YPEVVTPYNI DKLQQLVSNG PNEHPGARYI
VRDNGERIDL RHAKRAGGQQ LLYGWKVERH VMDGDVILFN RQPSLHKESM MGHRVRVMPY
STFRLNLSVT TPYNADFDGD EMNLHVPQSE ESRAELLQLA LVPMNIVSPQ RNGPLMGIVQ
DTLCGIYKIC RRDTFLTKDQ VMNLMMWVPD WDGVIPPPAI LKPRPRWTGK QIISMALPSG
LNLLRVDKDN SALSEKFAPL NDGGLLIHGG QLMYGMFSKK TVGASGGGVI HTIFNEYGPG
TAVAFFNGAQ AIVNYWLLHN GFSIGIGDTI PDAVTIQRIE NCVRERKKEV ETITASATDN
TLEPLPGMNV RETFESKVSR ALNNARDEAG SETEKSLKDL NNAIQMARSG SKGSTINISQ
MTAVVGQQSV EGKRIPFGFK YRTLPHFTKD DYSPESRGFV ENSYLRGLTP TEFFFHAMAG
REGLIDTAVK TAETGYIQRK LVKALEEVMV KYDGTVRNSL GDIIQFIYGE DGLDGAHIEN
QRVDIIKCSD DQFRDRFRID LMDPERSLGP EVLEQANEIA GDVEVQRYLD EEWEQLLKAR
AFLRTVAKED EEMMQLPINV QRILEMARTT FRIREGTISD LHPAEVIPQV QALLDRLLIV
RGDDPISQEA QENATLLFKA QLRSRLAFRR LVTEYSMNKL AFQHVIGAIE SRFAKANAPA
GEMVGVLAAQ SIGEPATQMT LNTFHFAGVS SKNVTLGVPR LKEILNVATN IKTPSMTVYQ
EPGRTHDKEG AKQLRSVVEH TSLRSVTEAT EIYYDPDIQS TVIENDRDMV ESYFIIPEDV
TDDSSRQSKW LLRIILSRPK LLDKGLTVQD VATRIKQAYP KDIAVIFSDN NADEQVIRIR
QIQDHKEDED DDDIEYDVTL KKLEQHLLDT LTLRGVNGVE RAFINEKSKV RVLEDGSLFT
SKVDPLCKEW VLETSGSALG EVLAVPGVDA TRTYSNQFIE VFEVFGIEAA RTAVLRELTQ
VLAFDGSYVN HRHLALLVDV MTVRGYLTPV TRHGINRADN GALMRCSFEE TVEILLEAAA
FGELDDCRGV SENLILGQMA PAGTGEFDIY LDQNMLNTVV SNNARFGVMG AIGAKDAIIS
DGAATQYDTG SPMQDNAYIG TPDPESNFSP IRQAGAESPG GFTEYQPTGG FGGGFSPAAT
SPAGYSPSSP FSANPTSPGY SPSSSYSPTS PGMAITSPRF SMTSPGFSPA SPSFAPTSPA
YSPTSPAYGQ ASPTSPSYSP TSPGFSPTSP NYSPTSPSFS PASPAFSPTS PSYSPTSPAI
GGAARHLSPT SPTSPKYTPT SPGWSPTSPQ TYSPTSPNFA GSPTSPGGPT SPGYSPTSPA
FSPSIAPDYK VHHSRSDLIL LHVAVTPADT SCLVLLQALA VESKAPTDVA HESYQHSNQS
PGGTEGSGAR PGSQHVDTAL KILRNSKIPI VTSEKPSGIL GNTLHYSREA FRVLFLNGPP
SDNAERQKIH PNVAKAVDEL KIAAQKDQNP DAMFLLAELN FYGNYTHPRD FKQAFQWYQS
LALATGNSTA QYMVGFMYAT GIGGGVERDQ AKALLYHTFA AEGGNTRSEM TLAYRNHAGI
GMPRNCDHAT YYYKKVADKA IQYFRSGPPG GNSMIRESYR WADEEGGVYG EGASVSSSGP
NAMRDAAHSS TEASLEDVLE YLDLMSRKGE LKATFSLGKM HYEGSRGLPR NLRKAMKYFK
QITKRYWNKD GSVNPNHPLG IEKLASKAAG HIGLMYLRGE GVEQNFATAL TWFRRGVTNG
DSLCQHQMGL MYLHGYGVQQ DAFRAASYFK SASEQDFPAA ETRLGALFLD QGDVPTATRY
FELAARWGWM EAFYYLAELS NNGIGRERHC GMAASYYKMV AERAEVIHSS FDEANTAYEN
GDKERALVAA MMAAEQGYEH AQSNVAFLLD EQRSLMSFDR ILPGAKKPRP SLLRNAALAL
IYWTRSAKQT NIDSLVKMGD YYLGGIGIAA DAEKASSCYH SAAEVHYSAQ AYWNLGWMHE
NGIAVEQDFH MAKRYYDLAL ETSTEAYLPV KLSLLKLRLR SYWNRITNGK INSIQDEEGM
DAAVKFSDTF LLTPCSESKP RRTLKEWIAA FIENDEEEEA YRAQMYKRAE EEDDLLSGGS
DRRHIDDRHE DGYYDDLELD IDESVLEGLI IVALAATLLV LVYMRQQRNR QRQDGNVGAN
PAAPGNGNDD RGFFPRPGDP EFAQWVAGGV GH
//
