ID A0A117DW74_ASPNG Unreviewed; 1747 AA.
AC A0A117DW74;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=ABL_01460 {ECO:0000313|EMBL:GAQ36048.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ36048.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ36048.1}.
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DR EMBL; BCMY01000002; GAQ36048.1; -; Genomic_DNA.
DR PaxDb; 5061-CADANGAP00001227; -.
DR VEuPathDB; FungiDB:An01g12710; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1132532; -.
DR VEuPathDB; FungiDB:ATCC64974_13200; -.
DR VEuPathDB; FungiDB:M747DRAFT_297091; -.
DR OMA; MVQYDRT; -.
DR Proteomes; UP000068243; 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; 13.
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 243..549
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 154..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..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..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1747 AA; 193235 MW; 194D1562198273F6 CRC64;
MANVYFPYSK APLRTIKEIQ FGLFSPEEIK RMSVVHVEYP ETMDDQRQRP RTKGLNDPRL
GTIDRQWNCE TCEEGQKECP GHFGHIELAT PVYHIGFLTK IKKLLETVCH NCGKIKANTS
DPKFLEALRM RDPKRRFDHI WRLSKDVLIC EADPPPDDDE PFSKENSKPV RMHGGCGNAQ
PQIRKEGITL VGTWKPNKMM DEMDMQQPEK KVITPQVALN VFRNISYEDV RIMGLSNDYA
RPEWMIITVL PVPPPPVRPS VLVGGSTSGQ RGEDDLTYKL AEIVRANQNV QRCEQEGAPE
HVVREFESLL QYHVATYMDN DIAGQPKAMQ KSNRPVKAIR SRLKGKEGRL RQNLMGKRVD
FSARTVITGD PNLSLEEVGV PKSIARTLTY PEVVTPYNIE KLQTLVSNGP NEHPGARYIV
RDNGERIDLR HAKRAGGQQL LYGWKVERHI MDGDVILFNR QPSLHKESMM GHRVRVMPYS
TFRLNLSVTT PYNADFDGDE MNLHVPQSEE SRAELSQLAL VPMNIVSPQR NGPLMGIVQD
TLCGIYKICR RDVFLTKDQV MNIMMWVPDW DGVIPPPAIL KPRPRWTGKQ MISMALPSGL
NLLRVDKDNS PLSEKFSPLA DGGLLIHNGQ LMYGMFSKKT VGASGGGVIH TIFNEYGHGT
AVAFFNGAQR IVNYWLLHNG FSIGIGDTIP DELTIQRIEN CVRNRKKEVE SITASATDNT
LEPLPGMNVR ETFESKVSRA LNNARDEAGS ETEKSLKDLN NAIQMARSGS KGSTINISQM
TAVVGQQSVE GKRIPFGFKY RTLPHFTKDD YSPESRGFVE NSYLRGLTPT EFFFHAMAGR
EGLIDTAVKT AETGYIQRKL VKALEEVMVK YDGTVRNSLG DIIQFIYGED GLDGAHIENQ
RVDIIKCSDD KFRDRFRVDL MDPERTLGPE VLEQANEIAG DVEVQRHLDE EWEDLLKDRA
FLRSVAKEDE EMMQLPINVQ RILETARTTF RIREGTISDL HPAEVIPQVR SLLDRLLVVR
GNDIISREAQ ENATLLFKAQ LRSRLAFRRL VTEYSMNKLA FQHVIGAIES RFAKAGANPG
EMVGVLAAQS IGEPATQMTL NTFHFAGVSS KNVTLGVPRL KEILNVATNI KTPSMTVYQE
AARSFDKEGA KQLRSAVEHT SLRSVTEATE IYYDPDIQTT VIENDRDMVE SYFIIPEDVT
DDASRQSKWL LRIILSRPKL LDKGLTVQDV ASRIKAAYPK DIAVIFSDNN ADEQVIRIRQ
IQDYKEDEED DDIEYDVTLK KLEQHLLDTL TLRGVPGVER AFINEKSKVR VLEDGSLFAS
KTDPLCKEWV LETSGSSLGE VLAIPGVDAT RTYSNQFIEV FEVFGIEAAR TAVLRELTQV
LAFDGSYVNH RHLALLVDVM TVRGYLTPVT RHGINRADNG ALMRCSFEET VEILLEAAAF
GELDDCRGVS ENLILGQMAP AGTGEFDIYL DQNLMNTVVS NNARFGVMGA IGAKDAIISD
GAATQYDTGS PMQESAYIGT PDPESNFSPI RQAGAETPGG FTEYQPTGGF GGGFSPAATS
PAGYSPSSPF SANPTSPGYS PTSSYSPTSP GMAITSPRFM STSPGFSPAS PSFAPTSPAY
SPTSPAYGQA SPTSPSYSPT SPGFSPTSPN YSPTSPSFSP ASPAFSPTSP SYSPTSPAVG
GVGRHLSPTS PTSPKYTPTS PGWSPTSPQT YSPTSPNFAG SPTSPGGPTS PGYSPTSPAF
SPTSPRQ
//
