ID A0A319EUH5_ASPSB Unreviewed; 1679 AA.
AC A0A319EUH5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=BO78DRAFT_393191 {ECO:0000313|EMBL:PYI11855.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI11855.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI11855.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI11855.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; KZ826317; PYI11855.1; -; Genomic_DNA.
DR STRING; 1448318.A0A319EUH5; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; 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 CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR CDD; cd01435; RNAP_I_RPA1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.357.120; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.2850; -; 2.
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; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
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; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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:UP000248423};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 364..691
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 142..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1679 AA; 186294 MW; 32A180ABC923847B CRC64;
MTTFARPVAS SIAGIDFGVY NDEDIKAISV KRIHNTPTLD TFNNPVPGGL YDPAMGAWGD
HVCTTCRQTS WSCTGHPGHI ELPVHVYNVT HFDQLYRLIK GQCVYCHRFQ MTRFNINTYT
CKLRLLQYGL VDEVAVIDTM AHRKTDKKKT AKDGDGSSSE DEDDDDIIDR RNAYVKKCIR
QAQADGRLKG LMAGSKNPLA AEQRRALVRE FFKDIGSPSK CASCSGISPS YRKDRSSKIF
RKALAEKSRH AMAQGGFQIP NSLVLLQQAK KLTSKEKEAL ANGVSDSVST TSETHGAEEE
VARGNAIVAL AESKKQAPGE SQQFMPSPEV HAAMTLLFEK EEEILSLVYN SRPLPKKESR
VSADMFFIKN ILVPPNKFRP AAAQGPGQIL EAQQNTSLTS ILKNCDIINQ ISKERQSAGA
DSATRVRDYR DLLHSIVTLQ DTVNMLIDRD RGNATGPAAA SAPMGIKQYL EKKEGLFRKN
MMGKRVNFAA RSVISPDPNI ETNEIGVPMV FAKKLTYPEP VTNHNFWEMK QAVINGPDKY
PGASAIENEF GQVTNLRFKS LDERTALANQ LLAPSNWRMK GSRNKKVYRH LTTGDIVLMN
RQPTLHKPSI MGHKARVLPN ERTIRMHYAN CNTYNADFDG DEMNMHFPQN ELARSEAMML
ADADHQYLVA TSGKPLRGLI QDHISMGTWF TCRDSFFDED DYHQLLYNCL RPENSHTITD
RIQTVGPAVI RPKRLWTGKQ VITTILKNIM PADRAGLNLK SKSSTPGDRW GEGNEEGEVI
FKDGEMLCGI LDKKQIGPTA GGLIDAIHEI YGHTIAGRLM SILGRLLTRV LNMRAFSCGI
DDLRLTPEGN RVRKEKISEA AAIGREVALK YVTLDQTTVP DEDAELCRRL EEVLRDDEKQ
GGLDSVSNAR TAKLSTEITK ACLPGGLVKP FPWNQMQSMT ISGAKGSGVN ANLISCNLGQ
QVLEGRRVPV MVSGKTLPSF RAFDTNPMAG GYVCGRFLTG IKPQEYYFHA MAGREGLIDT
AVKTSRSGYL QRCLIKGMEG LRAEYDSSVR EATDGSIVQF LYGEDGLDIT KQVHLKDFDF
LASNYVSIMA QVNLTSDFHN LEKEEVTNWH KDAMKKVRKT GKVEAMDPVL SLYHPGGNLG
SISESFSQAL KKYEDANPDK LLKDKKKDVN GIISKKAFNT LMHMKYMKSV VDPGEAIGIV
AGQSIGEPST QMTLNTFHLA GHSAKNVTLG IPRLREIVMT ASAHIMTPTM TLVLNEEMSK
EHSERFAKAI SKLSIAEVVD KVQVRERVSS GSMKAKVYDI EVTFFPADEY TAEYAITTKD
VQNTLQNKFI PRLVKLTKAE LKKRHEEKTM KKFSTAQPEI GVSVGTVQDA PRADDAEEEP
VDDDVEDDED DAKRARGTQN RSNQVSYEGP EDEEMEMVRQ QDDEEDDEEE DNDAGEKRDV
EMDDASDDES GGHTKDTKMR EEDIRGKYHE VTQFKFNPRD GGSCTIQLQY DISTPKLLLL
PLVEDAARSA VIQSIPGLGN CTFVEANPIK GEPAHVITDG VNLLAMRDYQ DIIKPHSIYT
NSIHDMLNLY GVEAARASIV KEMSDVFQGH SIAVDNRHLN LIGDVMTQSG GFRPFNRNGL
VKDGSSPLAK MSFETTVGYL KEAVVERDFD NLKSPSARIV VGRTGTVGTG AFDVLAPVA
//
