ID A0A395GPS7_9EURO Unreviewed; 1679 AA.
AC A0A395GPS7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=BO80DRAFT_414467 {ECO:0000313|EMBL:RAK97479.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK97479.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK97479.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK97479.1,
RC ECO:0000313|Proteomes:UP000249402};
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; KZ824462; RAK97479.1; -; Genomic_DNA.
DR STRING; 1448316.A0A395GPS7; -.
DR VEuPathDB; FungiDB:BO80DRAFT_414467; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000249402; 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:UP000249402};
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 145..166
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 1375..1389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1679 AA; 186577 MW; 6D6E855010DA1705 CRC64;
MTTFARPVAS SIAGIDFGVY NDEDIKAISV KRIHNTPTLD SFNNPVPGGL YDPAMGAWGD
HVCTTCRQTS WSCTGHPGHI ELPVHVYNVT HFDQLYRLLK GQCVYCHRFQ MTRFNINTYT
CKLRLLQYGL VDELAVIDTM AHKKSDKKKT AKDGDGSSSE DEDDDDIIDR RNNYVKKCIR
QAQADGRLKG LMAGSKNPLA AEQRRALVRE FFKDIGSPSK CASCSGISPS YRKDRSSKIF
RKALAEKSRH LMAQAGFQIP NSLVLLQQAK KLTSKEKEAL ANGVSDSVST TSETHGAEEE
VARGNAIVAQ AESKRQAPGE SQQFMPSPEV HAAMTLLFEK EEEILSLVYN SRPLPKKESR
VSADMFFIKN ILVPPNKFRP AAPQGPGQIM EAQQNQSLTS 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 DYHQLLYSCL RPENSHTITD
RIQTVGPAVI RPKRLWTGKQ VITTILKNIM PSDRAGLNLK SKSSTPGDRW GEGNEEGEVI
FKDGEMLCGI LDKKQIGPTA GGLVDAIHEI YGHTIAGRLM SILGRLLTRV LNMRAFTCGI
DDLRLTPEGD RVRKEKISEA AAIGREVALK YVTLDQTSVP DEDAELRRRM EEVLRDDEKQ
GGLDSVSNAR TAKLSTEITK ACLPGGLVKP FPWNQMQSMT ISGAKGSSVN ANLISCNLGQ
QVLEGRRVPV MVSGKTLPSF RAFDTNPMAG GYVCGRFLTG IKPQEYYFHA MAGREGLIDT
AVKTSRSGYL QRCLIKGMEG LRAEYDSSVR EATDGSIVQF LYGEDGLDIT KQVHLKDFDF
LASNYVSIMS QVNLTSDFHN LEKEEVTNWH KDAMKKVRKT GKVDAMDPVL SLYHPGGNLG
SISESFSQAL KKYEDANPDK LLKDKKKDVN GIISKKAFNT LMHMKYMKSV VDPGEAIGIV
AGQSIGEPST QMTLNTFHLA GHSAKNVTLG IPRLREIVMT ASAHIMTPTM TLVLNEEMSK
EHSERFSKAI SKLSIAEVVD KVQVRERVSS GSMKAKVYDI EITFFPADEY TAEYAITTKD
VQNTLQNKFI PKLVKLTKAE LKKRHEEKSM KRYSTAQPEI GVSVGTVQDA PRADDAEEEP
ADDDVEDDED DAKRARGTQN RSNQVSYEGP EDEEMEMVRQ QDDEEEDDDE DNEAGEKRDV
EMDDASDDES DGHTKDTKMR EEDIKGKYHE VTQFKFNPRD GGSCTIQLQY DIATPKLLLL
PLVEDAARNA VIQSIPGLGN CTFVEADPIK GEPAHVITDG VNLLAMRDYQ DIIKPHSLYT
NSIHDMLTLY GVEAARASIV KEMSDVFQGH SIAVDNRHLN LIGDVMTQSG GFRPFNRNGL
VKDGSSPLAK MSFETTVGYL KEAVVERDFD NLKSPSARIV VGRTGTVGTG AFDVLAPVA
//
