ID A0A0D2AV95_9EURO Unreviewed; 1739 AA.
AC A0A0D2AV95;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=PV08_11607 {ECO:0000313|EMBL:KIW10643.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW10643.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW10643.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW10643.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; KN847500; KIW10643.1; -; Genomic_DNA.
DR RefSeq; XP_016230859.1; XM_016385915.1.
DR STRING; 91928.A0A0D2AV95; -.
DR GeneID; 27338690; -.
DR VEuPathDB; FungiDB:PV08_11607; -.
DR HOGENOM; CLU_000487_2_4_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000053328; 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; -; 1.
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:UP000053328};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 380..703
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 770..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1461
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1739 AA; 193667 MW; 2C005965AC3E1100 CRC64;
MAGYPKPLPS ATAGLAFSRL PSEEIRKISV KQIHVSPALD SMFGPVPGGV HDLALGAISA
LDANCSTCRM NAVHCAGHCG HIELPVPCYH PQYMDMTLRL LRAQCAYCYR FKAPRNVTNQ
TICALRLLEY GLVDDYHTIR NMHLGGRRPK RQKTDDVVEE ILEADEDEDI DSLIERRTRA
TEKAIKRARR KDLLDMQALT RNHIAIAARK QVITDFLKEV PLLKSCASCG GASVNFRKDR
NVKIFRKPLA QRQREAMRVL GKTLPNPLEY LLETKKQQET AMKKPLVNGI HDGDVEMADA
SQTSAPETHG AEEEIALRNA LETTYASKNA KLEDEEDVQR YMSPPEVQAA LILLFEYEND
VLNLLFGSKS SRKQALVSPD MFFMTAVLVP PNKYRPLSRQ GAEQMTEAQI NGALNRIIRA
AADVRTIRRE NRKAKTDKTV RPRSFNENIQ AMIVLQETVN ALIDSPLPAS GKPVDQGIKQ
VLEKKEGLFR MHMMGKRVNF AARSVISPDP NIETNEIGVP LVFAKKLTYP EPVTSHNFDE
LSKAVINGPD KYPGAAAVEN ENGQVLSLKR KSLDQRRAIA KQLMTSVIPG SKGEIGKKVY
RHLQTGDVVI MNRQPTLHKP SMMGHRARVL TGQKTIRMHY ANCNTYNADF DGDEMNMHFP
QNELARTEAL QIADTDHQYL SATAGKPLRG LIQDHISMGV QFTSRDVFLD REQYQQLLYS
CLRPEDYNTV FERIQMVPPA ILKPKMMWTG KQVVTTVLKN ITPDRFHGLN LTSKSSTSSE
SWGEKTTNDS SKWDVTSEVV TFRDTEQIVI FRDGEHLSGI LDKNQLGPSA GGLVHSIHEL
YGHITAGKLL SIMGRLLTRV LNERAWSCGM DDLYLTKEGD ALRRTELLRG KQIGLETSAE
YVTLDKNQVD QDDPQLLSRL ENVLRNDEQL NGLDQLYKAK VKSITDNVSK SCLPAGLRKP
FPRNQMQAMT ISGAKGSSVN ANLISCNLGQ QVLEGRRVPT MVSGKTLPSF RAFETDPVAG
GYVSGRFLTG IKPQEYFFHT MSGREGLIDT AVKTSKSGYL QRCIVKGLEG ARTEYDTSVR
ETSNGNVLQF LYGEDGLEVT KQKHLREFTF LAENNQSVAT LMRAEEVLEK LPNEGLAEEQ
KAILKSVRRN KPRDPLTGLF SPASHLGSTS ESFAEALNAY IKENPDKLIR DKKTNPGGII
SKRTFQSIMD LKYMRSIVEP GEAVGVVAAQ SVGEPSTQMT LNTFHLAGHS AKNVTLGIPR
LREIIMTASA KIMTPTMTLK PIEEMTVADG ETFAKSISRL PLAHVIDTLS VTERTGAGAG
REHERHYDIQ IKLYEPDEYE KEYAIKQEDV RLCLEKRFLP RLNKMIKDEF KKKTREASLS
ETTAAVPAVG VSVGVAEEAR PTRTRTTDRE GGEDDIDEDA DPDDAKDAAA RKRREDTFDE
PDDEEKDIAN ESDDESMASD DETLADVLLK KSRTEKQSQA LREQNPDESD ANDAVDSEEE
ARQEQLKASI PHLSRFNFTS NEGRSCRIVL SYDSNTPKLL LLPLLEKCAH IAVIQSIPGL
GVCTQFMEEV HGPDGKPVKQ INPETGKEDI KKEPVITTEG VNLLAMRDYQ DQIMPHSVYT
NSVHDMLKYY GVEAARMTII KEIDGVFKGH GISVDSRHLN LIADAMTQSG SYQPFSRHGL
VKEGGSVLAK MSFETVMGFL KDAVLFGEND PLLGPSARIV AGRRGNIGTG SFDVVMPVH
//
