ID A0A178E774_9PLEO Unreviewed; 1730 AA.
AC A0A178E774;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-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=IQ07DRAFT_620487 {ECO:0000313|EMBL:OAL51807.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51807.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL51807.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51807.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441642; OAL51807.1; -; Genomic_DNA.
DR STRING; 765867.A0A178E774; -.
DR InParanoid; A0A178E774; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000077535; 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:UP000077535};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 368..694
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 142..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1730
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 1384..1398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1730
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1730 AA; 191679 MW; 7795DE16337D187A CRC64;
MNTHQPVSSA IQGVEFGFLA ANDIRSLSVK RITNPTTFDT LLHPVPGGLH DAALGSFLDN
PCSTCGLTTM LGCPGHCGHI ELPVPVYHLT FLDQLLRLLR GKCVYCHHFK IARVQVNEFV
SRLRLIRCGL VQEANEMHEH IDIGKGKAGK RGADDSESDD ENEDIISQRN NYVKRCMKKA
GISKHEARSA RGKNDTISEA RRLVLKEFYA QIVLGKKCKN CQGINPTFRK DRGIKIFRKN
LSSKEMALMA QAEKRMQNPL DVLARRDAKD KKNVHADEGV ADLDPDSEED MDIDMEDLED
ADGSLVATEA STRRKAGTAV DAADSSQEYI TTAEVRAAMV LLFENEPDMV RLLYSPHSSK
SLVDVSADMF FMEAVVVPAN RYRMEDKTGD SIAESPKNTL YKGILNACDA MRQISNEMKG
QENEAGYRRR NFDDLQTQWV NLQGAVNALI DRDANPVQGR ASVTNADGIK QNLEKKEGLF
RKNMMGKRVN FAARSVISPD PNIETNEIGV PPVFAMKLTY PEPVTNHNFY DLKEAVLNGP
DKWPGAHAIE NEFGQVIALR KKNYEERLAL ANQLLAPSNS YSNGSKNKKV HRHLNNGDVV
IMNRQPTLHK PSMMAHRARV LPGEKTIRMH YANCNTYNAD FDGDEMNMHF PQNELARAEA
MTIADTDHQY LSATAGKPLR GLIQDHISMG VWLTNKDTFF TREEYHQLLY SCLRPEDGHT
TSGRLETVEP VIIKPRPLWT GKQIITSVLK NIKPAEYQDL TLTSKSSTSG TLWGIHTEEQ
IVIVKDGQLL SGILDKSQIG PAAGGLINGV YEAYGETIAG RALSIIGRLL TKLLHMRAFS
CGVEDLILTA EGDKARLEEL QKAEKKGFEV AAKYVTMDSE TIDPRNPELL RRLENVLRDD
TKQHGLDLLT NTANGKVSSA VTKACLPLQL IKPFPKNQMQ AMTGSGAKGS LVNANQISCN
LGQQVLEGRR VPIMVSGKTL PCFKPFETSV RAGGYIVNRF LTGIRPQEYY FHMMAGREGL
IDTAVKTSRS GYLQRCIVKG MEGLHVEYDT SVRDSDGSMV QFLYGEDGLD PTKQKYLNDF
KFQAENFLSL AQALRAQEAY AQVYSPEASE HNKKAAKKAR KGDIAAMDPV TAAFTPSRHS
GSTSESFLSA KKEYCESNPD KLLKNKKKDP EGEILKKSFE QMLDVKYLKS LVEPGEAVGV
VAGQSIGEPS TQMTLNTFHL AGHSAKNVTL GIPRLREIVM TASAKISTPS MQLYPHPEMS
KEDNEKFAKS ITRLPLAAVL DKVTVTEVSG PGTQFGQARS YKIRLDFYPA KEYTQEYAIK
VRDVAESIEQ KFCPRLQKNI RFDLKKKGQN KSLSSANSAS VPAIGEGLRS IDQQARDVDP
ETEKEGANDD DESDDGEGEG DATHAKARGR RDDSVGYDEP GEEEQEFNDM LDREDASEDD
ETYGGSPRPS RAATPESESD EDDEQMLVPT DEASEIRRDR IVNKNQDIFE FTFDDRKGAF
CEITFEFAAT TPKLLMLNHV EAAADFSTIH VIPGITAASY STEGDEPFIT TDGSNLLAMR
EFSHIIDVNR IHTNDIAAML RLYGVEACRA SIAREMHNVF SGHGISVDQR HLNLIADTMT
KGGGFTPFNR IGLKDNVSPF MKMSFETTVG FLKEAVLEKD WDELKNPSAK IVVGRLGGIG
TGAFDVLAPV TVVDPLKQAV GQVDETVLEG VEERSGSEDD EDEDITMNDA
//
