ID A0A178AYC0_9PLEO Unreviewed; 1470 AA.
AC A0A178AYC0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=IQ06DRAFT_292865 {ECO:0000313|EMBL:OAL02139.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL02139.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL02139.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL02139.1,
RC ECO:0000313|Proteomes:UP000077206};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; KV441710; OAL02139.1; -; Genomic_DNA.
DR STRING; 765868.A0A178AYC0; -.
DR InParanoid; A0A178AYC0; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000077206; 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: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; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_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; 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; 1.
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; 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; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 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:UP000077206};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 265..578
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 1470 AA; 164239 MW; CDA6EAFE8DC03700 CRC64;
MEAPRYLAKP QVVDRIPARI KHIQFGIYSN QDIVNQAVIE VSDRNVYDLG NASDNSRTLT
ANGPMDPLMG ISSKTGACAT CGEKLEKCNG HFGHIKLALP AFHVGYLKHI IEVLNCICKD
CSRVLLDEME RRRYLRSMRR PDMDTLRRSA ISKKVLEDCR KKKTCPYCDA LQGTVRKVPG
HPLKIIHNRY DAFNRSTAKT KKPPAGKVEF DQSFDTAKTA NPDLEKHLKK AVDDMHPLRA
LNLFKKISPE DCELLAMIPE DARPEMLIWE YMPVPPVALR PSVMQEGGAT EDDVTNKIGD
ICQISSIIRA GLARGFPLQI LMEQWDFLQL QIAMYINSDA PGLKQQGLQK TMRGFSQRLK
GKGGRFRQNL SGKRVDFSGR TVIGPDPNLS IDEVAVPQRV AKVLTYPEKV TRYNIDKLKK
LVRNGAKKYP GANLIMKDMG PNQDPRKISL IALSRHGRGE KLNGPAEALR IGDVVERHLE
DGDIVLFNRQ PSLHKLSILS HRAKIRPWRT FRLNECVCNP YNADFDGDEM NLHVPQTEEA
RTEATELMGV KYNLATPKNG TPIIAAIQDF ITAAFILSNK SNFYDRRTFC QIVNYMFTGE
GAFDPDTGEY LPIEIPPPVI WKPQALWTGK QVFNLLMRPN KKSRVLVNLE AGCKQFKPVH
GRAHDLDEND AYLVIRNSEV MCGVMDKSTV GDGKKDSVFY VMMRDFGPQH AVQGMNRLAR
LSARWLTNNG FSLGISDVTP GDVLNQKKQA LVDEAYVKCD KLIRDFQEGK LQRDAGCDEE
QTMEVRIGGI LSGVRQAAGD ICFEELSRWN SPLLMAKCGS KGSNINVSQM VASVGQQMIG
GARVADGFHH RTLPHFPKAA RQPASKGFVS NSFFSGLTPS EFIFHAMSGR EGLVDTAVKT
AETGYMSRRL MKSLEDLSAQ YDDTVRNSSG TVVQFQYGDD NLDPVDMEGK AQPVHFDRTF
SHAITSTWDN DEPSLTPEAV RTHTEKKLDV ERTKYPRFKL DGVSALDYRD KSDSAIDQKE
SMRDFLDTVQ VYVFKKAQKL ETTLLHLGVT QTAGKRRSKK DAEIYTLADG IAKISQTALD
TFIDLCLTKY HRSRVQPGHA VGAIGAQSIG EPGTQMTLKT FHFAGVAGMS ITQGVPRIKE
IINASSTIST PVITCVLSNK ISESAARIVK ARVEKTYLRD IISYVEDVWH PNGAYIAMRI
DWDTVNALFV DVSPQEIVNA INKHKPLKWG KSGTKVRISS SLIRVEVADP SAAKKRPVKN
TKNHKEFFER VQQVKALIPD VVIKGYPDCT RAIIRKETKP NDQGLYECEL LVEGYGFKDC
LTTPGIEPYK TMSNHVMEVR TVLGIEAARA TIVREISSVM GNMDIDPRHM ALLADVMTFK
GDVYGITRFG LQKTRDSVLQ LASFEKTPDH LFEAAARGKT DTIDGVSESI IMGQSMKLGT
GALQVVRPLK LSTEELKEQR TMFEDGWDAL
//
