ID W9CD65_SCLBF Unreviewed; 1705 AA.
AC W9CD65;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=SBOR_4911 {ECO:0000313|EMBL:ESZ94717.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ94717.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ94717.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESZ94717.1}.
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DR EMBL; AYSA01000229; ESZ94717.1; -; Genomic_DNA.
DR STRING; 1432307.W9CD65; -.
DR HOGENOM; CLU_000487_2_4_1; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000019487; 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:UP000019487};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 358..688
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 262..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..294
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1705 AA; 188357 MW; 4ABA39F7130A4F98 CRC64;
MNISQPVPSA IDSVDFAFLS TADIKSLSVK RIENPVTFDS LLHPVPGGLY DPALGAWGDN
NCTTCNLSSF SCPGHAGHID LPAPVYHPTF MDQVLRLLRS KCKYCHQFKM SRKEVNRYVC
KLRLIQQGLL SAAEEIDNIE VAQPKEGEEP ASDSDEESPV DSVIRRRLAF VKKELKTAKA
SGWEWRRDKH EGVAEARRVV VKGFMKAITA GRLCGNCQGI SPTYRKDRYV KIFEKSLSVK
DKAKMAQGSY RAVNAVQLVH GEKKDRDGDE GIADIDLESN EDEDEGEGET LDVDGDLVMD
GPTTSTSKPR VAPLPQRYVD AMEVKASLTL LFEKEQEILS LIYNSRSSAK KPSVVRAEVF
FIQTLLVPPN RYRPEAKTGD GEISEAQQNS LYKQILKSAD TVNQIYLDIQ NPDRPSLSAT
LRKRDFFDLQ EACCSMQDAV NSLIDRDRNP IQGAAGKKNE DGIKQKLEKK EGLFRKNMMG
KRVNFAARSV ISPDPNIETN EIGVPPVFAK KLTYPEPVTS HNFKEMQQAV INGVDKWPGA
AAIENENGQV INLRSKTQDE RMALANQLLA SSSNGASGAR NKKVYRHLTN GDVVLMNRQP
TLHKPSIMGH RARVLPGEKT IRMHYANCNT YNADFDGDEM NMHFPQSEVA RAEALQIADT
DHQYLSGTAG KPLRGLIQDH ISISVWMCNK DTYFDRATYQ QLIYNCIRPE SGHIVGERIQ
TVPPAIIKPV ARWTGKQVIT TILKNITPIN CAPISLTGKT QTPADRWGEG SEEGVVLFKG
GEFITGILDK AQIGPAGGGL IHSVHEVYGP ATAGKLLSIL GRLLTKFLHM RAFTCGMDDL
MLTPEGEKTR TETLVDAGNI GLEVAAKYVS LEDQKPSDTD QELLNRLEDV MRDDSKQAGL
DALVNARAGK LSTLITNACL PQGLVKQFPH NQMQNMTVSG AKGTAVNANL ISCNLGQQVL
EGRRVPLMVS GKSLPCFKPF ETHVRAGGYI VNRFLTGIRP QEYYFHAMAG REGLIDTAVK
TSRSGYLQRC LIKGMEGLKV EYDTSVRDSD GSMIQFIYGE DGLDVTKQKH LTDFKFILQN
LMSELSQLNY GDPRYDTIFE EKETIIKRMK KALKHAKAND LNGPDPVLSK YNPGKYGYAT
SEKYFETLTN YMKTNPDGLV KDKEHPDGVG PRKALEPVLV AKYLKSIVEP GEAVGIVAGQ
SVGEPSTQMT LNTFHLAGHS SKNVTLGIPR LREIVMTASN HISTPSMTLT LNEELTPDES
EKFAKSISIL SLAEVLDWAT VKERIGRGVA FQQAKIYDIH IKLFPSKEYC ETYAIDIDDV
IFTLQRRFTQ KLQSLTRKAL GRKKVEKAGK AGANTAAVPE IGKSVGTIEE ARPDAERETG
EDDEDDDGED DATNDKRKAN RSEAVSYAAN DDEDDAIQAQ NAEPEDIEDM EDEGIGGSPR
APQSDDEDEG NADNGERRKR KMTAATEELE AQVMKRCQDI TRFRFDQENA EWCDVTLEYD
ADVPKVLMLS IVEDALRSCL IQHIAGIGSC TYDGNNEVKD TKTGKMVKVP VVHTAGVNLK
AMQNYAAFIN PNTISTNDIA AMLVNYGVEA CRSTIVQELH SVFDGHAIAV DMRHLNLIAD
YMTRGGGFSP FNRNGMKGSV SPFMKMSFET TVGFLADAVA ECDWDDLANP SSRIVIGRTS
KVGTGAFDVL TKVPTGKSED EVMEE
//
