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Database: UniProt
Entry: A0A137QQM0_9AGAR
LinkDB: A0A137QQM0_9AGAR
Original site: A0A137QQM0_9AGAR 
ID   A0A137QQM0_9AGAR        Unreviewed;      1699 AA.
AC   A0A137QQM0;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-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=AN958_05429 {ECO:0000313|EMBL:KXN89562.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN89562.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN89562.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN89562.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-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; KQ962079; KXN89562.1; -; Genomic_DNA.
DR   STRING; 1714833.A0A137QQM0; -.
DR   OrthoDB; 169836at2759; -.
DR   Proteomes; UP000070249; 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; 6.10.250.2940; -; 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:UP000070249};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          350..693
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          147..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1118..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1372..1478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1389..1427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1428..1452
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1457..1478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1699 AA;  190340 MW;  554DC707A5850361 CRC64;
     MNIAHSLPST VASIGFSFLT TQDVRRISVK QIVNPVLLDD LNRPNIGGLY DPALGPSDRS
     DICTTCRLTY FTCPGHYGHI ELPAPVFHPL FMGNMYNLLR GCCMFCHRFK MGRTTLCKYT
     AKFRLLERGL LEAAQGIDDI QLRARKRKTK ARGEDEEEEE TVDTGLPDET PQEFMTRINL
     YVAIHLSRAK GNTRDDYKDG LVYQARKELI NDFLKNTLIK KCQNGDCNSV AYTYRKEGYT
     KIIEYDLSPK QKASLTRKRP DVLLAEKTGN FTLLQQSKPA VDSAVDMDGS QAGEMKTARG
     RNERVVAPEE CRAHLRRLFR NEAVACSLIF GRHGPFAPLS HEQLSYASAD MFFMEVIPVS
     PTRFRPPAKM GETLFEHAQN ELLSRVLSTS YRMRDINVEL RALQQKKDEP IDENTRRTLL
     ASLLERLVQL QVDVNSFVDS SKNPQPVRQG KLPPPGVKQG LEKKEGLFRK HMMGKRVNYA
     ARSVISPDVN IEPNEIGVPP VFARKLTFPE PVTPANFHEM RQRVIIGPHG YPGASMVEYE
     DGHQQSLDKL TVEQRTAIAN QLLTPQEGER AASGRKGLHT RTPAINKKVY RHLKDGDILI
     LNRQPTLHKP SMMAHKAKVL KGEKTIRMHY ANCNSYNADF DGDEMNIHFP QNHVARAEAM
     MIANTDNQYL VPTSGNPLRG LIQDHVVAGV WMTSQDAFFS REEYFQLLYG ALRPEDEDYC
     ASGRLETLPP TIWKPKPLWT GKQIISTILK NITPPQYKGL NLNAKTKVPG FLWGKDSKED
     KVVFMDGELL CGVLDKAAFG ASDYGLVHSV YELYGADIAG KFLGILSRLF TKFLQHRAFT
     CRMDDLVLTP EGDHKRDELL EKGKNLGTEA AIENFPSLKN IPTSEIPVAL EALLQDVLRD
     DNKMAGLDMT VKTKLSKLTS SISDACLPNG LLRKFPHNHM QTMTQSGAKG SAVNARQISC
     GLGQQELEGR RVPVMISGKT LPSFRPFETK AIAGGYVASR FLTGIKPQEF YFHCMAGREG
     LIDTAVKTSR SGYLQRCLIK HLEGIHVHYD HTVRGSDNSV YQFTYGGDAL DVTKQKHLCQ
     FNFIAQNEES LVMRLQPGRV ADAVDNSAAL SYMKKVLKRS TEHPRRGEPS KRDKYDPALS
     TYSPSRFLGA TSEQFAVAVD NYMKGNTSGL LEKKGEEEFF KRRHEKMTAY NFKMLVNVKY
     MRSLVEPGEA VGLLASQGVG EPSTQMTLNT FHFAGHGAAN VTLGIPRLRE IVMTASQKPK
     TPSMTMTIRK GVPQAEIDLF CKRASRVALS QLVENVIVRE TSKVEGQARR TVFSIDINFF
     PQDEYTKEHD VEPSEILNVF AVRFPLTLKK EIANEMKRLD ADLKSQIAEL GKGKKVSERE
     GGDGDVDEES EEAPKKRRGD DEESEVGDGD AGDEKRARQK KQQATYESDE DEDEDEPEGE
     YDDAEIEAAY AEDQDTMEVG SDEKKKKKKP SSLEEEASRV ADTFTSHLHH AISFTFTPSQ
     CNFELEFTTD VPKLLFVGII ERTCRASVIR EIPGITDCFQ TKDDNKKEPE IKLTTNGSNL
     RGMWEFAAGS GESILEDEEI YSNDIYAILK TYGVEMARAA ILREMGGVFG AYNIQVDRRH
     LELIADYMTF EGGYKPFNRK GISTSPSPLL KASYETTAAF LSDATLYGDF DDLSTPSGNI
     VLGRPNATGT GVFDVVMPV
//
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