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Database: UniProt
Entry: A0A1Q3E6A4_LENED
LinkDB: A0A1Q3E6A4_LENED
Original site: A0A1Q3E6A4_LENED 
ID   A0A1Q3E6A4_LENED        Unreviewed;      1773 AA.
AC   A0A1Q3E6A4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   28-JAN-2026, entry version 35.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=LENED_004433 {ECO:0000313|EMBL:GAW02765.1};
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW02765.1, ECO:0000313|Proteomes:UP000188533};
RN   [1] {ECO:0000313|EMBL:GAW02765.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW02765.1,
RC   ECO:0000313|Proteomes:UP000188533};
RG   Lentinula edodes genome sequencing consortium;
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW02765.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW02765.1,
RC   ECO:0000313|Proteomes:UP000188533};
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RT   "A genome survey and senescence transcriptome analysis in Lentinula
RT   edodes.";
RL   Submitted (FEB-2017) 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=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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:ARBA00048552,
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|ARBA:ARBA00006460, 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:GAW02765.1}.
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DR   EMBL; BDGU01000112; GAW02765.1; -; Genomic_DNA.
DR   STRING; 5353.A0A1Q3E6A4; -.
DR   Proteomes; UP000188533; Unassembled WGS sequence.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IEA:TreeGrafter.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:UniProtKB-ARBA.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:UniProtKB-ARBA.
DR   CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR   CDD; cd02733; RNAP_II_RPB1_N; 1.
DR   FunFam; 2.40.40.20:FF:000019; DNA-directed RNA polymerase II subunit RPB1; 1.
DR   FunFam; 1.10.132.30:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR   FunFam; 1.10.150.390:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR   FunFam; 1.10.274.100:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR   FunFam; 3.30.1360.140:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR   FunFam; 3.30.1490.180:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR   FunFam; 4.10.860.120:FF:000003; DNA-directed RNA polymerase subunit; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.1360.140; -; 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; 2.
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; IPR000684; RNA_pol_II_repeat_euk.
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; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   NCBIfam; NF006336; PRK08566.1; 1.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   Pfam; PF05001; RNA_pol_Rpb1_R; 3.
DR   SMART; SM00663; RPOLA_N; 1.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 2.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU004279}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188533};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          243..546
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          152..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1545..1568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1598..1662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..165
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1545..1555
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1556..1568
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1601..1618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1619..1662
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1773 AA;  198084 MW;  CFFB9C5C54A8C0D2 CRC64;
     MLGHQFAFSA APVRRVKEVQ FGILSPEEIK AYSVAKIEHP EVMDEGTHKP KMGGLMDPRL
     GTIDRNFKCQ TCGEGMAECP GHFGHIELAR PVFHPGFIIK VKKILECICV NCGKLKADIA
     DPNFADKIRH VRDPKKRMAV VWSHCKSKMV CEPDDPKEEG AEPEPEDTKK GHGGCGHIQP
     LVRKEGLKLF LQYKKPKDDD EEIKSMQPDK RLMTPQEVYT TFKKMSDSDL HLIGLSEEFA
     RPEWMILTVM PVPPPPVRPS IAVDGGAMRS EDDLTYKLGD IIKASANVRR CEQEGAPAHV
     ITEFEQLLQF HVATYMDNDI AGIPQALQKS GRPVKAIRAR LKGKEGRLRG NLMGKRVDFS
     ARTVITGDPN LELDEVGVPR SIAMNLTFPE RVTPYNITYL QELVRNGPTT YPGARYVVRD
     TGERIDLRYN KRADAFLQYG WVVERHLKDG DFVLFNRQPS LHKMSMMSHR VRLMPYSTFR
     LNLSVTPPYN ADFDGDEMNM HVPQSEETRA ELSQIAWVAR QIISPQANKP VMGIVQDTLC
     GIRKFTLRDS FLDWNQVQNI LLWVPEWDGS VPIPAILKPK PLWTGKQILS LVIPRGINIH
     RSPDPKSSNP VFDDGMLIEN GEIIFGIVEK KTVGASQGGL VHVVFREKGP EVTRQLFTGL
     QTVVNYWLFH NGFSIGIGDT IADKNTMSYI TETIASRKAN VSKIIEDATH DRLKPAPGMT
     IRESFESLVE RELNLARDTS GQHAQKSLKE DNNVKQMVVA GSKGSFINIS QMSVCVGQQS
     VEGRRIPFGF RHRTLPHFTK DDFSPESRGF VENSYLRGLT PQEFFFHAMA GREGLIDTAV
     KTAETGYIQR RLVKALEDVM VCYDGTVRNS LGDLIQFVYG EDGMDGAFIE KQNIDTFSLN
     DREFEHNYRV DVTDPAGGFL PGVLQVGIDD SSLELQNKLD EEYDQLLSDR RLLREFIFPQ
     HATSFNQYLP VNLSRIVQNA AQIFHIDRRK PSDLDPAFII DSVKTLCDRL VVVRGDGPLS
     HEAQANATLL FRMHLRATFG CRRVLERFHL NKEAFEWVLG EVEAKFNQSV ANPGEMCGTL
     AAQSIGEPAT QMTLNTFHYA GVSSKNVTLG VPRLKEIINV ATNIKTPSLS VYLEPALRFD
     PNLAKNVQQE LAYTSLRTVT AAVEIWYDPD PSSTIIEEDE VFVESFFAIP DEEVESKLHL
     QSPWLLRLEL DRAKMLDRKL TMAYVASRIA ESFKTDLFVI WSEDNAEKLV IRCRVLGGAD
     KDEDGTETLE EDIFLRQLEN TMLNSVSLRG VQGINRVFLT RHDLVETKDD GSIVAEKDKQ
     WVLETDGVNL KTVMCIDGVD FTRTYSNSCV EVFNVLGIEA ARAAILKELR GVIEFDGSYV
     NYRHLALLCD LMTHRGSLMA ITRHGINRAD TGALMRCSFE ETVEILMEAA AVGEKDDCHG
     VAENVMFGQM APMGTGAFDV ALDIDMLKDA IVDHRLPVQS MLAAQVDGGM TPGQVAMTPY
     DTNSPMWDNH LFKGSDQAAF SPLAVNSNEE SGNFNYLPWG QSPRGAGGMS PGGPGYSPSS
     PNAYSPNSPA FAPTSPFGGG ATSPMVYGGT SPYYDPGRGV TSPTYSPTSP AFNPTSPAFS
     PTSPRYSPTS PSFSPTSPRY SPQSPSFSPT SPRYSPTSPS FSPASPRLFT LCVFIRFADR
     SSSTRNFIFQ LPLRNYLLHP LDIHPLLRWP RQLRPDILLL LPRTLLRRPL TPPHLPHTVL
     HLHYAHPRAL LRTGPLTAVT HTSHLLLGID QSW
//
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