ID A0A2A9NJ26_9AGAR Unreviewed; 1749 AA.
AC A0A2A9NJ26;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=AMATHDRAFT_65885 {ECO:0000313|EMBL:PFH48291.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH48291.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH48291.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH48291.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) 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|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; KZ302069; PFH48291.1; -; Genomic_DNA.
DR STRING; 703135.A0A2A9NJ26; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000242287; 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:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_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; 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 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; 14.
DR PRINTS; PR01217; PRICHEXTENSN.
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};
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:UP000242287};
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 244..547
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 153..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1749 AA; 194593 MW; 810869A51029EC55 CRC64;
MLGHQFAYSA APIRKVKEVQ FGILSPEEIK AYSVAKIEHP EVMDETTHKP KTGGLMDPRM
GTIDRNFKCQ TCGEGMSECP GHFGHIELAR PVFHPGFIIK VKKILECICV NCGKLKADIL
DPNFADKIRH IRDPKARMAV VWNHCKTKMI CDPDEPKEEG AEGENDEQSK KGHGGCGHVQ
PQIRKEGLKL FVQYKKAKDD DEDIKSLQPD KRLFTPSEVY TTFKKMSDSD LHLLGLSDEY
ARPEWMILTV MPVPPPPVRP SIAVDGGAMR SEDDLTYKLG DIIKASANVR RCEQEGAPAH
VINEFEQLLQ FHVATYMDND IAGIPQALQK SGRPVKAIRA RLKGKEGRLR GNLMGKRVDF
SARTVITGDP NLELDEVGVP RSIAMNLTYP ERVTPYNIAY LQELVRNGPT TYPGARYVVR
DTGERIDLRY NKRADAFLQY GWIVERHLKD GDYVLFNRQP SLHKMSMMAH RVKLMPYSTF
RLNLSVTPPY NADFDGDEMN MHIPQSEETR AELAQIAWVP RQIISPQANK PVMGIVQDTL
CGIRKMTLRD TFLDWNQVQN ILLWVPDWDG SVPIPAILKP KPLWTGKQIL SLTIPRGINI
HRSPDPKSSN PVFDDGMLVE NGEIIFGTVE KKTVGASQGG LVHVVFREKG PEATRMLFTG
IQMVVNYWLF HNGFSIGIGD TIADRGTMSY ITQTIAERKS NVTQIIDDAT HDRLKAKPGM
TIRESFESMV ERELNLARDR SGKYAQEHLK EDNNVKQMVV AGSKGSFINI SQMSVCVGQQ
SVEGRRIPFG FRHRTLPHFT KDDFSPESRG FVENSYLRGL TPQEFFFHAM AGREGLIDTA
VKTAETGYIQ RRLVKALEDV MVCYDGTVRN SLGDLIQFVY GEDGMDGAFI EKQTIETFGL
NDKEFEHNYR VDVTDPAGGF LPGVLQIGID DSSLELQAKL DEEYNQLVKD RRVLREFIFP
RSPTSHPHYL PVNLFRIVQN AVQIFHIDRR KPSDLDPAYI VDAVRELGKR LVVVRGDDPL
SREAQENATL MFRMHLRATF ASRRVLEKFH LTREAFDWVL GEVESKFNQS LVHPGEMCGT
LSAQSIGEPA TQMTLNTFHY AGVSSKNVTL GVPRLKEIIN VATNIKTPAL TVYLEPEIAG
SSALAKNVQQ ELAYTSLRTI TAAVEIWYDP DPTSTTIEED QVFVESFFAI PDEEIESKLH
LQSPWLLRLE LDRAKMIDRK LTMHYVASRI AESFKTDLFV IWSEDNSEKL IIRCRVLGGG
DKEDDGMGAI EEDIFLRQLE NTMLNSVSLR GVKGIKRVFL TEQDKVVVAD DGSIRTDYEK
EWVLETDGVN LKTVMCIEGV DFTRTYSNSC VEIFNVLGIE AARAAIMKEL RSVIEFDGSY
VNYRHLALLC DLMTHRGSLM AITRHGINRA DTGALMRCSF EETVEILMEA AAVGEKDDCH
GIAENVMFGQ MAPMGTGAFD VALDIDMLKD AIVDHRLPVQ SMLAAQIDGG MTPGQVAMTP
YDTNSPVWQD GLFKGDQASF SPLASNGGED SANFHYLSYG QSPLGAGGMS PAAPGYSPSS
PNVYSPTSPS FVPTSPFAGA TSPFSTSPYA TSPFYDRSRG PTSPTYSPTS PALNLTSPGY
SPTSPRYSPT SPSFSPTSPR YSPQSPSFSP TSPRYSPTSP SFSPASPRCM SVSPAQMSPS
SPKYSPTSPM ASPTSPKYSP TSPTYSPASP AYSPASPAYS PTSPQWSPSS PAQNGVSRTH
AYQTAPSWE
//
