ID M5FQ84_DACPD Unreviewed; 1770 AA.
AC M5FQ84;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=DACRYDRAFT_118311 {ECO:0000313|EMBL:EJT99020.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT99020.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJT99020.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT99020.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH795871; EJT99020.1; -; Genomic_DNA.
DR STRING; 1858805.M5FQ84; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OMA; MVQYDRT; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000030653; 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; 11.
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; 1.
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:UP000030653};
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 246..546
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1770 AA; 196128 MW; FFE073BBD2B157E8 CRC64;
MSMFAQTVTY SAAPVHKVRE VQFGIMSPEE IKAYSVAKIE HSEVMDESGY RPRVGGLMDP
RMGTIDRNYK CQTCGEGPGD CPGHFGHIEL ARPVYHAGFL VKVKKILECI CVNCGKLKAD
IGDDTFRVLV KRADNPKRRL QIVWEYCKGK MLCESDDMKE EEEDPEKPQK PSHGGCGHIQ
PLIRKDGLKL FLVYKKRKGD DDDEDVKLAQ PEKRLLTAAE AHSILRKIPT SDLRLMGLSE
RYARPEWMIL SVIPVPPPQV RPSIMSDSLR SEDDLTYKLA DILKTSATLR KHDAEGAPAH
VVSEIEQLLQ FHVATYMDNE IAGQPRAMQK SGRPVKAIRS RLKGKEGRLR GNLMGKRVDF
SARTVITGDP NIALDEVGVP RSIAMTLTYP ERVTKYNLER LTELVRNGPV EYPGARYIIR
DTGERIDLRY KRGDVSLQIG WVVERHLRDG DYVLFNRQPS LHKMSMMSHR VRVMPYSTFR
LNLSVTSPYN ADFDGDEMNL HVPQSEETRA ELKEIAWVPR QIVSPQANKP VMGIVQDTLC
GIYKMTQRDI FLDWPLVQNI LLWVPDWDGT IPHPCIIKPK PMWSGKQIIA LVIPQGINLA
NGNLSIGNPI NDDALIIENG EIMMGIFNKG IVGSSAGGLI HVVFRERGPE VTRDMIGGIQ
TVVNYWLFHN GFSIGIGDTV PDKPTEKSIM TNIETAKEDV RKVVEEAVKG LLKPRPGMTI
RESFEASVNG ILNQVRDKSG KSAQQSLKRD NNVKTMVTAG SKGSFINISQ MSAMVGQQNV
EGQRIPFGFK HRTLPHFTKD DFSPESRGFV ENSYLRGLTP QEFFFHAMAG REGLIDTAVK
TAETGYIQRR LVKAMEDVMV AYDGTIRNSL GDVLQWTYGE DGMDAAHVEE QKMSLLTISD
AVFQKSFRVD ILAGAGAGFS RNALQVGIID PKKEFDVQKR LDEEFQQLQD DRRLLRTFIF
PNGPPKRLVL PVPISRIVQN AKAAFEIDRR RSSDLDPVYI IDEVKALCTR LKVVPGEHAL
AMRMQQDATL LFQIMLREQL AVRRVIEEHR LQKVAFDFIV GEIEQQFLRA RAHAGEMCGV
LAAQSIGEPA TQMTLNTFHY AGVSSKNVTL GVPRLKEIIN VATHLKTPRL KVYLDPNVAI
SPEASKAVLT ELAHATLRTI TKSTEIYYDP EPSTTRIEED RDFVEAFFSI PDEEVEQKMN
LQSPWLLRLE LDRAQILDKK LEMSYVASKI SEAFQSDIFV IWSEDNAEKL IIRCRVINNQ
SDKDESGNIE EDVFLRKLEN TMLNSISLRG VDGISRAFMV QDSKTVLTPE GDYRTDKDDW
MLETEGINLK KVLCVEGVDA TRTTTNSLLE GFEVLGIEAA RAVLLTELRE VLEFDGSYVN
FRHLALLCDI MTYRGTLMSI TRHGINRTDA GALMRCSFEE TVEILFEAAA MGEKDDCRGI
AQNIMFGQVA PLGTGAFDVY LDMDMLKDVP IDEAITAAEF TMDGGMTPAA GSMTPYDRSP
VYEGGFRAEA AAFSPLVMAG ADETSQFSYR ATLGQSPLGA GLGGASPGYA PTSPAYSPTS
PFVPTSPGYT SGATSPFITS PLGAGATSPF YDPRRTAAMA TSPTYSPTSP ALQMTSPAYT
PTSPAYTPTS PNFSPTSPSF SPTSPNPRAA TGYSPTSPQY SPTSPQYSPT SPQYTPTSPQ
YSPTSPHLSP TSPRYSPTSP VHGASTQFSP TSPAMMSPTS PSYSPASPAY SPTSPAYEGA
ASPARGNQQN GQNTSGYASK QKFQASPSWE
//
