ID D7MC36_ARALL Unreviewed; 1839 AA. AC D7MC36; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 04-NOV-2026, entry version 75. DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279}; DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279}; GN ORFNames=ARALYDRAFT_491060 {ECO:0000313|EMBL:EFH43311.1}; OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=81972 {ECO:0000313|EMBL:EFH43311.1, ECO:0000313|Proteomes:UP000008694}; RN [1] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; RX PubMed=21478890; DOI=10.1038/ng.807; RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M., RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G., RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K., RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J., RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y., RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.; RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size RT change."; RL Nat. Genet. 43:476-481(2011). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GL348719; EFH43311.1; -; Genomic_DNA. DR STRING; 81972.D7MC36; -. DR Gramene; fgenesh2_kg.7__493__AT4G35800.1; fgenesh2_kg.7__493__AT4G35800.1; fgenesh2_kg.7__493__AT4G35800.1. DR eggNOG; KOG0260; Eukaryota. DR HOGENOM; CLU_000487_1_0_1; -. DR OMA; AAKFHID; -. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:EnsemblPlants. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC. 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 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; 2.40.40.20:FF:000018; 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:000002; 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; 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; 14. 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:UP000008694}; 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..550 FT /note="RNA polymerase N-terminal" FT /evidence="ECO:0000259|SMART:SM00663" FT REGION 153..175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1539..1839 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 153..163 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1539..1727 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1728..1746 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1748..1799 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1819..1839 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1839 AA; 204645 MW; 64A656AD9D8F6BC5 CRC64; MDTRFPFSPA EVSKVRVVQF GILSPDEIRQ MSVIHVEHSE TTEKGKPKVG GLSDIRLGTI DRKVKCETCM ANMAECPGHF GHLELAKPMY HVGFMKTVLS IMRCVCFNCS KILADEVCRN LSRQAMKIKN PKNRLKKILD ACKNKTKCEG GDDIDDVQNQ DTDEPVKKSR GGCGAQQPKL TIEGMKMIAE YKIPRKKNDE PDQLPEPAER KQTLGADRVL SVLKRISDED CQLLGFNPKF ARPDWMILEV LPIPPPPVRP SVMMDATSRS EDDLTHQLAM IIRHNENLKR QEKNGAPAHI ISEFTQLLQF HIATYFDNEL PGQPRATQKS GRPIKSICSR LKAKEGRIRG NLMGKRVDFS ARTVITPDPT INIDELGVPW SIALNLTYPE TVTPYNIERL QELVDYGPHP PPGKTGAKYI IRDDGQRLDL RYLKKSSDQH LELGYKVERH LQDGDFVLFN RQPSLHKMSI MGHRIRIMPY STFRLNLSVT SPYNADFDGD EMNMHVPQSF ETRAEVLELM MVPKCIVSPQ ANRPVMGIVQ DTLLGCRKIT KRDTFIEKDV FMNTLMWWED FDGKVPAPAI LKPRPLWTGK QVFNLIIPKQ INLLRYSAWH ADTETGFITP GDTQVRIERG ELLAGTLCKK TLGTSNGSLV HVIWEEVGPD AARKFLGHTQ WLVNYWLLQN GFTIGIGDTI ADSSTMEKIN ETISNAKTAV KDLIRQFQEK KLDPEPGRTM TETFENRVNQ VLNKARDDAG SSAQKSLAET NNLKAMVTAG SKGSFINISQ MTACVGQQNV EGKRIPFGFD GRTLPHFTKD DYGPESRGFV ENSYLRGLTP QEFFFHAMGG REGLIDTAVK TSETGYIQRR LVKAMEDIMV KYDGTVRNSL GDVIQFLYGE DGMDAVWIES QKLDSLKMKK SEFDRTFKYE IDDENWNPTY LSDEHLEDLK GIRELRDVFD AEYSKLETDR FQLGTEIATN GDSTWPLPVN IKRHIWNAQK TFKIDLRKIS DMHPVEIVDA VDKLQERLLV VPGDDALSVE AQKNATLFFN ILLRSTLASK RVLEEYKLSR EAFEWVIGEI ESRFLQSLVA PGEMIGCVAA QSIGEPATQM TLNTFHYAGV SAKNVTLGVP RLREIINVAK RIKTPSLSVY LTPEASKSKE GAKTVQCALE YTTLRSVTQA TEVWYDPDPM STIIEEDFEF VRSYYEMPDE DVSPDKISPW LLRIELNREM MVDKKLSMAD IAEKINLEFD DDLTCIFNDD NAQKLILRIR IMNDEGPKGE LQDESAEDDV FLKKIESNML TEMALRGIPD INKVFIKQVR KSRFDEEGGF KTSEEWMLDT EGVNLLAVMC HEDVDPKRTT SNHLIEIIEV LGIEAVRRAL LDELRVVISF DGSYVNYRHL AILCDTMTYR GHLMAITRHG INRNDTGPLM RCSFEETVDI LLDAAAYAET DCLRGVTENI MLGQLAPIGT GDCELYLNDE MLKNAIELQL PSYMDGLEFG MTPARSPVSG TPYHEGMMSP NYLLSPNMRL SPMSDAQFSP YVGGMAFSPS SSPGYSPSSP GYSPTSPGYS PTSPGYSPTS PGYSPTSPTY SPSSPGYSPT SPAYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PAYSPTSPAY SPTSPAYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPAYS PTSPGYSPTS PSYSPTSPSY GPTSPSYNPQ SAKYSPSIAY SPSNARLSPA SPYSPTSPNY SPTSPSYSPT SPSYSPSSPT YSPSSPYSSG ASPDYSPSAG YSPTLPGYSP SSTGQYTPHE GEKNAKTGKD VSKDDKSNP //