ID A0A0D9ZUB7_9ORYZ Unreviewed; 1824 AA.
AC A0A0D9ZUB7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM05G03530.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM05G03530.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM05G03530.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 STRING; 40148.A0A0D9ZUB7; -.
DR EnsemblPlants; OGLUM05G03530.1; OGLUM05G03530.1; OGLUM05G03530.
DR Gramene; OGLUM05G03530.1; OGLUM05G03530.1; OGLUM05G03530.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR Proteomes; UP000026961; 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:0009536; C:plastid; IEA:UniProtKB-KW.
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 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; 8.
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 Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
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 251..543
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1630..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1824 AA; 204024 MW; EB59628B47D1D4A8 CRC64;
MGLIIFRVIR FNRLSASLNA RTQKLHVECV RNTNFGMRHM SVVHIEHAET MEKGKPKPGG
LSDPRMGTID RKIKCETCMA GMAECPGHFG HLELAKPMFH IGFIKTVLSI MRCVCFNCSK
ILADEDDIKF KQALKIRNPK NKLKRIYDAC KNRKICAGGD NLDVQEQQGT DDPVKKRGGC
GAQQPNITVD GMKMVAEYKA PKKKNDDQEQ LPEPVDRKQI LSAERVLNVL KHISDEDCLL
LGLNPKFARP DWMILQVLPI PPPPDDLTHQ LAMIIRHNEN LRRQERNGAP AHIITEFAQL
LQFHIATYFD NELPGQPRAT QRSGRPIKSI YSRLKAKEGR IRGNLMGKRV DFSARTVITP
DPNINIDELG VPWSIALNLT YPETVTPYNI ERLKELVEYG PHPPPGKTGA KYIIREDGQR
LDLRYVKKSS DQHLELGYKV ERHLNDGDFV LFNRQPSLHK MSIMGHRIKI MPYSTFRLNL
SVTSPYNADF DGDEMNMHVP QSFETRAEVL ELMMVPKCIV SPQSNRPVMG IVQDTLLGCR
KITKRDTLIE KDVFMNILMW WEDFDGKVPA PAILKPRPIW TGKQVFNLII PKQINLIRFS
GWHSEAETGF ITPGDTMVRI EKGELLSGTL CKKTLGTSTG SLIHVIWEEV GPDAARKFLG
HTQWLVNYWL LQNGFSIGIG DTIADAATME NINETISKAK NDVKKLIKQF RDNQLEAEAG
RTTMESFENR VNEVLNKARD VAGSSAEKSL SESNNLKAMA TAGSKGTFIN ISQMTACVGQ
QNVEGKRIPF GFTNRTLPHF TKNDYGPESR GFVENSYLRG LTPQEFFFHA MGGREGLIDT
AVKTSETGYI QRRLVKAMED IMVKYDGTVR NSLGDVIQFL YGEDGMDAIW IESQKLDSLK
MKKADFDNVF RYELDDENWK PNYLSTQHAE DLKTISEIRN VFEAEVQKLE ADRFQLGTEI
ATTGDNTWPM PVNLKRLIWN AQKTFKIDLR RPSDMHPMEI VDAIDKLQER LKVVPGDDDI
SIEAQKNATL FFNILLRSTF ASKRVLKEYR LTKEAFEWVI GEIESRFLQS LVAPGEMIGC
VAAQSIGEPA TQMTLNTFHY AGVSAKNVTL GVPRLREIIN VAKNIKTPSL SVHLKPEVNK
KKELAKNVQC ALEYTTLRSV THATEIWYDP DPLGTIIEED AEFVQSYYEM PDEDIDPDKI
SPWLLRVELD REVMVDKKLS MADIAEKINH EFDDDLSCIF NDDNAHKLIL RVRITNDEAQ
KGEIQDEYGE DDVFLKKIES NMLTEMALRG IPGINKVFIK EGNVNKFEDN DGFKTEKGWM
LDTEGVNLLA VMCHEDVDAT RTTSNHLIEV IEVLGIEAVR RALLDELRVV ISFDGSYVNY
RHLAVLCDTM TYRGHLMAIT RHGINRNDTG PLMRCSFEET VDILLDAAVY AESDPLRGVS
ENIMLGQLAP IGTGGCDLYL NDQMLKQAIE LQLPSYVEGL DFGMMTPACS PISGTPYHQG
MMSPSYLLSP DIRASPTAAD AQFSPYVGGM AFSPVSSPGN YTPSSGGGYS PSPPVCTPGP
GSFTSSSPYN PVSPFYSPAS PLSCPLTSPS YVPTSLPYSP TSPIYSATSP IYSPSSPIYS
PTSLSYSPTS PVYSPTSPVY NPTSSAYSPT SPSYSPTPPS YSYSPTSPSY SPTSPSYSYS
PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPAYSPTSPG YSPTSPSYSP SSPSYNPSSV
KYTPSHAYSP SSPNYYSSTS PTYSPTSPSY SQPSPSYSPT RILGFYLIIK DAGNFIILEK
VPRVEWKKKR MRRLKRKSQK DEAI
//