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Database: UniProt
Entry: A0A0D9ZUB7_9ORYZ
LinkDB: A0A0D9ZUB7_9ORYZ
Original site: A0A0D9ZUB7_9ORYZ 
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
//
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