ID A0A0D9XW28_9ORYZ Unreviewed; 1800 AA.
AC A0A0D9XW28;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR12G00550.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR12G00550.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR12G00550.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR12G00550.1}
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; 77586.A0A0D9XW28; -.
DR EnsemblPlants; LPERR12G00550.1; LPERR12G00550.1; LPERR12G00550.
DR Gramene; LPERR12G00550.1; LPERR12G00550.1; LPERR12G00550.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR Proteomes; UP000032180; Chromosome 12.
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 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; 6.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000032180};
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 234..526
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1570..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1689..1800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 673..700
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1689..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1800 AA; 201564 MW; D1F48F87F92DD2BF CRC64;
MDARFPYSVA EVELVQFGIL SPDEIRQMSV LQIEHAETME RGKPKPGGLS DPRLGTTDRK
IKCETCMAGM AECPGHFGHL ELAMPMFHIG FIKTVLSIMR CVCFNCSKIL ADEVNPKFKQ
ALKIRNPKNR LKRIYDACKS KKFCALDVQE LQNTDEPVKR RDVCGAQQPN ISVDGMKMVA
EFKALKKSDD QEQLPEPVER KQILSAERVL NVLKRISDDD CHLLGLNPKF ARPEWMILQV
LPIPPPPDDL THQLASIIRH NENLRRQERN GAPAHIITEF AQLLQFHIAT YFDNELPGQP
RATQRSGRPI KSICSRLKAK EGRIRGNLMG KRVDFSARTV ITPDPNINID ELGVPWSIAL
NLTYPETVTP YNIERLKELV EYGPHPPPGK TGAKYIIRED GQRLDLRYVK KSSDQHLELG
YKVERHLNNG DFVLFNRQPS LHKMSIMGHR IKIMPYSTFR LNLSVTSPYN ADFDGDEMNM
HVPQSFENRA EVSELMMVPK CIVSPQSNKP VMGIVQDTLL GCRKITTRDT LIEKDVFMNI
LMWWEDFDGK VPAPAILKPR PIWTGKQVFS LIIPKPINLI RFSAWHSETE TGFITPTDTM
VRIEKGELLS GTLCKRHLEH QLEALFMLFG KEEVGPDAAC KFLGHTQWLV NYWLLQNGFS
IGIGDTIADA ATIEKINDTI SKAKSDVKEL IKQAHDKQLE AEPGRTMMES FENKVNEVLN
KARDAAGTSA EKSLPESNNL KAMATAGSKG TFINISQMTA CVGQQNVEGK RIPFGFVDRT
LPHFTKDDYG PESRGFVENS YLRGLTPQEF FFHAMGGREG LIDTAVKTSE TGYIQRRLVK
AMEDIIVKYD GTVRNSLGDV IQFLYGEDGM DAVWIEPQQL DSLKMKKAEF DNVFRYELDD
ENWRPNYMLP KHVDDLKTIH EIRNVFEAEV QKLEADRFQL GTEIATTGDN TWPMPVNLKR
LIWNAQKTFK IDLRRPSDMH PMEIVDAIDK LEERLKVVPG DDAMSIEAQK NATLFFNIML
RSTFASKRVL KEYRLTKEAF EWVIGEIESR FLQSLVAPGE MIGCVAAQSI GEPATQMTLN
TFHYAGVSAK NVTLGVPRLR EIINVAKKIK TPSLSVYLKP EVNERELAKN VQCALEYTTL
RSVTHATEIW YDPDPMETII EEDVEFVRSY YEMPDEDIDP DKISPWLLRI ELNREMMVDK
KLSMADIAEK INHEFDDDLS CIFSDDNADK LILRVRITND EAPKGVIQDE FAEDDVFLKK
IESNMLTEMA LRGIPDINKV FIKHGKVNKF KDDDGFKSDE EWMLDTEGVN LLAVMCHEDV
DATRTTSNHL IEVIEVLGIE AVRRALLDEL RAVISFDGSY VNYRHLAILC DTMTYRGHLM
AITRHGINRN DTGPLMRCSF EETVDILLNA AVYAESDYLR GVTENIMLGQ LAPIGTGGCT
LYLNDQMLQQ AIELQLPSSV EGLDFGTTPA LSPISRTPYH EGMMSPNSLQ SPDIRASPIT
DAQFSPYAGG MAPFSPVASP ACYYTPSSGG DNNPCSPVYI PTSPIYRPVS PIYTPISPIW
TPASPIYTPT SPSSYTTPDS STYSPNTSSS YLPTRGSSYS PTSPIYSPTS PIYSPTSPIY
SPTSPVYSPT SVSYSPTSPV YSPTSHAYSP TSPAYCPTSP SYSLAPLSYS PTSPSFNCPS
YSPTSPSYSP TSPLYSPTSL SYSPTSPAYS PTSPGYSPTS PSYSPTSPNY NLTSPNYSPT
SPAYSPTSPS NSQPSPSYSP TSPYTTSGGP SPDYCPTSPN YSISVEEKTE EEASKDEAEI
//
