ID A0A0E0HTF3_ORYNI Unreviewed; 1666 AA.
AC A0A0E0HTF3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA06G24660.2};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA06G24660.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA06G24660.2};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA06G24660.2}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA06G24660.2};
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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR STRING; 4536.A0A0E0HTF3; -.
DR EnsemblPlants; ONIVA06G24660.2; ONIVA06G24660.2; ONIVA06G24660.
DR Gramene; ONIVA06G24660.2; ONIVA06G24660.2; ONIVA06G24660.
DR eggNOG; KOG0262; Eukaryota.
DR OMA; NREDYQQ; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR CDD; cd01435; RNAP_I_RPA1_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; 3.30.70.2850; -; 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; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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; 2.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000006591};
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 305..617
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 148..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1666 AA; 187253 MW; 5FD75E439E4D4FCF CRC64;
MADVRPDEAA SEEVNSIHFS FYNDDEIKRI SVKQITKSDR VDAKNCPVPG GLLDPAMGPM
NDTDTCKSCG QQSIRCPGHF GHIELAKPLF NPLLFMSLKN LLQVTCFHCH KFRLNKEQVD
RYTNELELLV RGDIAHAKNL EDLGGKVLSK EDDETEATSG DKSARSEREN KTWTSIQLKE
ALSIFSKLMK KRQKKCAHCE KKNPIIKNPI YGWLIKDTTS SSVRANAIAN AKLSGDGHVN
DSRETGVSGL DEELTSPGTL SRRSTNETRR ISDDTIKEMV ASSGKKHLLT TENTLSVSEK
RRGYEMFFLK NLLVAPNRFR PSISSSLGIM EHPQNVLLSK VQESNLALQQ SIAASNHMEV
LRRWMDLQRN VNVLYDSTKN EKNANGIRQL LEKKEGILRQ KMMGKRVNYA CRSVISPDPY
LAVNEIGIPP VFATRLTYPE KVTPWNARKL QEAINNGADI HPGATHYRDN NNMYKLQAAP
PKRRAIAKML PASRGSISQP GKDPKCEFES KVVYRHLQDG DVVLVNRQPT LHKPSMMAHV
VRVLPGEKTI RMHYANCSTY NADFDGDEMN VHFPQDEISR AEAINIVDAN KQYIGPRSGD
AVRGLIQDHI IGAVLLTKLD TLLSREEYNQ LVYGSVLSST RRSGQFGKKI SIIMDDDALE
PVPPAIWKPK PLWTGKQVIT TILNHVTKGR PPFTVEKKGR IEKEYLIPEE RNGDKVKTIN
PSEQVLYVHD NELIKGMIDK AQFGNYGIVH TVHELYGPET AGVLLSSFSR LFTMVLQLHG
FTCGVDDLLL SQESDMTREE ILGKSEKHSK IVHINFTRPK KDDKAEAKAE DIRPKEGDEA
EDTRPKEGDE AEDTRPKEDH EAEDSTHPKE DHEAEDSTHP KEDHEAEGDD EDQMKLQMEV
EKIIRRNGES ATVILDRNMS SELNTLTSKV NKKVFPYGLR KPFPGNCLSL MTQTGAKGGL
VNMTQISSLL GQQELEGKRV PRMISGKTLP CFPPWDTSSR AGGFIGDRFL TGLRPQEYYF
HCMAGREGLV DTAVKTSRSG YLQRCLIKSL ESLKVSYDHT VRDVDGSIIQ FCYGEDGVDV
LKTSFLDDKF RELSDNRRAL LGKLDSHNDK HLLLNPNGYI SELPEKLIEN AMEFLKSKRN
EKGRYDIKEK ELMKLLKVKY ISSLVDPGEA VGVVAAQSIG EPSTQMTDDD EEEMDDKLKK
ARDAERLAAK LRTIDDAERI AAKLRRVRVA DIVERIEVCT VPFHNNNGCV STLYKLQLKL
YPQGLYPRQS ELTVEECHET LRTVFIDAMD LAISKHLDLL HKINEIQAVK SNDMESQRSD
GVEESENGPT DEDNGVSDGE NEDDLGADAE KWKRQEIDEM EYDDDAEKEE GFDMDSESEE
DTKSKPESEG HQAKLDEELE ESEEGHVLDS SNKGENLKAK QATARLEDEM NEAEDEKAQV
TIKFKKNIKW TIHYESTGLN FEVHYALQEQ PHILLAQIAQ RTARSVFVKA CKNIDRCEVN
KPKKIDNNTI NTPITLQTAG VNFEVFHKLV DYLDINEVRS NDIHAMLNTY GVEAARATII
EEVKGVFGAY GIHVDMRHLN LIADFMTFDG GYRPMSRLGM GQFSTSPFGK MTFETATKFI
VEAASHGESD TLDGPSASVC LGKPVKVGTG SFGLLQNFSL EQPVAM
//
