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Database: UniProt
Entry: A0A3B6N0X9_WHEAT
LinkDB: A0A3B6N0X9_WHEAT
Original site: A0A3B6N0X9_WHEAT 
ID   A0A3B6N0X9_WHEAT        Unreviewed;      1847 AA.
AC   A0A3B6N0X9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   ORFNames=CFC21_080580 {ECO:0000313|EMBL:KAF7075840.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5D02G498900.1};
RN   [1] {ECO:0000313|EMBL:KAF7075840.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7075840.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS5D02G498900.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS5D02G498900.1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS5D02G498900.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7075840.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7075840.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CM022225; KAF7075840.1; -; Genomic_DNA.
DR   SMR; A0A3B6N0X9; -.
DR   STRING; 4565.A0A3B6N0X9; -.
DR   EnsemblPlants; TraesCS5D02G498900.1; TraesCS5D02G498900.1; TraesCS5D02G498900.
DR   Gramene; TraesCLE_scaffold_049682_01G000200.1; TraesCLE_scaffold_049682_01G000200.1; TraesCLE_scaffold_049682_01G000200.
DR   Gramene; TraesCS5D02G498900.1; TraesCS5D02G498900.1; TraesCS5D02G498900.
DR   Gramene; TraesCS5D03G1093100.1; TraesCS5D03G1093100.1.CDS; TraesCS5D03G1093100.
DR   Gramene; TraesKAR5D01G0386720.1; cds.TraesKAR5D01G0386720.1; TraesKAR5D01G0386720.
DR   Gramene; TraesROB_scaffold_078606_01G000100.1; TraesROB_scaffold_078606_01G000100.1; TraesROB_scaffold_078606_01G000100.
DR   Gramene; TraesWEE_scaffold_043890_01G000200.1; TraesWEE_scaffold_043890_01G000200.1; TraesWEE_scaffold_043890_01G000200.
DR   OMA; VMELMMV; -.
DR   OrthoDB; 7998at2759; -.
DR   Proteomes; UP000019116; Chromosome 5D.
DR   Proteomes; UP000815260; Chromosome 5D.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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; 5.
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:UP000019116};
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          246..552
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          158..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1620..1665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1685..1847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          698..725
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1685..1835
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1847 AA;  206051 MW;  68923309C3D679CF CRC64;
     MDARFAYSPA ETARVQLVQF GILSPDEIRQ MSVAVIEHAE TMEKGKPKPG GLSDPRLGTI
     DRRTKCETCM AGMAECPGHF GHLELAKPMF HIGFIKTVLS IMRCVCFNCS KILADEDDEK
     DGKFKQALRI KNPKNRLRKI QEACKGKKVC AAGEDDLEGQ DQMDTDEPVK KRGGCGAQQP
     KITVDGMKMV AEFKATNKKN GDQDQLPEPV ERKQILSAER VLNVLKRISD EDCLLLGLDP
     KYARPDWMIL QVLPIPPPPV RPSVMMDTSS RSEDDLTHQL AMIIRHNENL RRQERNGVPA
     HIITEFAQLL QFHIATYFDN DLPGQPRATQ RSGRPIKSIC SRLKAKEGRV RGNLMGKRVD
     FSARTVITPD PNINIDELGV PWSIALNLTY PETVTPYNIE RLKELVENGP HPPPGKTGAK
     YIIREDGQRL DLRYVKKSSD QHLELGYKVE RHLIDGDFVL FNRQPSLHKM SIMGHRIKIM
     PYSTFRLNLS VTSPYNADFD GDEMNMHVPQ SFETRAEVME LMMVPKCIVS PQANRPVMGI
     VQDTLLGCRK ITKRDTLIEK DVFMNILMWW EDFDGKVPAP AILKPRPIWT GKQVFNLIIP
     KRINLIRFSA WHDEEESRFI TPGDTVVRIE KGELLSGILC KKTLGTSMGS LIHVIWEEVG
     PDAARKFLGH TQWLVNYWLL QHGFSIGIGD TIADAGTMKK ISDTISKAQD DVNELIKEAR
     DNKLEPEPGR TMMESFENKV NQVLNKARDD SGSSAQQSLS ESNNLKAMVT AGSKGSFINI
     SQMTACVGQQ NVEGKRIPFG FAGRTLPHFT QNDDSPESRG FVENSYLRGL TPQEFFFHAM
     GGREGLIDTA VKTSETGYIQ RRLVKAMEDI MVKYDGTVRN SLGDVIQFLY GEDGMDAVWI
     EPQKLDSLGM KKAEFDNVFR YELDDENWRP TYMSPEDADV LKTVPDIRLV FEAEFQKLEA
     DRLQLGTEIA TTGDITWPMP VNLKRLIWNA QKTFKIDLRR PSDMHPMEIV EAMDKLQERL
     KVVPGDDAMS IEAQKNATLL FNILLRSTFA SKRVLKEYRL TRESFEWVIG EIESRFLQSL
     VAPGEMIGCV AAQSIGEPAT QMTLNTFHYA GVSAKNVTLG VPRLREIINV AKKIKTPSLS
     VFLKPEVSKK KELAKNVQCA LEYTTLRSVT HATEIWYDPD PLRTTIEEDV EFVKSYYEMP
     DEDIDPDKMS PWLLRIELNR EMMVDKRLSM AEIAEKIKCE FDDDLSCIFN DDNADKLILR
     IRIKNDDEVP KQDEDDDVFL KKVESNMLTE MALGGIPDIN KVFIKERKVN KFDENDGFTQ
     KSDNKDKNKE WMLDTEGVNL LAVMCHEDVD TTRTTSNHLI EVIEVLGIEA VRRSLLDELR
     AVISFDGSYV NYRHLAILCD TMTYRGHLMA ITRHGINRND TGPLMRCSFE ETVDILLDAA
     MYAESDHLRG VTENIMLGQL APIGTGGCEL YLNDKMLEQA IELQLPSFVE GLDYGMTPAP
     SPISGMMSPV PSPNFRTSPV TDHALQFSPY VGGLAFSPVP SNYSTSSGSG YCPSSPVFSP
     GPGGQGYSPV SPVYSPLSPI YTPTSLSYSP VSPIHSPESP VYSPASPVFR PTSLQYSPTS
     PVYSPTSLEY SPTSPSYSPT SHAYSPTSPS YSPTSHAYSP TSPSYSPTSP VYSPASFSTS
     PYYNPTSPSY SPTSHSYSPT SPRYSPASPS YSPTSPNYSP TSPAYSPTSP SYSPTSPSYS
     PTSPSYSPTS PSYSPSRAYS PSSPMMMSPY SQLPPNYSLA SPTYSPTSPS YAAQPSPSYS
     PTSPCTASGG PSPDYSLTSP NYSPSASYSP PSTEPQTSDK DDDKSAP
//
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