ID A0A453CSP6_AEGTS Unreviewed; 1441 AA.
AC A0A453CSP6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20949100.13, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv20949100.13}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) 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|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EnsemblPlants; AET2Gv20949100.13; AET2Gv20949100.13; AET2Gv20949100.
DR EnsemblPlants; AET2Gv20949100.4; AET2Gv20949100.4; AET2Gv20949100.
DR EnsemblPlants; AET2Gv20949100.8; AET2Gv20949100.8; AET2Gv20949100.
DR Gramene; AET2Gv20949100.13; AET2Gv20949100.13; AET2Gv20949100.
DR Gramene; AET2Gv20949100.4; AET2Gv20949100.4; AET2Gv20949100.
DR Gramene; AET2Gv20949100.8; AET2Gv20949100.8; AET2Gv20949100.
DR Proteomes; UP000015105; Chromosome 2D.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; 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; 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; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
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 216..522
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 671..698
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1441 AA; 163598 MW; F8F95892C0ACC495 CRC64;
MSVAVIEHAE TREKGKPKPG GLSDPRLGTI DRRTNCETCM AGAAECPGHF GHLELAKPMF
HIGFIKTVLS IMRCVCFNCS KILADEVDPM DNRFMEALRI KNPKTRLRKI NEACKSKKVC
SVGEDDLKGQ DQQHTNEPVK KRGGCGARQP NITIDGMKMV AEFKVTNKRN DDQDQLPEPV
EPKQILSAER VLNVLKHISD RDCLLLGLDP KYARPDWMIL QVLPIPPPPM RPSVMMDTCS
RSEDDLTHQL AMIIRHNENL RRQETNGASA HIITEFAQLL QFHIATYFDN DLPGQPRTTQ
RSGRPIKSIC SRLKGKEGRI RGNLMGKRVD FSARTVITPD PNINIDELGV PWSIALNLTY
PETVTPYNIE RLKKLVEYGP HPPPGKTGAK YIIREDGQRL DLCYVKKSSD QHLELGYKVE
RHLTDGDFVL LNRQPSLHKM SIMGHRIKIM PYSTFRLNLS VTSPYNADFD GDEMNMHVPQ
SFETRAEVLE LMMVPKCIVS PQANRPVMGI VQDTLLGSKK ITKRDTLIEK DVFMNILMWW
EDFDGKVPAP SIYKPRPIWT GKQVFNLIIP KEINLIRFSA WHDADAEKES GFITPSDTMV
RIEKGELLSG ILCKKTLGTS IGGLIHVIWE EVGPDAARKF LGHTQWLVNY WLLQHGFSIG
IGDTIADAGT MKKISDTISK AKNDVDELIK QAHDKKLEPE PGRTMMESFE NRVNQVLNKA
RDDAGSSAQK SLPESNNLKA MVTAGSKGSF INISQMTACV GQQNVEGKRI PFGFAGRTLP
HFTQNNYSPE SRGFVENSYL RGLTPQEFFF HAMGGREGLI DTAVKTSETG YIQRRLVKAM
EDIMVKYDGT VRNSVGDVIQ FLYGEDGMDA VWIEPQKLDS LGMKKAEFDS AFRYELDDEN
WRPTYMSPKY ADDLKTIHKF RIVFEAEFQK LEADRLQLGT EIATTGDITW PMPVNLKRLI
WNAQKTFKID LRRPSDMHPM EIVEAMDKLQ ERLKVVPGDD AMSIEAQKNA TLLFNILLRS
TFASKRVLKE YGLTRESFEW VIGEIESRFL QSLVAPGEMI GCVAAQSIGE PATPMTLNSF
HYAGVSAKNV TLGVPRLTEI INVAKKIKTP SLSVFLKPEV SKKKELAKNV QCALEYTTLR
SVIHATEIWY DPDPLGTTIE EDVEFVKSYY EMPDEDINLD KLSPWLLRIE LNREMMVDKR
LSMAEIAEKI KHEFDDDLSC IFNDDNADKL ILRIRIKNDD EAPKQHENDG VFLKEIDSNM
LTELALGGVP DINKVFIKEG EVNKFDEKDG FTQKAKNKEW MLDTEGVNLL AVMCHEDVDA
TRTTSNHLIE VIEVLGIEAV RRSLLDELRV VISFDGSYVN YRHLAILCDT MTYKGHLMAI
TRHGINRNDT GPLMRCSFEE TVDILLDAAV YAESDYLRCH REHYTWPARS YWYRRLWIVS
E
//
