(data stored in ACNUC11299 zone)

HOGENOM: ARATH_4_PE4762

ID   ARATH_4_PE4762                       STANDARD;      PRT;   1839 AA.
AC   ARATH_4_PE4762; P18616; P31635; Q56Z04; Q9SZS8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA-directed RNA polymerase II subunit RPB1; Short=RNA
DE   polymerase II subunit B1; EC=2.7.7 6;AltName: Full=DNA-directed RNA
DE   polymerase III largest subunit; (ARATH_4.PE4762).
GN   Name=RPB205; Synonyms=RPB1, RPII; OrderedLocusNames=At4g35800;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_4.PE4762.
CC       Arabidopsis thaliana chromosome 4 TAIR10 full sequence 1..18585056
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:RPB1_ARATH
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. Largest and catalytic component of RNA polymerase II
CC       which synthesizes mRNA precursors and many functional non-coding
CC       RNAs. Forms the polymerase active center together with the second
CC       largest subunit. Pol II is the central component of the basal RNA
CC       polymerase II transcription machinery. It is composed of mobile
CC       elements that move relative to each other. RPB1 is part of the
CC       core element with the central large cleft, the clamp element that
CC       moves to open and close the cleft and the jaws that are thought to
CC       grab the incoming DNA template. At the start of transcription, a
CC       single stranded DNA template strand of the promoter is positioned
CC       within the central active site cleft of Pol II. A bridging helix
CC       emanates from RPB1 and crosses the cleft near the catalytic site
CC       and is thought to promote translocation of Pol II by acting as a
CC       ratchet that moves the RNA-DNA hybrid through the active site by
CC       switching from straight to bent conformations at each step of
CC       nucleotide addition. During transcription elongation, Pol II moves
CC       on the template as the transcript elongates. Elongation is
CC       influenced by the phosphorylation status of the C-terminal domain
CC       (CTD) of Pol II largest subunit (RPB1), which serves as a platform
CC       for assembly of factors that regulate transcription initiation,
CC       elongation, termination and mRNA processing (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC       consisting of 12 subunits (By similarity). Interacts with RDM1.
CC   -!- INTERACTION:
CC       Q6Q151:CYP59; NbExp=3; IntAct=EBI-1540537, EBI-1625989;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Note=Peri-nucleolar.
CC   -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD)
CC       can be highly phosphorylated. The phosphorylation activates Pol
CC       II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5'
CC       of the heptapepdtide repeat. The phosphorylation state is believed
CC       to result from the balanced action of site-specific CTD kinases
CC       and phosphataes, and a "CTD code" that specifies the position of
CC       Pol II within the transcription cycle has been proposed.
CC   -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the
CC       RNA polymerase II transcribing complex probably involves a two-
CC       step mechanism. The initial binding seems to occur at the entry
CC       (E) site and involves a magnesium ion temporarily coordinated by
CC       three conserved aspartate residues of the two largest RNA Pol II
CC       subunits. The ribonucleoside triphosphate is transferred by a
CC       rotation to the nucelotide addition (A) site for pairing with the
CC       template DNA. The catalytic A site involves three conserved
CC       aspartate residues of the RNA Pol II largest subunit which
CC       permanently coordinate a second magnesium ion.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA36735.1; Type=Erroneous gene model prediction;
CC   -!- GENE_FAMILY: HOG000222975 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT4G35800;AT4G35800.1;AT4G35800.1.
DR   EMBL; AK221166; - ;
DR   EMBL; AL031986; - ;
DR   EMBL; AL161588; - ;
DR   EMBL; X52494; - ;
DR   EMBL; X52954; - ;
DR   UniProtKB/Swiss-Prot; P18616; P31635; Q56Z04; Q9SZS8; -.
DR   EMBL; X52954; CAA37130.1; -; Genomic_DNA.
DR   EMBL; X52494; CAA36735.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL031986; CAA21466.2; -; Genomic_DNA.
DR   EMBL; AL161588; CAB81489.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86573.1; -; Genomic_DNA.
DR   EMBL; AK221166; BAD95215.1; -; mRNA.
DR   IPI; IPI00545790; -.
DR   PIR; G85422; G85422.
DR   PIR; T04690; JDMU1.
DR   RefSeq; NP_195305.2; NM_119746.3.
DR   UniGene; At.23499; -.
DR   UniGene; At.67132; -.
DR   DIP; DIP-40008N; -.
DR   IntAct; P18616; 1.
DR   STRING; P18616; -.
DR   PRIDE; P18616; -.
DR   EnsemblPlants; AT4G35800.1; AT4G35800.1; AT4G35800.
DR   GeneID; 829734; -.
DR   GenomeReviews; CT486007_GR; AT4G35800.
DR   KEGG; ath:AT4G35800; -.
DR   NMPDR; fig|3702.1.peg.21671; -.
DR   TAIR; At4g35800; -.
DR   eggNOG; KOG0260; -.
DR   InParanoid; P18616; -.
DR   PhylomeDB; P18616; -.
DR   ProtClustDB; CLSN2685306; -.
DR   ArrayExpress; P18616; -.
DR   Genevestigator; P18616; -.
DR   GermOnline; AT4G35800; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IPI:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:InterPro.
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; 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   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   Pfam; PF05001; RNA_pol_Rpb1_R; 25.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 23.
DR   HOGENOMDNA; ARATH_4.PE4762; -.
KW   AT4G35800pg.C_scaffold_1320000031; AT4G35800.10C_scaffold_1320000031;
KW   Q56Z04; AK221166; AL031986; AL161588; X52494; X52954;
KW   Complete proteome; DNA-binding; DNA-directed RNA polymerase;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transferase; Zinc.
SQ   SEQUENCE   1839 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDTRFPFSPA EVSKVRVVQF GILSPDEIRQ MSVIHVEHSE TTEKGKPKVG GLSDTRLGTI
     DRKVKCETCM ANMAECPGHF GYLELAKPMY HVGFMKTVLS IMRCVCFNCS KILADEEEHK
     FKQAMKIKNP KNRLKKILDA CKNKTKCDGG DDIDDVQSHS TDEPVKKSRG GCGAQQPKLT
     IEGMKMIAEY KIQRKKNDEP DQLPEPAERK QTLGADRVLS VLKRISDADC QLLGFNPKFA
     RPDWMILEVL PIPPPPVRPS VMMDATSRSE DDLTHQLAMI IRHNENLKRQ EKNGAPAHII
     SEFTQLLQFH IATYFDNELP GQPRATQKSG RPIKSICSRL KAKEGRIRGN LMGKRVDFSA
     RTVITPDPTI NIDELGVPWS IALNLTYPET VTPYNIERLK ELVDYGPHPP PGKTGAKYII
     RDDGQRLDLR YLKKSSDQHL ELGYKVERHL QDGDFVLFNR QPSLHKMSIM GHRIRIMPYS
     TFRLNLSVTS PYNADFDGDE MNMHVPQSFE TRAEVLELMM VPKCIVSPQA NRPVMGIVQD
     TLLGCRKITK RDTFIEKDVF MNTLMWWEDF DGKVPAPAIL KPRPLWTGKQ VFNLIIPKQI
     NLLRYSAWHA DTETGFITPG DTQVRIERGE LLAGTLCKKT LGTSNGSLVH VIWEEVGPDA
     ARKFLGHTQW LVNYWLLQNG FTIGIGDTIA DSSTMEKINE TISNAKTAVK DLIRQFQGKE
     LDPEPGRTMR DTFENRVNQV LNKARDDAGS SAQKSLAETN NLKAMVTAGS KGSFINISQM
     TACVGQQNVE GKRIPFGFDG RTLPHFTKDD YGPESRGFVE NSYLRGLTPQ EFFFHAMGGR
     EGLIDTAVKT SETGYIQRRL VKAMEDIMVK YDGTVRNSLG DVIQFLYGED GMDAVWIESQ
     KLDSLKMKKS EFDRTFKYEI DDENWNPTYL SDEHLEDLKG IRELRDVFDA EYSKLETDRF
     QLGTEIATNG DSTWPLPVNI KRHIWNAQKT FKIDLRKISD MHPVEIVDAV DKLQERLLVV
     PGDDALSVEA QKNATLFFNI LLRSTLASKR VLEEYKLSRE AFEWVIGEIE SRFLQSLVAP
     GEMIGCVAAQ SIGEPATQMT LNTFHYAGVS AKNVTLGVPR LREIINVAKR IKTPSLSVYL
     TPEASKSKEG AKTVQCALEY TTLRSVTQAT EVWYDPDPMS TIIEEDFEFV RSYYEMPDED
     VSPDKISPWL LRIELNREMM VDKKLSMADI AEKINLEFDD DLTCIFNDDN AQKLILRIRI
     MNDEGPKGEL QDESAEDDVF LKKIESNMLT EMALRGIPDI NKVFIKQVRK SRFDEEGGFK
     TSEEWMLDTE GVNLLAVMCH EDVDPKRTTS NHLIEIIEVL GIEAVRRALL DELRVVISFD
     GSYVNYRHLA ILCDTMTYRG HLMAITRHGI NRNDTGPLMR CSFEETVDIL LDAAAYAETD
     CLRGVTENIM LGQLAPIGTG DCELYLNDEM LKNAIELQLP SYMDGLEFGM TPARSPVSGT
     PYHEGMMSPN YLLSPNMRLS PMSDAQFSPY VGGMAFSPSS SPGYSPSSPG YSPTSPGYSP
     TSPGYSPTSP GYSPTSPTYS PSSPGYSPTS PAYSPTSPSY SPTSPSYSPT SPSYSPTSPS
     YSPTSPSYSP TSPSYSPTSP AYSPTSPAYS PTSPAYSPTS PSYSPTSPSY SPTSPSYSPT
     SPSYSPTSPS YSPTSPAYSP TSPGYSPTSP SYSPTSPSYG PTSPSYNPQS AKYSPSIAYS
     PSNARLSPAS PYSPTSPNYS PTSPSYSPTS PSYSPSSPTY SPSSPYSSGA SPDYSPSAGY
     SPTLPGYSPS STGQYTPHEG DKKDKTGKKD ASKDDKGNP
//

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