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UniProtKB/Swiss-Prot entry P28364


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RPB1_EUPOC
Primary accession number P28364
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 52)
Name and origin of the protein
Protein name DNA-directed RNA polymerase II subunit RPB1 [Fragment]
Synonyms RNA polymerase II subunit B1
EC 2.7.7.6
DNA-directed RNA polymerase III largest subunit
Gene name
Name: RPB1
From
Euplotes octocarinatus [TaxID: 5937] 
Taxonomy Eukaryota; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea; Hypotrichia; Euplotida; Euplotidae; Euplotes.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=(68)-VIII;
DOI=10.1093/nar/20.17.4445; PubMed=1408746 [NCBI, ExPASy, EBI, Israel, Japan]
Kaufmann J., Klein A.;
"Gene dosage as a possible major determinant for equal expression levels of genes encoding RNA polymerase subunits in the hypotrichous ciliate Euplotes octocarinatus.";
Nucleic Acids Res. 20:4445-4450(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124.
DOI=10.1093/nar/20.22.5985; PubMed=1461731 [NCBI, ExPASy, EBI, Israel, Japan]
Kaufmann J., Florian V., Klein A.;
"TGA cysteine codons and intron sequences in conserved and nonconserved positions are found in macronuclear RNA polymerase genes of Euplotes octocarinatus.";
Nucleic Acids Res. 20:5985-5989(1992).
Comments
  • FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing (By similarity).
  • CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits (By similarity).
  • SUBCELLULAR LOCATION: Nucleus (By similarity).
  • PTM: The tandem 7 residues repeats can be highly phosphorylated. The phosphorylation activates POL2.
  • MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucelotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.
  • SIMILARITY: Belongs to the RNA polymerase beta' chain family.
  • SIMILARITY: Contains 1 C2H2-type zinc finger.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X66452; CAA47068.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S33886; S33886.
3D structure databases
HSSP P04050; 1K83. [HSSP ENTRY / PDB]
ModBase P28364.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0003899; Molecular function: DNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000722; RNA_pol_A.
IPR006592; RNA_pol_N.
IPR007080; RNA_pol_Rpb1_1.
Graphical view of domain structure.
Gene3D G3DSA:2.40.40.30; RNA_pol_A; 1.
G3DSA:3.90.1120.10; RNA_pol_Rpb1_1; 1.
Pfam PF04997; RNA_pol_Rpb1_1; 1.
PF00623; RNA_pol_Rpb1_2; 1.
Pfam graphical view of domain structure.
SMART SM00663; RPOLA_N; 1.
SMART graphical view of domain structure.
BLOCKS P28364.
ProtoNet P28364.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
DNA-binding; DNA-directed RNA polymerase; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Repeat; Transcription; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   >478  >478     DNA-directed RNA polymerase II subunit RPB1. PRO_0000073939
ZN_FING   68     84  17     C2H2-type (By similarity). 
METAL   68     68        Zinc. 
METAL   71     71        Zinc. 
METAL   78     78        Zinc. 
METAL   81     81        Zinc. 
METAL   474    474        Magnesium 1; catalytic (By similarity). 
METAL   474    474        Magnesium 2; shared with RPB2 (By similarity). 
METAL   476    476        Magnesium 1; catalytic (By similarity). 
METAL   476    476        Magnesium 2; shared with RPB2 (By similarity). 
NON_TER   478    478         
Sequence information
Length: 478 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 54026 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: 47A1ADD6ED98EB3D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRGTIYTES TMDFQKVRKI QFGLLDPKEI QAMSVVQVEN EKIYDNGIPT DGGINDLRMG 

        70         80         90        100        110        120 
TMEKAMRCST CQGDSKECPG HFGHIELAQP VFHIGFIDLV KKILKCVCFN CNKLLITDKH 

       130        140        150        160        170        180 
DKYSALKRVK DPKLKLNKVY KVCKDIKVCG KADRKSETYT EGSGQKQPRL RKTGLKIKAE 

       190        200        210        220        230        240 
FPIDEDDPST NDNKRDLSAS ECLKILGRIS PDDCKFLGFD MVLARPEWLI ISRLPVAPPP 

       250        260        270        280        290        300 
VRPSVCMGSN IRQEDDLTHQ YQQILKANNQ LRKHLSTANH IINENYQLLQ FYCATLIDNE 

       310        320        330        340        350        360 
QAGQMVSRHK SGGKAIKAIR ARLKGKEGRL RGNLMGKRVD FSARTVITCD PTLDLDQLGV 

       370        380        390        400        410        420 
PRSIAENITI PEVVTPQNID EMRKLVINGP NKWPGAKYIK GEGGKMIDLS YAKTTETFID 

       430        440        450        460        470 
YGYVIERHLK NDDFVLFNRQ PSLHKMSIMG HRVKVLPYST FRLNLSVTAP YNADFDGS 

P28364 in FASTA format

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