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Pre-mRNA cleavage complex 2 protein Pcf11Known also as: Pre-mRNA cleavage complex II protein Pcf11 Known abbreviations: PCF11, hPcf11, KIAA0824 Yeast homolog: PCF11 Protein
This protein is highly disordered (87 % of residues are predicted to be disordered)
Top 3 models:
Sequence: 1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130 MSEQTPAEAGAAGAREDACRDYQSSLEDLTFNSKPHINMLTILAEENLPFAKEIVSLIEAQTAKAPSSEKLPVMYLMDSIVKNVGREYLTAFTKNLVATFICVFEKVDENTRKSLFKLRSTWDEIFPLKK LYALDVRVNSLDPAWPIKPLPPNVNTSSIHVNPKFLNKSPEEPSTPGTVVSSPSISTPPIVPDIQKNLTQEQLIRQQLLAKQKQLLELQQKKLELELEQAKAQLAVSLSVQQETSNLGPGSAPSKLHVSQ IPPMAVKAPHQVPVQSEKSRPGPSLQIQDLKGTNRDPRLNRISQHSHGKDQSHRKEFLMNTLNQSDTKTSKTIPSEKLNSSKQEKSKSGEKITKKELDQLDSKSKSKSKSPSPLKNKLSHTKDLKNQESE SMRLSDMNKRDPRLKKHLQDKTDGKDDDVKEKRKTAEKKDKDEHMKSSEHRLAGSRNKIINGIVQKQDTITEESEKQGTKPGRSSTRKRSRSRSPKSRSPIIHSPKRRDRRSPKRRQRSMSPTSTPKAGK IRQSGAKQSHMEEFTPPSREDRNAKRSTKQDIRDPRRMKKTEEERPQETTNQHSTKSGTEPKENVENWQSSKSAKRWKSGWEENKSLQQVDEHSKPPHLRHRESWSSTKGILSPRAPKQQQHRLSVDANL QIPKELTLASKRELLQKTSERLASGEITQDDFLVVVHQIRQLFQYQEGVREEQRSPFNDRFPLKRPRYEDSDKPFVDSPASRFAGLDTNQRLTALAEDRPLFDGPSRPSVARDGPTKMIFEGPNKLSPRI DGPPTPASLRFDGSPGQMGGGGPLRFEGPQGQLGGGCPLRFEGPPGPVGTPLRFEGPIGQAGGGGFRFEGSPGLRFEGSPGGLRFEGPGGQPVGGLRFEGHRGQPVGGLRFEGPHGQPVGGLRFDNPRGQ PVGGLRFEGGHGPSGAAIRFDGPHGQPGGGIRFEGPLLQQGVGMRFEGPHGQSVAGLRFEGQHNQLGGNLRFEGPHGQPGVGIRFEGPLVQQGGGMRFEGPSVPGGGLRIEGPLGQGGPRFEGCHALRFD GQPGQPSLLPRFDGLHGQPGPRFERTPGQPGPQRFDGPPGQQVQPRFDGVPQRFDGPQHQQASRFDIPLGLQGTRFDNHPSQRLESVSFNQTGPYNDPPGNAFNAPSQGLQFQRHEQIFDSPQGPNFNGP HGPGNQSFSNPLNRASGHYFDEKNLQSSQFGNFGNIPAPMTVGNIQASQQVLSGVAQPVAFGQGQQFLPVHPQNPGFVQNPSGALPKAYPDNHLSQVDVNELFSKLLKTGILKLSQTDSATTQVSEVTAQ PPPEEEEDQNEDQDVPDLTNFTVEELKQRYDSVINRLYTGIQCYSCGMRFTTSQTDVYADHLDWHYRQNRTEKDVSRKVTHRRWYYSLTDWIEFEEIADLEERAKSQFFEKVHEEVVLKTQEAAKEKEFQ SVPAGPAGAVESCEICQEQFEQYWDEEEEEWHLKNAIRVDGKIYHPSCYEDYQNTSSFDCTPSPSKTPVENPLNIMLNIVKNELQEPCDSPKVKEERIDTPPACTEESIATPSEIKTENDTVESV Gene location: 11q13 Summary Component of pre-mRNA cleavage complex II. Functions as a scaffold for the processing machinery during the termination and polyadenylation of transcripts. Yeast Pcf11p is only about half the size of hPcf11, and is equivalent to the N-terminal half of hPcf11. The function of the C-terminal half of hPcf11 is not known. Pcf11p contains a conserved PolII CTD interacting domain (CID) that covers ~130 residues in the N-terminus, which prefers the phosphorylated form of the CTD. The crystal structure of Pcf11p in complex with a phosphorylated CTD peptide has been reported. Mutations in the CID reduce or abolish binding to the CTD and result in cell death. Interestingly, these mutations do not affect 3?-end processing, but instead cause incorrect transcriptional termination (can also bind RNA to affect transcriptional termination). Studies of the CID indicate that the RNA binding and the protein binding regions overlap, and this competition for binding may play a role in the release of the 3?-end processing factors from PolII. The CID is followed by a 20-residue stretch of glutamines (234–253 in Pcf11p), which is followed by the Rna14p/Rna15p binding domain. The binding of Rna14p/Rna15p to Pcf11p is dependent on the binding of Clp1p first. This CstF binding region is followed by the Clp1 interacting segment (477–499), which is flanked by a zinc finger on each side (N-terminal C2H2 and C-terminal C2HC type). Pcf11p also interacts with Cft1p/ Yhh1p, Cft2p/Y. See this protein in other databases: Literature:
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