Signal recognition particle protein
Details
- Name
- Signal recognition particle protein
- Synonyms
- Fifty-four homolog
- Gene Name
- ffh
- Organism
- Thermus aquaticus
- Amino acid sequence
>lcl|BSEQ0011279|Signal recognition particle protein MFQQLSARLQEAIGRLRGRGRITEEDLKATLREIRRALMDADVNLEVARDFVERVREEAL GKQVLESLTPAEVILATVYEALKEALGGEARLPVLKDRNLWFLVGLQGSGKTTTAAKLAL YYKGKGRRPLLVAADTQRPAAREQLRLLGEKVGVPVLEVMDGESPESIRRRVEEKARLEA RDLILVDTAGRLQIDEPLMGELARLKEVLGPDEVLLVLDAMTGQEALSVARAFDEKVGVT GLVLTKLDGDARGGAALSARHVTGKPIYFAGVSEKPEGLEPFYPERLAGRILGMGDVASL AEKVRAAGLEAEAPKSAKELSLEDFLKQMQNLKRLGPFSEILGLLPGVPQGLKVDEKAIK RLEAIVLSMTPEERKDPRILNGSRRKRIAKGSGTSVQEVNRFIKAFEEMKALMKSLEKKK GRGLMGMFRR
- Number of residues
- 430
- Molecular Weight
- 47355.705
- Theoretical pI
- 10.17
- GO Classification
- Functions7S RNA binding / GTP binding / GTPase activityProcessesSRP-dependent cotranslational protein targeting to membraneComponentssignal recognition particle
- General Function
- Gtpase activity
- Specific Function
- Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0003552|1293 bp ATGTTCCAACAGCTTTCGGCGCGACTGCAAGAGGCCATCGGCCGCCTTAGGGGGCGGGGC CGGATCACCGAGGAGGACCTGAAGGCCACCCTCAGGGAGATCCGCCGGGCCCTCATGGAC GCCGATGTCAACCTGGAGGTGGCCCGGGACTTCGTGGAGCGGGTGCGGGAGGAGGCCTTG GGGAAGCAGGTCCTGGAGAGCCTCACCCCCGCCGAGGTGATCCTGGCCACCGTCTACGAG GCCCTCAAGGAGGCCCTGGGGGGCGAGGCCAGGCTCCCTGTCCTCAAGGACAGGAACCTC TGGTTCCTGGTGGGCCTCCAGGGCTCCGGCAAGACCACCACCGCCGCCAAGCTGGCCCTC TACTACAAGGGCAAGGGGAGGAGGCCCCTCTTGGTGGCCGCCGACACCCAGAGGCCCGCC GCCAGGGAGCAACTAAGGCTTCTGGGCGAGAAGGTGGGCGTGCCCGTGCTGGAGGTGATG GACGGGGAGTCCCCTGAGTCCATCCGCCGCCGGGTGGAGGAGAAGGCCCGCCTCGAGGCC CGGGACCTGATCCTGGTGGACACCGCCGGCCGCCTGCAGATTGACGAGCCCCTCATGGGG GAGCTGGCCCGCCTCAAGGAGGTCCTTGGCCCGGACGAGGTTCTCCTGGTCCTGGACGCC ATGACCGGGCAGGAAGCCCTTTCCGTGGCCAGGGCCTTTGACGAGAAGGTGGGGGTCACG GGCCTCGTCCTCACCAAGCTGGACGGGGATGCCCGGGGCGGGGCGGCCCTTTCCGCCCGC CACGTGACGGGCAAGCCCATCTACTTCGCCGGGGTTTCCGAGAAGCCGGAGGGCCTGGAG CCCTTCTACCCCGAGCGCCTGGCGGGCCGCATCCTGGGCATGGGGGACGTGGCCAGCCTG GCGGAGAAGGTGCGGGCGGCGGGGCTGGAGGCGGAGGCGCCCAAGTCCGCCAAGGAGCTT TCCCTGGAGGACTTCCTCAAGCAGATGCAGAACCTCAAGCGCCTGGGCCCCTTCTCCGAG ATCCTGGGCCTCCTGCCCGGGGTTCCCCAGGGGCTTAAGGTGGACGAGAAGGCCATAAAG CGCCTGGAGGCCATCGTCCTCTCCATGACCCCCGAGGAGCGCAAAGACCCCCGCATCCTA AACGGTTCCCGGCGCAAGCGCATCGCCAAGGGAAGCGGGACCTCGGTCCAGGAGGTCAAC CGCTTCATCAAGGCATTTGAGGAGATGAAGGCCCTAATGAAGTCCCTGGAGAAGAAGAAG GGCCGGGGACTCATGGGAATGTTCAGGAGGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O07347 UniProtKB Entry Name SRP54_THEAQ GenBank Protein ID 2149137 GenBank Gene ID U82109 - General References
- Freymann DM, Keenan RJ, Stroud RM, Walter P: Structure of the conserved GTPase domain of the signal recognition particle. Nature. 1997 Jan 23;385(6614):361-4. [Article]
- Keenan RJ, Freymann DM, Walter P, Stroud RM: Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell. 1998 Jul 24;94(2):181-91. [Article]
- Freymann DM, Keenan RJ, Stroud RM, Walter P: Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nat Struct Biol. 1999 Aug;6(8):793-801. [Article]
- Shepotinovskaya IV, Focia PJ, Freymann DM: Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY. Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1834-7. Epub 2003 Sep 19. [Article]