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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01943; PubMed=12917641 [NCBI, ExPASy, EBI, Israel, Japan]
Palenik B.,
Brahamsha B.,
Larimer F.W.,
Land M.L.,
Hauser L.,
Chain P.,
Lamerdin J.E.,
Regala W.,
Allen E.E.,
McCarren J.,
Paulsen I.T.,
Dufresne A.,
Partensky F.,
Webb E.A.,
Waterbury J.;
"The genome of a motile marine Synechococcus.";
Nature 424:1037-1042(2003).
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- FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
- SIMILARITY: Belongs to the peptidase S14 family [view classification].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 224 AA [This is the length of the unprocessed precursor] |
Molecular weight: 24092 Da [This is the MW of the unprocessed precursor] |
CRC64: A642583A8E200BC5 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MIDARSHHPI QNRWRAEMPI SAPGPLPTVV EQSGRGDRAF DIYSRLLRER IIFLGTGVDD
70 80 90 100 110 120
AVADALVAQM LFLEAEDPEK DIQIYINSPG GSVTAGLAIY DTMQQVAPDV VTICYGLAAS
130 140 150 160 170 180
MGAFLLSGGC KGKRLALPNA RIMIHQPLGG AQGQAVDIEI QAKEILFLKE TLNGLMADHT
190 200 210 220
GQPLDKIAED TDRDYFLSPA EAVQYGLIDR VVDSSGGEGI VTEG
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Q7UA36 in FASTA format |
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