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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1101/gr.7020108; PubMed=18032721 [NCBI, ExPASy, EBI, Israel, Japan]
Thomson N.R.,
Holden M.T.G.,
Carder C.,
Lennard N.,
Lockey S.J.,
Marsh P.,
Skipp P.,
O'Connor C.D.,
Goodhead I.,
Norbertzcak H.,
Harris B.,
Ormond D.,
Rance R.,
Quail M.A.,
Parkhill J.,
Stephens R.S.,
Clarke I.N.;
"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates.";
Genome Res. 18:161-171(2008).
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[2]
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PROTEIN SEQUENCE OF 2-11.
Bini L.,
Santucci A.,
Magi B.,
Marzocchi B.,
Sanchez-Campillo M.,
Comanducci M.,
Christianen G.,
Birkelund S.,
Vtretou E.,
Ratti G.,
Pallini V.;
Submitted (SEP-1994) to UniProtKB.
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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: 192 AA [This is the length of the unprocessed precursor] |
Molecular weight: 21073 Da [This is the MW of the unprocessed precursor] |
CRC64: 589EF06C344F20EF [This is a checksum on the sequence] |
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10 20 30 40 50 60
MPEGEMMHKL QDVIDRKLLD SRRIFFSEPV TEKSAAEAIK KLWYLELTNP GQPIVFVINS
70 80 90 100 110 120
PGGSVDAGFA VWDQIKMISS PLTTVVTGLA ASMGSVLSLC AVPGRRFATP HARIMIHQPS
130 140 150 160 170 180
IGGTITGQAT DLDIHAREIL KTKARIIDVY VEATGQSPEV IEKAIDRDMW MSANEAMEFG
190
LLDGILFSFN DL
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B0B803 in FASTA format |
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