ID A0A1T5CPH6_9SPHI Unreviewed; 721 AA.
AC A0A1T5CPH6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=SAMN05660841_01496 {ECO:0000313|EMBL:SKB61337.1};
OS Sphingobacterium nematocida.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1513896 {ECO:0000313|EMBL:SKB61337.1, ECO:0000313|Proteomes:UP000190150};
RN [1] {ECO:0000313|Proteomes:UP000190150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24091 {ECO:0000313|Proteomes:UP000190150};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. {ECO:0000256|RuleBase:RU366067}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000256|ARBA:ARBA00010491, ECO:0000256|RuleBase:RU366067}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FUZF01000004; SKB61337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5CPH6; -.
DR STRING; 1513896.SAMN05660841_01496; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000190150; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR38469; -; 1.
DR PANTHER; PTHR38469:SF1; DIPEPTIDYL-PEPTIDASE; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU366067}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 25..721
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023080358"
SQ SEQUENCE 721 AA; 81839 MW; 88BA3F5F55ED99E3 CRC64;
MKYNFKSSIL LAALLGLGTF NFSASIPDEG MFPLSDLNRA GLKKAGLKIN ERDIYNPGQI
GLVDALVQVS GCSGSFVSPN GLIVTNHHCA FSAVQLASSP QHNYLEHGFV ANSQEQEIEA
RGLTIRITES YEDVSSQILN AVAQVNDPVE RINIINKKRA EIAQEAERKD ASIKAEVSEM
FIGKSYVLFR YRTIEDVRLV YIPRQDIGEF GGETDNWVWP RHTGDFSFLR AYVAPDGKSA
KYSKSNVPYK PKKHLKVNPK GVNENDFVFI LGYPGKTFRH RPAQYIEYQQ QFLLPYTSEL
YDFQNQQMLL AGKNDKTTEL ALATRIKRNA NVLKNYRGKL KGLRNIDLIQ SKKQEDLALS
QFIASKPELK AKYASLMTDI DQHYQLVFSD AERELWFNNL YTGIRSLQIA SLVNDFKDML
AKQAGNSSKQ QFFENNIVRF KQQLDGIYES YNNKADQHIA GHMFGQAYLF KDKNRIVAIA
DKSFANQEQA SQYIENAIVQ SKVSNKETLY TQVLKDMNSL SAYKDELLAF QQKIEKEMEP
FRQEQKRREG VLNRLMGDYV AVKEVYQSKN FIPDANSTLR LTYGNIKGYS PADATYMKPF
TTVQGLLEKG NSGDTEFRYP EAIKQAWLKK NFGAYGKSDL NDVPVNILYN MDTTGGNSGS
PIMNAYGELI GVNFDRSYDA TINDFAWNES YSRSIGVDIR YVLWIADKID NAQFILKEMG
I
//