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Database: UniProt
Entry: A0A1T5CPH6_9SPHI
LinkDB: A0A1T5CPH6_9SPHI
Original site: A0A1T5CPH6_9SPHI 
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}.
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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
//
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