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Database: UniProt
Entry: A0A127MCF8_9SPHN
LinkDB: A0A127MCF8_9SPHN
Original site: A0A127MCF8_9SPHN 
ID   A0A127MCF8_9SPHN        Unreviewed;       683 AA.
AC   A0A127MCF8;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=AZE99_02835 {ECO:0000313|EMBL:AMO70929.1};
OS   Sphingorhabdus sp. M41.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO70929.1, ECO:0000313|Proteomes:UP000073959};
RN   [1] {ECO:0000313|EMBL:AMO70929.1, ECO:0000313|Proteomes:UP000073959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M41 {ECO:0000313|EMBL:AMO70929.1,
RC   ECO:0000313|Proteomes:UP000073959};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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; CP014545; AMO70929.1; -; Genomic_DNA.
DR   RefSeq; WP_067197921.1; NZ_CP014545.1.
DR   AlphaFoldDB; A0A127MCF8; -.
DR   STRING; 1806885.AZE99_02835; -.
DR   KEGG; sphg:AZE99_02835; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000073959; Chromosome.
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|RuleBase:RU366067};
KW   Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           26..683
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023106284"
SQ   SEQUENCE   683 AA;  74075 MW;  4AE20DFB64A1B9D4 CRC64;
     MTQRSVYLAT GMICLFGAAA SPAYAEEGMW TFGAFPTEQM REAYGWAPDK AWLDRVQAAS
     VRLTGGCSAS FVSSQGLILT NHHCVASCLY QNSDDDNDFL KNGFTAGNRA EEKKCAGQQA
     EVVTMISDVT ADITAAIGNL SGEALTKARD AKIAAIESAG CPDTDTTRCQ VVTLFGGGQY
     KLYSYRKYSD VRLAWSPEDR AATFGGDPDN FNFPRYSLDA SFLRAYENGK PVATPAHLKW
     NPRAPKEGEL TFVVGNPGST SRLYTQSQLA FEREVRLPVT VATMSELRGR LIRAMEESPE
     KNREGLDLLG GIENSLKVYI GRTKALNDPA FTAKLAKAEA DLKAKSAGND AIGDPWADVD
     AAMQAYRSYY LPARFTDPTG DLYNYAQVLV LAAIESAKPN AERLPGFTDS ALPLTKKRLL
     DERPIYPWLD ELKFGWSLSK AREYLGPDDS DTKLLLGKES PEQLAERLVA GTGLADPKMR
     QKLWDGGLAA IEASDDPMIL YARKLEARQR ELKQQIDENY AGPLTNAGAK LADARFAAYG
     DKLYPDATFT LRISYGQVKG WMERGNQVPI ATTLGGTFDR ATGNEPFDLA PAFVANKDKI
     DPSITYDFVS TNDIIGGNSG SPVIDKAGTV IGAAFDGNIH SLGGNYGYDP ALNRTVSVSV
     AAVQEALETI YPAPNLVKEL AGK
//
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