ID A0A1F7ZKW7_9EURO Unreviewed; 771 AA.
AC A0A1F7ZKW7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
DE AltName: Full=Dipeptidyl peptidase IV {ECO:0000256|ARBA:ARBA00030567};
GN ORFNames=ABOM_011408 {ECO:0000313|EMBL:OGM40093.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM40093.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM40093.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC Pro nor hydroxyproline.; EC=3.4.14.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001257};
CC -!- SIMILARITY: Belongs to the peptidase S9B family.
CC {ECO:0000256|ARBA:ARBA00006150}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM40093.1}.
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DR EMBL; LYCR01000160; OGM40093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZKW7; -.
DR STRING; 109264.A0A1F7ZKW7; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF162; DIPEPTIDYL PEPTIDASE 4-RELATED; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..771
FT /note="dipeptidyl-peptidase IV"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009533896"
FT DOMAIN 104..463
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 557..735
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 771 AA; 86603 MW; 30F7FB8F5B5F21FC CRC64;
MKYSKLLLLL VGVAQALDVP RKPHAPTGEG SKRLTFNETV IKQAITPTSR SVQWLSGAED
GSYVYAADDG SLTIENIVTN ESRTLIPADK IPTGKEAFDY WIHPDLSSVL WASNHTKQYR
HSFFADYYVQ DVESLKSVPL MPDQEGDIQY ARWSPAGNTI AFVRDNDLYV WDNGTVTRIT
DDGGPDMFHG VPDWIYEEEI LGDRYALWFS PDGEYLAYLS FNETGVPTYT VQYYMDNQPL
APAYPRELKI RYPKVSQTNP TVTLSLLNIA SKEVKQAPID AFEPTDLIIG EVTWLTDTHT
TVAAKAFNRV QDQQKVVAVD TASNKATVIS DRDGTDGWLD NLLSINYIGS IKPSDKAAYY
IDISDHSGWA HLYLFPVSGG KPIPLTKGEW EVTSILSIDQ ERQLVYYLST QHHSTERHLY
SVSYSTFEVT SLVDDTVAAY WSASFSANSG YYILTYGGPD VPYQELYTTN STKPLRTITD
NAKVLEQIKD YALPNITYFE LPLPSGETLN VMQRLPPGFS PDKKYPILFT PYGGPGAQEV
TKRWQALNFK AYVASDSELE YVTWTVDNRG TGFKGRKFRS AVTGQLGLLE AEDQIYAAQQ
AANIPWIDAD HIGIWGWSFG GYLTSKVLEK DSDAFTLGVI TAPVSDWRFY DSMYTERYMK
TLSTNEEGYT TSAVRNTDGF KNVEGGFLIQ HGTGDDNVHF QNSAALVDLL MGDGVSPEKL
HSQWFTDSDH GISYNGGGVF LYKQLARKLY QEKNRQAQVL LHQWTKKDLE E
//
