ID A0A094BRC9_9PEZI Unreviewed; 787 AA.
AC A0A094BRC9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=V494_02543 {ECO:0000313|EMBL:KFY42178.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY42178.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY42178.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini provided that the penultimate residue is proline. Contributes
CC to pathogenicity. {ECO:0000256|ARBA:ARBA00037607}.
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:KFY42178.1}.
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DR EMBL; JPJW01000880; KFY42178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BRC9; -.
DR STRING; 1420907.A0A094BRC9; -.
DR HOGENOM; CLU_006105_0_2_1; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000029288; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IPR002471; Pept_S9_AS.
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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000029288};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..787
FT /note="dipeptidyl-peptidase IV"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001897713"
FT DOMAIN 109..469
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 558..763
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 787 AA; 88073 MW; 4C972F29734A77CA CRC64;
MKRFIILLGG LISLHFSTAY PTLSTRQSDS PNPTTKKVIT FADAFSGDFT VQKTSLQWTS
QGEDGSYVDA DADGNLNLVN IVTGDSKVFV NASDLAPAAK DFYDYTIHPS GDYVLFIANY
RKQHRHSYFA DYYVYSVADK TTIPLVEDQQ GDIQYATWSP VNYTIAYVRG NNLYIWQDGL
TTQITKDGGP DVFNAIPDWV YEEEIFGDRS TLWFSPDGEE LAFLRFDETG VETFSIPYYL
GYPGGDAAPP YPEELDIRYP KVSTTNPTVT FHLLSINGLT EVGAALRTVE FNAFAQNDTI
IGEVAWVTDD HSHVIFRAFN RVQDQEKLVL VDVLGNSTSN VRERDARPGW IDNNLAIQYI
PGTDSYVDLS DENGWNHIYL YSVNSSEPTA ITTGEWEVTA ILNIDSANQT IYYQSTERDS
TERHVYSISL DGTKKTALVD DSKPGSWAAS FSAGGGYYIL SYNGPELPYQ ELYNTSLTNS
AMKTINNNTK LESRLSEYTL PKVTWSTIDH PDGYSFNVME RLPPNFNSSQ QYPVVFDIYG
GPGSQQTAKT FRQVDFRAYL ASDPELEYII LSVDNRGTGY KGRDYRTIVS GQLGKVEAED
QIYAASEYAK RSYVDADHIA IMGWSYGGYL SSKVLEAQGN STHKSNSPFS FALITAPVSD
WRFYDSMYTE RYMKTIETNE AGYNESSVHD VTGFKDVAGG FLIQHGTGDD NVHFQNSAVL
VDTLTVGGVG PSKMHVQWFT DSDHSIGFHG ASGFVYRQMA QYLFGEKNRG EEVVTHQFDR
RALKSLK
//
