ID A0A094CS05_9PEZI Unreviewed; 908 AA.
AC A0A094CS05;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN ORFNames=V497_05976 {ECO:0000313|EMBL:KFY56764.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY56764.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY56764.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
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: Type IV dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini provided that the penultimate residue is proline.
CC {ECO:0000256|ARBA:ARBA00002218}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC membrane {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004576}.
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:KFY56764.1}.
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DR EMBL; JPJZ01001073; KFY56764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CS05; -.
DR STRING; 1420910.A0A094CS05; -.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000029268; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; 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:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 223..598
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 682..886
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 101162 MW; 5F5935C82D8BB30C CRC64;
MVGREEEAAG LLENSHEGPS RASIDSMSSA STTSLVFERI DEQNKSQAKS SRMPGQNGSR
PYSDHVEALS LDAEDEKQQD LENGLTSSKG SSRWCTKLVW ILAGTFVTLW AAGTVIFLIR
HPVADAPHNP NAPNIGNGNK VTLPQVMGGQ WAARKHGISW IEGANGEDGL LLEQGAAGKN
YLVVEDVRGD NATQSSAPDN VLMKIPVFTA GGERHKASKV WPSKNLKHVL IATNVESNWR
HSFYARYWIF DVETQTAQPL DPTNLRGRVQ LASWSPQSDA IVFTRDNNVF LRKLSSPTVI
PITTDGNKDL FYGIPDWVYE EEVFGGNSAT WWAEDGKYIA FLRTNESQVP EYPVQYFIKR
PSGTEAAPGE ENYPEVRQIK YPKAGAPNPI VSLRFYDVAK GDVFDVKTAD DFADDTRLIT
EVIWAGATGK AIVKETNRES DILQVVLVDV LSRSGKTVRT VNVAEIDGGW FEVSQKTRYI
PADPTNGRPH DGYIDTIIHE NYDHLGYFTP LDNATPVLLT SGNWEVESAP SAVDLKNNLV
YFVSTKESPI QRHIYSVKLD GTDLKPLTDT SKEGYYSGSF SSGAGYSLLS YDGPAIPWQR
VISTPSNSDS YEKIVEENQA LERMAKKHDL PENIYSNVTI DGFNLQVIER RPPHFDKKKK
YPVLFHLYGG PGSQTVDKKF KVDFQAYVAA NLGYIVVTVD GRGTGFIGRK ARCIIRGDLG
HWEAHDQIET AKIWAAKPYV DASRLAIWGW SYGGFMTLKT LEQDAGQTFQ YGMAVAPVTD
WRYYDSIYTE RYMHTPQENP GGYDNATVSD AVALQKNVRF LIMHGVADDN VHMQNTLALL
DRLDLAGVEN YDVHVFPDSD HGIYFHNANK IVYDKLNNWL INAFNGEWLR TSNAVPIAVD
TAAEREKE
//
