ID B2WGG5_PYRTR Unreviewed; 779 AA.
AC B2WGG5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=PTRG_09021 {ECO:0000313|EMBL:EDU42072.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU42072.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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}.
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DR EMBL; DS231624; EDU42072.1; -; Genomic_DNA.
DR RefSeq; XP_001939353.1; XM_001939318.1.
DR AlphaFoldDB; B2WGG5; -.
DR STRING; 426418.B2WGG5; -.
DR ESTHER; pyrtr-b2wgg5; DPP4N_Peptidase_S9.
DR MEROPS; S09.008; -.
DR EnsemblFungi; EDU42072; EDU42072; PTRG_09021.
DR GeneID; 6347308; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_2_1; -.
DR InParanoid; B2WGG5; -.
DR OMA; SLMFAKF; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000001471; 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:UP000001471};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..779
FT /note="dipeptidyl-peptidase IV"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002782800"
FT DOMAIN 100..466
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 552..747
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 756..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 87541 MW; 888A4A7C0C270C2B CRC64;
MRSFALLAAV LPLVQAIEPP RMPHQPLGNG TKRLSYNEST TSALSPSTRS FTWVGTGKDG
DYIYTAASGD FVFENVATGE SSTFLSADQV PKDYWDYFIS PDATKVMWAV NYTKQYRHSY
FADYLIMDVA TGESVPLDPE QVGDIQYAKW SPVSSSQVAF VKGNNLYMST NGTVSQITEN
GGPDYFNAIP DWVYEEEIFG DRYTLWFSPD GTRIAFLSFN ETGVGTFRIP YYINDDAEYV
PVYPNELELR YPKVGTKNPT VVMNMLDVAS GEVSNIPIDA FPEDDLVIGE VVWLTEEHSK
VIYRAYNRVQ DMEKLVVVNV ESGSSKVTRE RDGTDGWLEN LMQIRYIGAV ETSNASYGNA
TEYYMDLSDM SGWAHIYLFP VDGGEPIALT SGEWEVISVP KVDYSRRLIY YTSTEHHSAE
SHMYSVSFSG KKTPLVDDSV TAFWTGSFSS GGSYYVLRYA GPDVPYQELY SINSSEPIRT
IVNNTALYEK LQGYALPNIT YLDMEHPSGY TLDAMLRLPP NFDPSKKYPL LLIPYGGPNA
KEVQKSFNPL NWKAYVASDP ELEYVTLTVD GRGTGRKGRA FRSLVTSNLG ELEAKDQIWA
AKEMAKNEWI DSEHIGIWGW SYGGYLSSKV VEVGDPIISY AMITAPVSDW RFYDSLYTER
YMKTPTINPA GYNRSRVYDA SGFKKIAGGV VIQHGTGDDN VHFQNSAALV DLLMVNQVTP
EKMQNTFFTD SDHSINFHNN GKFLYKQLSK KLYEEKARKG DSKGSHQWSK RGEARTWAA
//
