ID   DAPB_PYRTR              Reviewed;         880 AA.
AC   B2WC36;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=PTRG_07545;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
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: 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:0000250}.
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   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass type
CC       II membrane protein {ECO:0000250}. Note=Lysosome-like vacuoles.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; DS231622; EDU50464.1; -; Genomic_DNA.
DR   RefSeq; XP_001937877.1; XM_001937842.1.
DR   AlphaFoldDB; B2WC36; -.
DR   SMR; B2WC36; -.
DR   STRING; 426418.B2WC36; -.
DR   ESTHER; pyrtr-dapb; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; B2WC36; 2 sites, No reported glycans.
DR   EnsemblFungi; EDU50464; EDU50464; PTRG_07545.
DR   GeneID; 6345817; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; B2WC36; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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:UniProtKB-KW.
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; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   CHAIN           1..880
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412160"
FT   TOPO_DOM        1..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..880
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        724
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        801
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        834
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        533
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        778
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   880 AA;  99739 MW;  2EBBF7438A194B42 CRC64;
     MPRQRAPKEE EAELLTKQER SARSSEDASD TSISSISTTS LVLEHINDPA INGTSRSRRG
     EKYTDEDDEA QEAFDVEGGR YKSPISVDKK TRRWLWIVGI ACVTGWALAL VFFLMSGSYK
     HVSTRPHDPL ASSTKGSGKK ITMDDVFGGR FYAREQSLKW IAGPNGEDGL LLERDAGNAE
     YLVVEDIRNK GDGDSSAKKT KLMQKSGFNV NGYFVRPVEV WPSKDFKKTG EPLDPENQDG
     RVQLASLSPQ SDAVVFTRNN NMYLRKLDSK EVIQITRDGG SELFYGIPDW VYEEEVFQTN
     SATWWSEDGK YIAFLRTDES TVPTYPVQYF VSRPSGDKPK AGEENYPEVR NIKYPKAGAP
     NPIVTLQFYD VEKAEVFSVE IEDDFRDNNR LITEIVWAGK TKQVLVRETN RESDILKVVL
     MDVEKRTGKT VRTENVAELD GGWFEVSQKT TFVPADPANG RKDDGYIDTI IHEGYDHIGY
     FTPLDNDKPI VLSQGEWEVV DAPSRVDLKN NIVYYISTAK SSMERHAYSV FLNGTGTSEV
     VENSGSGYYG ASFSAGGSYA LITYQGPGIP WQKIISTPSS KDKFEKVLEE NKALDRFVRE
     REMPILNYQT IEVDGFKLNV LERRPPHFNE KKKYPVLFYQ YSGPGSQEVN KKFHVDFQAY
     IAANLEYIVV TVDGRGTGFL GRKLRCITRG NIGYYEAHDQ IAAAKIWASK KYVDADRLAI
     WGWSYGGFNT LKTLEQDAGQ TFKYGMAVAP VTDWRYYDSI YTERYMHTPQ NNAAGYNNST
     ITDVASLAKN TRFLLMHGVA DDNVHMQNTL TLLDRLDLAG VENYDVHVFP DSDHSIYFHN
     ANRIVYDKLR WWLINAFNGE WAKIKTAEPK AQVDARMERR
//