ID   DAPB_PYRTT              Reviewed;         907 AA.
AC   E3S9K3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=PTT_19734;
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1;
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
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; GL537929; EFQ85356.1; -; Genomic_DNA.
DR   RefSeq; XP_003306558.1; XM_003306510.1.
DR   AlphaFoldDB; E3S9K3; -.
DR   SMR; E3S9K3; -.
DR   STRING; 861557.E3S9K3; -.
DR   ESTHER; pyrtr-dapb; DPP4N_Peptidase_S9.
DR   PRIDE; E3S9K3; -.
DR   EnsemblFungi; EFQ85356; EFQ85356; PTT_19734.
DR   KEGG; pte:PTT_19734; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OrthoDB; 269253at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 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..907
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412161"
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..907
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..70
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..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        751
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        828
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        861
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        560
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        805
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   907 AA;  102862 MW;  6A5E656B4F204015 CRC64;
     MPRQRAPKEE EAELLTKQER STRSSEDASD ASVSSISTTS LVLEHINNPA INGTSRSRRG
     EKYTDEDDEA QEAFDVEDGR YKAPVAVDKK TRRWLWIVGI ACVTGWALAL VFFLMSGSYK
     HVSTRPHDPL ASSTKGSGKK ITMDDVFGGS FYAQQQSVKW IAGPNGEDGL LLEKNTGNAG
     YLVVEDIRNK GDGDSSAKKT KLMQKSSFDV DGKLVRPNEV WPSKDFKKVL VQSDFEKNWR
     HSGTGKYWIF DVATQTGEPL DPENQDGRVQ LASLSPQSDA VVFTRDNNMY LRKLDSKEVI
     QITRDGGSEL FYGIPDWVYE EEVFQGNSAT WWSEDGKYIA FLRTDESTVP TYPVQYFVSR
     PSGNKPKAGE ENYPEVRNIK YPKAGAPNPI VALQFYDVEK AEVFSVEIED DFRDNNRLIT
     EIVWAGKTKQ VLVRETNRES DILKVVLMDV EKRTGKTVRT ENVAELDGGW FEVSQKTTFV
     PADPDNGRKD DGYIDTIIHE GYDHIGYFTP LDNDKPVLLS QGEWEVVDAP SRVDLKNNMV
     YYVSTEKSSM ERHAYSVFLN GTGTSEVVEN SGSGYYEASF SAGGSYALIT YQGPGIPWQK
     IISTPSNKDK FEKVLEENKH LDRFVREREM PILNYQTIDV DGFKLNVLER RPPHFNEKKK
     YPVLFYQYSG PNSQEVNKKF HVDFQAYVAA NLGYIVVTVD GRGTGFLGRK LRCITRGNLG
     YYEAHDQIAA AKIWASKKYV DADRLAIWGW SFGGFNTLKT LEQDGGQTFK YGMAVAPVTD
     WRYYDSIYTE RFMHMPQNNA AGYDNSTITD VASLAKNTRF LIMHGVADDN VHMQNTLTLL
     DRLDLAGVEN YDVHVFPDSD HSIYFHNANR IVYDKLRWWL INAFNGEWAK IKTAEPKSQV
     DARLERR