ID   DAPB_PYRO7              Reviewed;         938 AA.
AC   A4QYQ5; G4N0L8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=MGG_07745;
OS   Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Magnaporthe oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001233; EHA53149.1; -; Genomic_DNA.
DR   RefSeq; XP_003712956.1; XM_003712908.1.
DR   AlphaFoldDB; A4QYQ5; -.
DR   SMR; A4QYQ5; -.
DR   STRING; 242507.A4QYQ5; -.
DR   ESTHER; mago7-dapb; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; A4QYQ5; 3 sites, No reported glycans.
DR   EnsemblFungi; MGG_07745T0; MGG_07745T0; MGG_07745.
DR   GeneID; 2683672; -.
DR   KEGG; mgr:MGG_07745; -.
DR   VEuPathDB; FungiDB:MGG_07745; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; A4QYQ5; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
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..938
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412147"
FT   TOPO_DOM        1..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..938
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        765
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        842
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        875
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        824
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   938 AA;  105281 MW;  394BD6652B2C8283 CRC64;
     MPVDKKSGNG RPSLDSVSSI STTSIVFDHL NDLEIHKKHR PHLMTESIRR DDHLSDFDDD
     DPLKQEMDGE GDLETGPFLA GRDAYTFGGG KYMDRKFRRI MIVVAGLLVA AWVGGLFVYI
     ASKSYKHATT VEHDPEKTKA AALTSGKKIT MDQVRSGTWY AASHDITWIA GPKGEDGLMI
     EVGADGKDYI VIEDGRAENP DSSAEAEVDV TASRRTLMKN GSFRYQGRMH IPSGAEPSRD
     QQKVLLRTEQ KSNWRHSHTA CYWIWDVATE TAEPLIPASP DARVQNAQWS PTSDAIVFTR
     ENNLYLRTIG SKKVTQITKD GGADLFYGVP DWVYEEEVIA GASTTWWSED GKYVAFLRTN
     ETGVPAFPVQ YFMSRPSGAS PKAGEETYPE VRDIKYPRSG SHNPVVDVQF YDIARGDVFT
     VDINGGFADE DRLITTVLWA GSQVIVKETN RVSDIMRVVL IDVKKRTGKT TRTVDVGKID
     GGWFEISQNT KYIPADPKKG RDQDGYIDTV IHNDGDHLAY FSPPDNPDPI MLTSGPGWEV
     VDAPSAVDLE NNLVYFIATK EGSTQRHVYS VQLDGKNMKS FTDTEAKGYY DVSFSSGAGY
     ALLSYKGPKI PWQKVVSTPA NNQRYEVLIE ENKELAESAR KYDLPLLNYG TLNVEGVELN
     YLERRPPQFS EKKKYPVLFH QYSGPGSQSV SQKFSVDFQS YVAASLGYIV VTFDGRGTGF
     IGRKNRVLVR SRLGEIEAQD QIAAAKHWAS LGYVDPSRIA IWGWSYGGFQ TLKTLEADAG
     RTFSYGMAVA PVTDWRFYDS IYTERYMLTP QQNEDGYTKS AVHNVSALAS NKRFLLMHGA
     SDDNVHFQNS LTLLDKLDMG AVENYDVHVF PDSDHSIFFH NANKIIYDKL ENWLVNAFNG
     EWLKVNNAKP VELVHPTQLV REREKAKLRK RWQEIQNK
//