ID   DAPB_BOTFB              Reviewed;         921 AA.
AC   A6SL49; A0A384K439;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   04-NOV-2026, entry version 89.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=BC1G_13641, BCIN_15g01570;
OS   Botrytis cinerea (strain B05.10) (Noble rot fungus) (Botryotinia
OS   fuckeliana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=B05.10;
RX   PubMed=23104368; DOI=10.1128/ec.00164-12;
RA   Staats M., van Kan J.A.L.;
RT   "Genome update of Botrytis cinerea strains B05.10 and T4.";
RL   Eukaryot. Cell 11:1413-1414(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=B05.10;
RX   PubMed=26913498; DOI=10.1111/mpp.12384;
RA   van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L.,
RA   Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D.,
RA   Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.;
RT   "A gapless genome sequence of the fungus Botrytis cinerea.";
RL   Mol. Plant Pathol. 18:75-89(2017).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP009819; ATZ57595.1; -; Genomic_DNA.
DR   RefSeq; XP_001547950.1; XM_001547900.2.
DR   AlphaFoldDB; A6SL49; -.
DR   SMR; A6SL49; -.
DR   ESTHER; botfb-dapb; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; A6SL49; 2 sites, No reported glycans.
DR   EnsemblFungi; Bcin15g01570.1; Bcin15p01570.1; Bcin15g01570.
DR   GeneID; 5428447; -.
DR   KEGG; bfu:BCIN_15g01570; -.
DR   VEuPathDB; FungiDB:Bcin15g01570; -.
DR   OMA; AAAKMWS; -.
DR   OrthoDB; 16520at2759; -.
DR   Proteomes; UP000001798; Chromosome 15.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   FunFam; 3.40.50.1820:FF:000003; Dipeptidyl peptidase 4; 1.
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_fold.
DR   InterPro; IPR001375; Peptidase_S9_cat.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   InterPro; IPR050278; Serine_Prot_S9B/DPPIV.
DR   PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE 10, ISOFORM B; 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..921
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412140"
FT   TOPO_DOM        1..109
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..921
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..33
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        768
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        845
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        878
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        822
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   921 AA;  103088 MW;  8839279EA0C373D8 CRC64;
     MAGHPEENAQ LLSTEQESMS RNSSDSVAST ASTTSLVFDR IGERVAANGS EKPTMVTPKF
     PPRGERAYAD DEHTQIHLEE EEEKDYDMED GAFLTNGATN KSVDKKLRRL IWIIGGVFIG
     AWVLALFIFL GKQAYKHSSE SPHDPQATSS RGSGKKVTMD QVMGGQWRAT KHSISWIEGA
     NGEDGLLLEQ GSVGKDYLIV EDVRTQSPSA VGTLDTMTLM KNGYFEVAGR SLTPSKVYPS
     KDLKKVLVAT DVQSNWRHSF YAKYWIFDVE TQTAEPLDPV DLDGRVQLAS WSPKSDAIVF
     TRDNNMYLRK LASPTVVQIT VDGGPEFFYG VPDWVYEEEV FAGASATWWD DSGKYIAFLR
     TNESEVPEYP VQYFVSRPSG KDPLPGEENY PEVREIKYPK AGAPNPTVDL LFYDISKAEV
     FEVKIAGGFE PKDLLITEVV WAGSTGKALI RETNRESDVL RVVLVDVVAR EGKTVRFTDI
     AKLDGGWFEV SEDTRYIPAD PANGRPHDGY IDTIIHENYD HLGYFTPMDN SEPILLTSGD
     WEVVKAPSAV DLKNNIVYFI STKESPITRQ LYSVKLDGTD LKAITDTSTE GYYGASFSKG
     AGYVLLNYNG PNIPWQKVIS TPSNDNQYTH IIEENKGLAD MAKKHELPIL IYQTVTVDGF
     ELQVVERRPP HFNPKKKYPV LFYLYGGPGS QTVSKSFGVD FQSYIASNLG YIVVTVDGRG
     TGFIGRKART IIRGNIGHYE ARDQIETAKI WASKKYVDES RMAIWGWSYG GFMTLKTLEQ
     DAGETFSYGM AVAPVTDWRF YDSIYTERYM HTPQHNPGGY DNTSISDVKS LAKNVRFLVM
     HGVADDNVHM QNTLTLLDKL DLAGVENYDV HVFPDSDHSI YFHNANRIVY DKLNNWLINA
     FNGEWLRTAN AVPLEIDAAK V
//