DAPB_BOTFB
ID DAPB_BOTFB Reviewed; 921 AA.
AC A6SL49;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=dapB; ORFNames=BC1G_13641;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
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).
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; CH476961; EDN19610.1; -; Genomic_DNA.
DR RefSeq; XP_001547950.1; XM_001547900.1.
DR AlphaFoldDB; A6SL49; -.
DR SMR; A6SL49; -.
DR ESTHER; botfb-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR PRIDE; A6SL49; -.
DR GeneID; 5428447; -.
DR KEGG; bfu:BCIN_15g01570; -.
DR VEuPathDB; FungiDB:Bcin15g01570; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
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 Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW 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 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..156
FT /note="Polar residues"
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
