ID   DAPB_SCLS1              Reviewed;         921 AA.
AC   A7EQZ1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=SS1G_07744;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
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}.
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; CH476630; EDN91883.1; -; Genomic_DNA.
DR   RefSeq; XP_001591119.1; XM_001591069.1.
DR   AlphaFoldDB; A7EQZ1; -.
DR   SMR; A7EQZ1; -.
DR   STRING; 665079.A7EQZ1; -.
DR   ESTHER; scls1-dapb; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GeneID; 5487167; -.
DR   KEGG; ssl:SS1G_07744; -.
DR   VEuPathDB; FungiDB:sscle_11g083720; -.
DR   InParanoid; A7EQZ1; -.
DR   OMA; MRTPQEN; -.
DR   Proteomes; UP000001312; 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; IBA:GO_Central.
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..921
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412162"
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   COMPBIAS        7..33
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;  103235 MW;  5425BDA802477FD3 CRC64;
     MAGHTEENAQ LLSTEQESVS RHSSDSAAST ASTTSLVFDR IGERVAANRS EKSMMVTPKF
     PPRGEMAYAD DEHTQIHLDE EEEKDYDLED SAFLTNGATN KSVDKKLRKL IWIVGGVFIG
     AWVLALFIFL GKQAYKHSSE IPHDPQATSS RGNGKKVTMD QVMGGQWRAT KHSISWIAGA
     NGEDGLLLEQ GSAGKDYLIV EDVRTQNPET VGTLDRMTLM KDGSFTVAGR SLYPSKVYPS
     KDLKKVLVAT DVQSNWRHSF YAKYWIFDVE SQTAEPLDPV DLDGRVQLAS WSPKSDAIVF
     TRDNNMYLRK LSSPTVIQIT TDGGPEFFYG VPDWVYEEEV FAGASATWWD DSGKYIAFLR
     TNESEVPEYP IQYFVSRPSG KEPLPGEENY PEVREIKYPK AGAPNPTVDL LFYDIFKAEV
     FEVTIAGGFE PKNLLITEVV WAGSTGKALI RETNRESDIL RVVLVDVVAR EGKTVRYTDI
     NKLDGGWFEV SEDTRYIPAD PANGRPHDGY IDTIIHENYD HLGYFTPMDN PEPILLTSGN
     WEVVQAPSAV DLKNNLVYFV STKESPITRQ VYSVKLDGTD MKAITDTSNE GYYGASFSKG
     AGYVLLNYNG PGIPWQKVIS TPSNGNQYTH TIEENKGLAE MAKKHDLPIL IYQTVTIDGF
     ELQVVERRPP HFNPKKKYPV LFYLYGGPGS QTVSKSFNVD FESYIASNLG YIVVTVDGRG
     TGFIGRKART IIRGNIGHYE ARDQIETAKI WASKKYVDAS RMAIWGWSYG GFMTLKTLEE
     DAGETFSYGM AVAPVTDWRF YDSIYTERYM HTPQHNPGGY DNTSISNVEA LSKNVRFLVM
     HGVADDNVHM QNTLTLLDKL DLAGVENYDV HVFPDSDHSI YFHNANRIVY DKLNNWLINA
     FNGEWLRTAN AVPLQIDAAK V