ID   DAPB_ARTBC              Reviewed;         909 AA.
AC   D4AQT0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=ARB_06590;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10084};
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; ABSU01000005; EFE34824.1; -; Genomic_DNA.
DR   RefSeq; XP_003015464.1; XM_003015418.1.
DR   AlphaFoldDB; D4AQT0; -.
DR   SMR; D4AQT0; -.
DR   STRING; 663331.D4AQT0; -.
DR   ESTHER; artbc-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; D4AQT0; 8 sites, No reported glycans.
DR   GeneID; 9521191; -.
DR   KEGG; abe:ARB_06590; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IPR002471; Pept_S9_AS.
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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 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..909
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412129"
FT   TOPO_DOM        1..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..909
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        760
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        837
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        870
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        814
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        819
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        822
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        888
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   909 AA;  102308 MW;  42AF0D1B44FB8434 CRC64;
     MRVGSRINDE EAMPLTAPES RARDSIDSSS TASISLTLVE GASHATTEPS KPAHNHNGRA
     QGNYAEKYRD DLEEDWEEDN YIPSNGKSNQ RRTLIVFWLL VALCVGGWAV AFLFFVTSPG
     NKTSTSPHSG SNSPEGDVTK PGIPATGKKI PLDDAIGGVW SPAEHTISWI TGAKGEDGLL
     LQKSEGGTGP YLHVEDVRNI HGTQSNNNSI VLMKESVFFV NDERISPEKV WPSPDLKTVL
     AMTREKKNWR HSFTGLYWLF DVETQTAQPL DPDAPNGRIQ LATWSPTSDA VAFTRDNNLY
     IRNLTSKSVK AITTDGGTNL FYGIPDWVYE EEVFEGNCAT WWSLDGKYIS YLRTNETLVP
     EFPIDFYLSS PPGYSPKPNE ESYPYVQQIK YPKAGAPNPT VNLQFYDVER EESFSVDVKD
     TLKDDDRLIV EVIPGSKGKV LVRETNRESY IVKVAVIDAN KREGKIVRSD NIDEIDGGWV
     EPSHTTTYIP ADPSAGRPDD GYIDTVIHEG YIHLAYFTPL ENPKPKMLTT GKWEVVAAPS
     GVDLKNNVVY FVATKESPID RHVYSVKLDG SELQMLKDSD KSAYYDVSFS HGAGYMLLKY
     QGPQIPWQKL ISSPSNADNY IEILEENKKL AKLSNEFSLP SLHYSTINVD GFELPVVERR
     PPNFDETKKY PVLFQLYGGP GSQTVNKKFL VNFQTYVASS LGYIVVTVDG RGTGFNGRKF
     KCIVRRNLGH YESHDQIQAA KAWGKKPYVD KTRMAIWGWS YGGFMTLKTL EQDAGETFQY
     GMAVAPVTNW RYYDSVYTER YMHMPQNNEG GYENASISNA TNLSQNTRFL IMHGSADDNV
     HFQNTLTLLD KLDILGVHNY DMHVFPDSNH GIYFHHAYKM VHQRKYFNLS FLGHGFFSFY
     SNFLPIRSF
//