DAPB_ARTBC
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 03-AUG-2022, entry version 48.
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 EnsemblFungi; EFE34824; EFE34824; ARB_06590.
DR GeneID; 9521191; -.
DR KEGG; abe:ARB_06590; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR Proteomes; UP000008866; 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; 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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
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.
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
