ID   DAPB_METAQ              Reviewed;         934 AA.
AC   E9ED72;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   02-SEP-2026, entry version 53.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=MAC_07820;
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102;
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(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; GL698555; EFY86155.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9ED72; -.
DR   SMR; E9ED72; -.
DR   FunCoup; E9ED72; 303.
DR   STRING; 655827.E9ED72; -.
DR   ESTHER; metaq-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; E9ED72; 3 sites, No reported glycans.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; E9ED72; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 16520at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
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..934
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412148"
FT   TOPO_DOM        1..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..934
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..32
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        759
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        836
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        869
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        818
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   934 AA;  104515 MW;  89ED7648E4BC6754 CRC64;
     MAPPFTDDPE SQRPSTSRLS QDSLSSVSTT SLVFDRIQEE MDRDPSSSRS ARRDLLSATK
     DEGDYEDASE TGAFLGQPGV PLQRQPMDRG FRRILIIIGA VFVGAWLAGL GVFVLSGSYR
     HESDSEHDPD AISRGSGKAV TMDQVFGGFW SAKSRSISWI ADPDGGDGLL LEVGTANGYL
     VVEDVRADKQ GTDTTSRQTA DTQPAKPRVL MKDPYFMYNG EIKRPEWNEP SPDLKKVLLA
     VNLEKNWRHS FQATYFILHV ETAQIQPLVP DNVNAKVQLA NWSPKSDAIS FTMDNNIYIR
     RLNQANDVVQ ITKDGGPEYF YGIPDWVYEE EVLAGRSATW WSDDGNYLAF LRTNETAVPE
     YAIEYYIQRP SGKKPAVGEE AYPEIRKIKY PKPGAHNPVV DVQYYDVSKG DVFSISAPDE
     FPDKDRIISN VLWAGNKVLL KQSNRVGDFL KVILVDPSER KAKIVNSINI AEIDGGWFEI
     SHTMTYIPAD PSKGRQQDGY VDTVIHEGYE HIGYFTPIDN PKPIMLTSGS WEVEDAPSAV
     DLDNNLVYFV ATKESSIQRH VYSVKLDGSN LTPLTNTSSE GYYAVSFSSR SGFALLSYQG
     PKIPYQKVIS TPSIPIEFSR TIEDNAGLAD KAKKHELPIL KYGTLQLPNG ISVNYLERRP
     PHFNPKKKYP ILFQQYSGPK SQTVTKKFAV NFQSYVASSL GYLVVTIDPR GTGFLGRQHR
     VVVRSQLGVL EAQDHIAAAK HYSSLPYVDP SRLAIWGWSY GGFQTLKTLE VDAGDTFSYG
     MAVAPVTDWR FYDSIYTERY MRLPQDNAAG YDASAVHNAT ALGMSKRFLI MHGSADDNVH
     FQNSLKLLDY LDLARIENYD VHVFPDSDHG IAFHGANRMV YDSKSEFSVL FSWILSPMLT
     LSGLNNWLVN AFNGEWLKIA DPKPIDTKKR RHVS
//