ID   DAPB_ARTGP              Reviewed;         917 AA.
AC   E4UYL6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=MGYG_05182;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS989825; EFR02179.1; -; Genomic_DNA.
DR   RefSeq; XP_003172590.1; XM_003172542.1.
DR   AlphaFoldDB; E4UYL6; -.
DR   SMR; E4UYL6; -.
DR   STRING; 535722.E4UYL6; -.
DR   ESTHER; artgp-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; E4UYL6; 4 sites, No reported glycans.
DR   GeneID; 10027863; -.
DR   VEuPathDB; FungiDB:MGYG_05182; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; E4UYL6; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000002669; 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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; 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.
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..917
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412130"
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..917
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..68
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        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
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   917 AA;  103346 MW;  68958EEB003D17D8 CRC64;
     MTVGRRLNDE EAIPLTAKEA GSRDSIDSSS TASVSLTLVD GTNHTTAKPS KSAHKGVSRD
     RYADEKYRDD VEEDWEEDRY IPSNAKPSQR RTQIVFWLLV ALCVGGWAVA FLFFVTSPGN
     TISTTPDTGS GSPDSDVIKP GSPPAGKKIP LDDVLGGAWS PTQHTISWIA GPKGEDGLLL
     QKSEGGTGPY LHVEDVRNIH GTQSNNKSMV LMKDSVFFVN DERISPEKVW PSPDLKTVLA
     MTRQKKNWRH SYTGLYWLFD VETQTAQPLD PGAPNGRIQL ATWSPTSDAV AFTRDNNLYI
     RNLTSKTVKA ITTDGGANLF YGIPDWVYEE EVFEGNSATW WSLDGKYISF LRTNETTVPE
     FPVDFYLSSP PDYAPKPGEE AYPYVQQIKY PKAGAPNPTV GLQFYDVERE ESFSVDVKDS
     LNDDDRIIIE VIPGSNGRIL VRETNRESYI VKVAAIDATK REGKIIRSDN IDEIDGGWVE
     PSHTTTYIPS DPASGRPNDG YIDTVIHEGY NHLAYFTPLE NPKPKMLTTG KWEVVAAPSG
     VDLKNNVIYF VATKESPIDR HVYSVKLDGS ELQLLKDSEK SAYYDVSFSH GAGYMLLQYQ
     GPKIPWQKLM NSPSNTDSYT EILEENKRLA KLSNEFALPS LHYSSITVDG FKLPVVERRP
     PNFDETKKYP VLFHLYGGPG SQTVNKKFLV NFQTYVASTL GYIVVTVDGR GTGFNGRKFR
     CIVRRNLGHY EAYDQIQTAK AWGRKPYVDK TRIAIWGWSY GGFMTLKTLE QDAGETFQYG
     MAVAPVTDWR YYDSIYTERY MHMPQNNEEG YETASVSNST ALSQNTRFLI MHGSADDNVH
     FQNTLTLLDK LDIMGVHNYD MHVFPDSNHG IYFHHAYKMV HQRLSDWLVN AFNGEWVRLR
     DPKPTIIKRV IRRLLHR
//