DAPB_ARTGP
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 03-AUG-2022, entry version 46.
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; 63402.XP_003172590.1; -.
DR ESTHER; artgp-dapb; DPP4N_Peptidase_S9.
DR PRIDE; E4UYL6; -.
DR EnsemblFungi; EFR02179; EFR02179; MGYG_05182.
DR GeneID; 10027863; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; E4UYL6; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000002669; 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: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..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
