DAPB_ARTOC
ID DAPB_ARTOC Reviewed; 919 AA.
AC C5FYZ3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=MCYG_07560;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
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; DS995707; EEQ34741.1; -; Genomic_DNA.
DR RefSeq; XP_002843777.1; XM_002843731.1.
DR AlphaFoldDB; C5FYZ3; -.
DR SMR; C5FYZ3; -.
DR STRING; 63405.XP_002843777.1; -.
DR ESTHER; artoc-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; EEQ34741; EEQ34741; MCYG_07560.
DR GeneID; 9225176; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000002035; 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..919
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412131"
FT TOPO_DOM 1..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..919
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 760
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 837
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 870
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
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 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
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"
SQ SEQUENCE 919 AA; 103544 MW; ECAF6F5752D96F70 CRC64;
MGANSRVNDD EAMPLTGHGA GSRDSIDSSS TASISLTLVD GASHTATEPS KSTNGHKSHT
EGSYVNEKYH DSEEESWRED GYVPSGGKPA QRRTRIVFWL LVALCVGGWA MAFIIMATSP
NNRHSTSDSS SGGSESEIVK PNTPHDGKKI PLDDVLGGMW GPVEHTISWI SGPKGEDGLL
LQKSEGGIGP YLHIEDVRNI HGMRANNNSI VLMKESVFFV NDERISPEKV WPSPDLKTVL
AMTREKKNWR HSFTGLYWLF DVETQTAQPL DPEAPNGRVQ LASWSPTSDA VVFTRDNNIY
IRNLTSKAVK PITTDGGANL FYGIPDWVYE EEVFEGNSAT WWSLDGKYIS FLRTNETMVP
EFPIDFYLSR PPGYTPEPGE EAYPYVQQIK YPKAGAPNPT VNLQFYDVER EESFSVNVDN
NLKDDDRIIA EVIPASGGKM LVRETNRESY IVKVTVIDAA KREGKMVRSD NVDEIDGGWV
EPSHSTTYIP SDPSAGRPHD GYIDTIIHEG YNHLAYFTPV ENPKPMMLTT GNWEVVDAPS
GVDLKNNVVY FVATKESPID RHVYSVKLDG SELQMLNDSE KSAYYDVSFS NGAGYMLLKY
QGPNIPWQKL ISSPSNEDFY DEIIEENKNL ARLSNEFSLP SLHYSTITVD GFKLPVVERR
PPNFNETKKY PVLFHLYGGP GSQTVNKKFT VNFQTYVASN LGYLVVTVDG RGTGFNGRKF
RCIVRRNLGY YEAHDQIQTA KEWGKKPYVD KTRIAIWGWS YGGFMTLKTL EQDAGETFQY
GMAVAPVTDW RFYDSVYTER YMHMPQHNTE GYENASISNA TSLSQNTRFL IMHGSADDNV
HFQNTLTLLD KLDIMGMHNY DVHVFPDSNH GIYFHHAYKM VHQRLSDWLV NAFNGEWVRL
RNPKPSGLKR VIRRLLHFG
