DAPB_MAGO7
ID DAPB_MAGO7 Reviewed; 938 AA.
AC A4QYQ5; G4N0L8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=MGG_07745;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001233; EHA53149.1; -; Genomic_DNA.
DR RefSeq; XP_003712956.1; XM_003712908.1.
DR AlphaFoldDB; A4QYQ5; -.
DR SMR; A4QYQ5; -.
DR STRING; 318829.MGG_07745T0; -.
DR ESTHER; mago7-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; MGG_07745T0; MGG_07745T0; MGG_07745.
DR GeneID; 2683672; -.
DR KEGG; mgr:MGG_07745; -.
DR VEuPathDB; FungiDB:MGG_07745; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; A4QYQ5; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
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..938
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412147"
FT TOPO_DOM 1..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..938
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT ACT_SITE 765
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 842
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 875
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 938 AA; 105281 MW; 394BD6652B2C8283 CRC64;
MPVDKKSGNG RPSLDSVSSI STTSIVFDHL NDLEIHKKHR PHLMTESIRR DDHLSDFDDD
DPLKQEMDGE GDLETGPFLA GRDAYTFGGG KYMDRKFRRI MIVVAGLLVA AWVGGLFVYI
ASKSYKHATT VEHDPEKTKA AALTSGKKIT MDQVRSGTWY AASHDITWIA GPKGEDGLMI
EVGADGKDYI VIEDGRAENP DSSAEAEVDV TASRRTLMKN GSFRYQGRMH IPSGAEPSRD
QQKVLLRTEQ KSNWRHSHTA CYWIWDVATE TAEPLIPASP DARVQNAQWS PTSDAIVFTR
ENNLYLRTIG SKKVTQITKD GGADLFYGVP DWVYEEEVIA GASTTWWSED GKYVAFLRTN
ETGVPAFPVQ YFMSRPSGAS PKAGEETYPE VRDIKYPRSG SHNPVVDVQF YDIARGDVFT
VDINGGFADE DRLITTVLWA GSQVIVKETN RVSDIMRVVL IDVKKRTGKT TRTVDVGKID
GGWFEISQNT KYIPADPKKG RDQDGYIDTV IHNDGDHLAY FSPPDNPDPI MLTSGPGWEV
VDAPSAVDLE NNLVYFIATK EGSTQRHVYS VQLDGKNMKS FTDTEAKGYY DVSFSSGAGY
ALLSYKGPKI PWQKVVSTPA NNQRYEVLIE ENKELAESAR KYDLPLLNYG TLNVEGVELN
YLERRPPQFS EKKKYPVLFH QYSGPGSQSV SQKFSVDFQS YVAASLGYIV VTFDGRGTGF
IGRKNRVLVR SRLGEIEAQD QIAAAKHWAS LGYVDPSRIA IWGWSYGGFQ TLKTLEADAG
RTFSYGMAVA PVTDWRFYDS IYTERYMLTP QQNEDGYTKS AVHNVSALAS NKRFLLMHGA
SDDNVHFQNS LTLLDKLDMG AVENYDVHVF PDSDHSIFFH NANKIIYDKL ENWLVNAFNG
EWLKVNNAKP VELVHPTQLV REREKAKLRK RWQEIQNK
