DAPB_TUBMM
ID DAPB_TUBMM Reviewed; 907 AA.
AC D5GM60;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=GSTUM_00010539001;
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28;
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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; FN430352; CAZ85603.1; -; Genomic_DNA.
DR RefSeq; XP_002841412.1; XM_002841366.1.
DR AlphaFoldDB; D5GM60; -.
DR SMR; D5GM60; -.
DR STRING; 656061.D5GM60; -.
DR ESTHER; tubmm-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; CAZ85603; CAZ85603; GSTUM_00010539001.
DR GeneID; 9187387; -.
DR KEGG; tml:GSTUM_00010539001; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; D5GM60; -.
DR OMA; MRTPQEN; -.
DR Proteomes; UP000006911; 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..907
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412166"
FT TOPO_DOM 1..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..907
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 746
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 823
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 856
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 907 AA; 102621 MW; 137143AE5B685B7F CRC64;
MYDQVPYRDT DEATPQIKND ASDSNRSSID TTSTTSLILE RLHREDPDDS PGEYESSGPS
QRGKPDEDDD LEIGRAARLK PMERKVRRAM YLLAFLMIGG WFLALAVYVS REHFGTPDTA
HDPSATATRK AGKKITLNQV MRGAWRSKTH GIQWINGPHG DQDGLLLTQN SFGDGNFLEV
QDVKNDSNTI VLIKDGALQG SGQPVSAIKG WPSSDLKKVL VASDHEKRWR HSYNARYWIY
DVEKATTEPL VPSEPEARLS LATWSPKGDA IAFVKDNNVF IRQLGLDLTS EYYSVTQVTK
DGGPDLFYGI PDWVYEEEVF SGNSALWWSQ DGEFLAFLRT NETEVPEYPI QYFVSRPSGN
NPPNGLENYP ELEFIKYPKA GAPNPVVHLR FYDLKKKEDF AVTVENDFPD DDRLITEVVW
SDGKYLLVRE TNRESDVLRM VLIDVSARSG KVVREVDISA IDGGWFEVSK NTRYIPADPA
SGRPYEGYID TVIHEGYDHL GYFTPLDNKD PILLTKGQWE VVDAPSAVDL KNGIVYFVAT
EKSPIERHVY SVKLDGSNFR PVTSTSEDGR YDVSFSKLSG YALLTYEGPG IPWQKVVGTP
SGDQSFVKDI EKNQGLATLA AKHELPTFHY STVNIDGFDL HVVERRPPHF NKKRKYPVLF
QVYGGPGSQQ VSKSFSIDFQ AYIAAGLEYI VVTVDGRGTG FIGRKARVAV RGNLGYWEAH
DQIETAKIWG KKGYVDKKRI AIWGWSYGGF MTLKTLEQDA GRTFSYGMAV APVTDWRFYD
SIYTERYMHT PQHNQEGYRN ATISDTQALS KSVRFLLMHG VADDNVHMQN SLALLDKLDL
ASVENYDVHV FPDSDHSIYF HNANRMVYDR LEQWLIRAFN GEFLKLDGLK PIREISEPLR
KRNRELV
