ID D5GL16_TUBMM Unreviewed; 878 AA.
AC D5GL16;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=GSTUM_00009912001 {ECO:0000313|EMBL:CAZ85209.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ85209.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ85209.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85209.1,
RC ECO:0000313|Proteomes:UP000006911};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; FN430344; CAZ85209.1; -; Genomic_DNA.
DR RefSeq; XP_002841018.1; XM_002840972.1.
DR AlphaFoldDB; D5GL16; -.
DR STRING; 656061.D5GL16; -.
DR MEROPS; M01.007; -.
DR EnsemblFungi; CAZ85209; CAZ85209; GSTUM_00009912001.
DR GeneID; 9185803; -.
DR KEGG; tml:GSTUM_00009912001; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; D5GL16; -.
DR OMA; MENWGVV; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR GO; GO:0005771; C:multivesicular body; IEA:EnsemblFungi.
DR GO; GO:0061957; C:NVT complex; IEA:EnsemblFungi.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0120113; P:cytoplasm to vacuole transport by the NVT pathway; IEA:EnsemblFungi.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 25..209
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 243..460
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 532..851
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 401
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 878 AA; 98473 MW; 2D9DD72D8F719247 CRC64;
MCCGNDSSGS VDITQGREVL PGNVKPTHYA VELEPSFETF KYDGTVTIDL AVVKNSTTVA
VNLIDIDIKE VSLEYNGSSH SPTDSSHDEE TQTITWTFEE TIPEDTQASL TIKFQGFLND
NMAGFYRSSY KDEEGNIKYM ATTQMEPTDA RRALPCFDQP DLKATWDVTL ICDKNLTALS
NMDVKEEKEL DNGKKSVSFN RSPKMSTYLL AFIVGDLRFV ENNDFRVPIR VYATPGSEHH
GLFSAELAAK TLEFYDKTFD YPYPLPKMDM VAIPDFSAGA MENWGLVTYR VVDLLYDEKT
AALDRKQRIA EVVQHELAHQ WFGNLVTMDF WEGLWLNEGF ATWMSWYSGN KFYPQWKVWE
SYVTDSYAGA LGLDGLRSSH PIEVPVKKVS EINQIFDSIS YLKGSSILRM ISVYLGEDVF
LEGVRRYLRK HAYGNTQTGD LWAALSDASG KHVESDMATW TKKIGYPVIT VEEQGSKLHL
TQNRYLRTAD VKPEEDETLW PIFLGLRTKS GIADNLTFKT RDTTIELDDP EFYKLNANHT
GVYRTLYPPE RLAKLGQAAD LLSVEDRAGL LGDAGALATS GYQKTSGLLD LLVGLKNEKE
YIVWSEVASR IGNIKAAWLF EPKEVFKGFR GLQKDLFAPI AHEIGWDFKP EDSDILQQLK
ALTFGQAGYG GDEEVVAAAK EMFKKFADGD VDAINPNIRT PVYHIVLQHG DNDGEKEWDI
IHNVYLNGRT SDQRNGALRA LGRSENAENI QKTLDICLNG EVKEQDIYQP ISGLRAHAAG
TEALWAWTQK NWDTLVKKLP PGLSMLGGVV STCTGGFTSE ESIANIEKFF EDKSQKGFDR
SLAQSLDGIR AKAAWVKRDA DDVKAWLKAK GYTSAEKL
//
