ID D5G8I4_TUBMM Unreviewed; 476 AA.
AC D5G8I4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ80831.1};
GN ORFNames=GSTUM_00002887001 {ECO:0000313|EMBL:CAZ80831.1};
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:CAZ80831.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ80831.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ80831.1,
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR037242-3};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR037242-3};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; FN430046; CAZ80831.1; -; Genomic_DNA.
DR RefSeq; XP_002836640.1; XM_002836594.1.
DR AlphaFoldDB; D5G8I4; -.
DR STRING; 656061.D5G8I4; -.
DR MEROPS; M20.017; -.
DR EnsemblFungi; CAZ80831; CAZ80831; GSTUM_00002887001.
DR GeneID; 9186051; -.
DR KEGG; tml:GSTUM_00002887001; -.
DR eggNOG; KOG2276; Eukaryota.
DR HOGENOM; CLU_029469_3_0_1; -.
DR InParanoid; D5G8I4; -.
DR OMA; HITIPGF; -.
DR OrthoDB; 177966at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0008242; F:omega peptidase activity; IEA:EnsemblFungi.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:EnsemblFungi.
DR CDD; cd05676; M20_dipept_like_CNDP; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF4; CARNOSINE DIPEPTIDASE 2, ISOFORM A; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|PIRSR:PIRSR037242-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037242-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 219..366
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 100
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 195
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 228
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 330
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 343
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 417
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 445
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT SITE 228
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
SQ SEQUENCE 476 AA; 52449 MW; 46F812F28B8B13ED CRC64;
MAPQLDGYFK QVDLMADSFI NRLRSAVAIP SVSADPGLRP KVVAMADFLE KELRALGASV
ERRLPGKQPG HPDLDLPPIL LGRYGNDAKK RTILVYGHYD VQPALKEDGW ATEPFDLTVD
EQGRMYGRGS TDDKGPVLGW INSIEAHQKA GVDFPVNLLM CFEGMEEYGS EGLDDVIKEE
ASKFFKDAEA VCISDNYWLG TKKPCLTYGL RGCSYYSLAV SGPGQDLHSG VFGGTVTEPM
TDLVRLLATL VGNKGKIHIP GLNELVAPLT DEEKELYKDI SFEMSDLYQS LGSETSIYLN
KEDTLMARWR FPALSIHGIE GAYSAPGAKT VIPAKVIGKF SIRTVPNMEP DKVDELVFKF
VDAEWKKLGS NNTMKCELQH SGNWWVASPK HWNFSAAGKA VEKVFGVKPD FTREGGSIPV
TLTFEQATGK NVLLLPMGSS TDAAHSINEK LDKRNYIEGT KLLGAYLHYV AEEEQV
//
