ID A0A0C3PJ98_PISTI Unreviewed; 436 AA. AC A0A0C3PJ98; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 22-FEB-2023, entry version 24. DE RecName: Full=Cupin type-1 domain-containing protein {ECO:0000259|SMART:SM00835}; GN ORFNames=M404DRAFT_12093 {ECO:0000313|EMBL:KIO14220.1}; OS Pisolithus tinctorius Marx 270. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus. OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO14220.1, ECO:0000313|Proteomes:UP000054217}; RN [1] {ECO:0000313|EMBL:KIO14220.1, ECO:0000313|Proteomes:UP000054217} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO14220.1, RC ECO:0000313|Proteomes:UP000054217}; RG DOE Joint Genome Institute; RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A., RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B., RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N., RA Hua S.X.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000054217} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217}; RG DOE Joint Genome Institute; RG Mycorrhizal Genomics Consortium; RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W., RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A., RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A., RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.; RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR617774-2}; CC Note=Binds 2 manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR617774-2}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KN831945; KIO14220.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0C3PJ98; -. DR STRING; 870435.A0A0C3PJ98; -. DR HOGENOM; CLU_030515_2_0_1; -. DR OrthoDB; 2358302at2759; -. DR Proteomes; UP000054217; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0033609; P:oxalate metabolic process; IEA:InterPro. DR CDD; cd20305; cupin_OxDC_C; 1. DR CDD; cd20304; cupin_OxDC_N; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 2. DR InterPro; IPR017774; Bicupin_oxalate_deCO2ase/Oxase. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR35848:SF6; CUPIN_2 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR35848; OXALATE-BINDING PROTEIN; 1. DR Pfam; PF00190; Cupin_1; 2. DR SMART; SM00835; Cupin_1; 2. DR SUPFAM; SSF51182; RmlC-like cupins; 1. DR TIGRFAMs; TIGR03404; bicupin_oxalic; 1. PE 4: Predicted; KW Manganese {ECO:0000256|PIRSR:PIRSR617774-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR617774-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000054217}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..436 FT /note="Cupin type-1 domain-containing protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002167982" FT DOMAIN 99..242 FT /note="Cupin type-1" FT /evidence="ECO:0000259|SMART:SM00835" FT DOMAIN 277..416 FT /note="Cupin type-1" FT /evidence="ECO:0000259|SMART:SM00835" FT REGION 22..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 380 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR617774-1" FT BINDING 142 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2" FT BINDING 144 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2" FT BINDING 148 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2" FT BINDING 187 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2" FT BINDING 322 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2" FT BINDING 327 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2" FT BINDING 366 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2" SQ SEQUENCE 436 AA; 47393 MW; 537A775A2FFE67BD CRC64; MYSWSLLSIL TILSTALAAP ASSETSSAPA PSPTVPYASD DPNYPLWNPE SDITPEPIRS GLGATILGPQ NVPVELQNPD VLAPPTTDNG AVPNFKWPFS LSHNRLQTGG WAREQNVNVM PVATDIAGVN MRLEAGAIRE LHWHTDAEWA YMLSGYVRVS TVTPDGQVYL ADVGPGDLWY FPPGFPHSIQ AKNTTEEGAE FLLIFDNGSF SEDSTFLLTD WLAHVPKEVI AKNFQTDISA FDRIPSHELY ILPSHPPPAD VATDMVVPND TPIPYTFPMS QVEGTKTAGG TYKVVDSRTF TAATTICAAE VTVEVGGMRC WHPTEPEWTF FISGEARITV FASSSNAQTS DFQAGDIAYI PPSFGHYIEN TGNSTLKFLE VFKSGIFQDI SLSQWLALIP HELVKAHLRV DDATIAKFSR TKQEVVGPTS SGSTSA //