ID A0A1V6TJT3_9EURO Unreviewed; 469 AA.
AC A0A1V6TJT3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cupin type-1 domain-containing protein {ECO:0000259|SMART:SM00835};
GN ORFNames=PENSTE_c005G00575 {ECO:0000313|EMBL:OQE26264.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE26264.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE26264.1}.
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DR EMBL; MLKD01000005; OQE26264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TJT3; -.
DR STRING; 303698.A0A1V6TJT3; -.
DR OrthoDB; 2358302at2759; -.
DR Proteomes; UP000191285; 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 NCBIfam; TIGR03404; bicupin_oxalic; 1.
DR PANTHER; PTHR35848:SF6; CUPIN 2 CONSERVED BARREL 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.
PE 4: Predicted;
KW Manganese {ECO:0000256|PIRSR:PIRSR617774-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR617774-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..469
FT /note="Cupin type-1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012686640"
FT DOMAIN 134..272
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT DOMAIN 311..452
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT REGION 24..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 177
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 181
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 220
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 358
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 363
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 402
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ SEQUENCE 469 AA; 51067 MW; 48AB80952E76936C CRC64;
MKVQTLSHSV SLLFLLLSPS SAIPARRTEE SGSNPGLRGS KSLVGYSPSE KVGSTTTPDI
KYSLLPGQTN DPKIGTWLDF TKVDNPQPIR GDTGGDDPGP RNYVYDKINS DKLAPPGTDH
GQTINAQWPM GLSHNRLGID NAGWARQENS VVMPAATEMA GVDMRLEPAG YRELHWHVAS
EWSLVLNGSC RIQAVNENGE TFVDDLVAGD VWFFPPGVPH SIQALDDGVE FLLVFDDGDF
NEDNTFLATE VFLHSPKEVL AKDLGVPIAA FDDIPDDELY IFKGTPAPKD IEKQNVTTSS
GIVPRSESYS YHFSEQPAHE VAGGSVKIVD PLTFPVAKNF SAAIVTVHPG GMREIHWHPS
SDEWTFFISG QGRATLFTAP DAATTFDYMA GDVGYFPQSN SHYIENTGEE DLVFLEVLQA
TQFTDIALGQ WIASTPKQIV SDTLKLSDST LSKLKTEKQY VVAGSSSSD
//
