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Database: UniProt
Entry: A0A1V8SCE2_9PEZI
LinkDB: A0A1V8SCE2_9PEZI
Original site: A0A1V8SCE2_9PEZI 
ID   A0A1V8SCE2_9PEZI        Unreviewed;       500 AA.
AC   A0A1V8SCE2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Cupin type-1 domain-containing protein {ECO:0000259|SMART:SM00835};
GN   ORFNames=B0A48_17163 {ECO:0000313|EMBL:OQN96739.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN96739.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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   -!- 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:OQN96739.1}.
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DR   EMBL; NAJO01000062; OQN96739.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8SCE2; -.
DR   STRING; 1507870.A0A1V8SCE2; -.
DR   InParanoid; A0A1V8SCE2; -.
DR   OrthoDB; 2358302at2759; -.
DR   Proteomes; UP000192596; 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   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 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:UP000192596};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..500
FT                   /note="Cupin type-1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012822443"
FT   DOMAIN          152..294
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   DOMAIN          333..474
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   REGION          25..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        438
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT   BINDING         197
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         242
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         378
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         380
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         385
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         424
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ   SEQUENCE   500 AA;  53617 MW;  09A090C35BEB8313 CRC64;
     MFYRLLATQV LFAVTLATPI AIERRQSASA SDSPAATVVP TATAVGPPGA SGYLRGSTDL
     GGFSSSNPVD TTADASVVSP DQYELAPGQD ADKDLGLFLD LSTVENPQPI RGSTDAPTDP
     GPRNIALDRE NSDAFAPPGT DAGTVPNGKW PLGLSANRHG LGSAGWARQQ NIDALPIATA
     MAGVDMRLSP NAYREMHWHK ANEWSLILNG SVRLNSMNEA GETFVDDLQA GDVWFFPAGI
     PHSIQASEAG VEFLLVFDSG DFSEDGTNLL SETFERNSKA VLAKDLRVDT SAFDKIPDGE
     LYIFDGTPFP KNISTDNITG PAGVIPQSST YSYHLSQQAA YEVPGGSVKI IDPVSFPIAS
     NFAAGLFVIK PGAMRELHWH TTSDEWNYII SGQGRLTVYS APASSRTFDF QAGDVGYVPV
     PASHYLENTG TEDLVYLEVL QAPAYNDISV AQWLGLTPKR VVKDHLGFSD DTLNRLPKIK
     PYILPGNTNL TQTNFTSESE
//
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