ID A0A0D9X559_9ORYZ Unreviewed; 405 AA.
AC A0A0D9X559;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cupin type-1 domain-containing protein {ECO:0000259|SMART:SM00835};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR08G04990.2, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR08G04990.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR08G04990.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR08G04990.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Plays a role in broad-spectrum disease resistance. Probably
CC has no oxalate oxidase activity even if the active site is conserved.
CC {ECO:0000256|ARBA:ARBA00037125}.
CC -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC {ECO:0000256|ARBA:ARBA00011268}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000256|ARBA:ARBA00004271}.
CC -!- SIMILARITY: Belongs to the germin family.
CC {ECO:0000256|ARBA:ARBA00007456}.
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DR AlphaFoldDB; A0A0D9X559; -.
DR STRING; 77586.A0A0D9X559; -.
DR EnsemblPlants; LPERR08G04990.2; LPERR08G04990.2; LPERR08G04990.
DR Gramene; LPERR08G04990.2; LPERR08G04990.2; LPERR08G04990.
DR eggNOG; ENOG502QQ4A; Eukaryota.
DR HOGENOM; CLU_015790_4_1_1; -.
DR Proteomes; UP000032180; Chromosome 8.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR CDD; cd02241; cupin_OxOx; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR001929; Germin.
DR InterPro; IPR019780; Germin_Mn-BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR31238:SF102; GERMIN-LIKE PROTEIN 8-7; 1.
DR PANTHER; PTHR31238; GERMIN-LIKE PROTEIN SUBFAMILY 3 MEMBER 3; 1.
DR Pfam; PF00190; Cupin_1; 3.
DR PRINTS; PR00325; GERMIN.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; RmlC-like cupins; 2.
DR PROSITE; PS00725; GERMIN; 2.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601929-3};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR601929-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601929-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 33..170
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT DOMAIN 239..393
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT BINDING 285
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 290
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 295
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT DISULFID 209..224
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
SQ SEQUENCE 405 AA; 43998 MW; 092537FEB61B00C7 CRC64;
MEHNSVRYKN MRVNGFPCLN PMDVNADHFF KAAMLDKPKN TKDSKFGSNV TLINVMQLPG
LNTLGISIAR IDYAPLGENP PHTHPRATEI FTVLEGTLYV GFVTSNQNNM NKLFSKVLNK
GDVFPAVAVA ALSSQNPGAI TIANAVFGSK PPISDDVLAK AFQVEKGTID WLQAQNIMAS
SSFLLLATLL ALASWQGMAS DPSPLQDFCV ADMHSPVRVN GFPCLNPMDV NADHFFKAAM
LDTPKNTKDS KVGSNVTLIN VMQLPGLNTL GISIARIDYA PLGENPPHTH PRATEILTVL
EGTLYVGFVT SNQNNMNKLF SKVLNKGDVF VFPVGLIHFQ FNPNPHQPAV AIAALSSQNP
GVITIANAVF GSTPPISDDV LAKAFQVEKG TIDWLQAQFW ENNHY
//
