ID A0A0D3GX32_9ORYZ Unreviewed; 225 AA.
AC A0A0D3GX32;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART08G05190.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART08G05190.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART08G05190.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART08G05190.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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, ECO:0000256|RuleBase:RU366015}.
CC -!- SIMILARITY: Belongs to the germin family.
CC {ECO:0000256|ARBA:ARBA00007456, ECO:0000256|RuleBase:RU366015}.
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DR AlphaFoldDB; A0A0D3GX32; -.
DR SMR; A0A0D3GX32; -.
DR STRING; 65489.A0A0D3GX32; -.
DR PaxDb; 65489-OBART08G05190-1; -.
DR EnsemblPlants; OBART08G05190.1; OBART08G05190.1; OBART08G05190.
DR Gramene; OBART08G05190.1; OBART08G05190.1; OBART08G05190.
DR eggNOG; ENOG502QQ4A; Eukaryota.
DR HOGENOM; CLU_015790_0_0_1; -.
DR Proteomes; UP000026960; Chromosome 8.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd02241; cupin_OxOx; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
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; 1.
DR PRINTS; PR00325; GERMIN.
DR SMART; SM00835; Cupin_1; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
DR PROSITE; PS00725; GERMIN; 1.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU366015};
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:UP000026960};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366015};
KW Signal {ECO:0000256|RuleBase:RU366015}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU366015"
FT CHAIN 24..225
FT /note="Germin-like protein"
FT /evidence="ECO:0000256|RuleBase:RU366015"
FT /id="PRO_5019620574"
FT DOMAIN 63..213
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT BINDING 107
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 112
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 112
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 117
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 158
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT DISULFID 33..48
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
SQ SEQUENCE 225 AA; 24379 MW; 704DC6C211518AD4 CRC64;
MASPSSFCLL AVLLALVSWQ AIASDPSPLQ DFCVADKHSP VLVNGFACLD PKYVNADHFF
KAAMLDTPRK TNKVGSNVTL INVMQIPGLN TLGISIARID YAPLGENPPH THPRATEILT
VLEGTLYVGF VTSNPNNTLF SKVLNKGDVF VFPEGLIHFQ FNPNPHQPAV ALAALSSQNP
GAITIANAVF GSKPPISDDI LAKAFQVEKG TIDWLQAQFW ENNHY
//
