ID A0A058ZR22_EUCGR Unreviewed; 218 AA.
AC A0A058ZR22;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_L02342 {ECO:0000313|EMBL:KCW44232.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW44232.1};
RN [1] {ECO:0000313|EMBL:KCW44232.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW44232.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK199562; KCW44232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A058ZR22; -.
DR EnsemblPlants; KCW44232; KCW44232; EUGRSUZ_L02342.
DR Gramene; KCW44232; KCW44232; EUGRSUZ_L02342.
DR eggNOG; ENOG502QQ4A; Eukaryota.
DR InParanoid; A0A058ZR22; -.
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:SF300; GERMIN-LIKE PROTEIN SUBFAMILY 1 MEMBER 13-RELATED; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU366015};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601929-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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 Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366015};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366015}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366015"
FT CHAIN 21..218
FT /note="Germin-like protein"
FT /evidence="ECO:0000256|RuleBase:RU366015"
FT /id="PRO_5019611316"
FT DOMAIN 61..212
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT BINDING 106
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 111
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT BINDING 116
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT BINDING 116
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 30..47
FT /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
FT NON_TER 218
FT /evidence="ECO:0000313|EMBL:KCW44232.1"
SQ SEQUENCE 218 AA; 23655 MW; 95CE27615997528D CRC64;
MMKFLLTFVL LALASCHAFA SDPSPLQDFC VAVNDPNSAV FVNGKFCKDP KLVIADDFSF
TKFRYPGSTS NPLGSKVTTA FVDQFPGLNT LGIATARLDF APYGLNPPHI HPRGTEMLLV
VEGTLHVGFV TSNQLNNTLF TKVLTKGDVF VFPQGLIHFQ LNIGQTNALA FAFLSSQNPG
LITIANTVFG SKPPINVDVL TKAFQVDNKL INYLQAQS
//
