ID A0A059C8G2_EUCGR Unreviewed; 526 AA.
AC A0A059C8G2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
GN ORFNames=EUGRSUZ_E03224 {ECO:0000313|EMBL:KCW74509.1};
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:KCW74509.1};
RN [1] {ECO:0000313|EMBL:KCW74509.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW74509.1};
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 -!- FUNCTION: May be involved in modulation of pathogen defense and leaf
CC cell death. {ECO:0000256|RuleBase:RU280816}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU280816}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU280816}.
CC -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC binds calmodulin in a calcium-dependent fashion.
CC {ECO:0000256|RuleBase:RU280816}.
CC -!- SIMILARITY: Belongs to the MLO family. {ECO:0000256|ARBA:ARBA00006574,
CC ECO:0000256|RuleBase:RU280816}.
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DR EMBL; KK198757; KCW74509.1; -; Genomic_DNA.
DR RefSeq; XP_010057357.1; XM_010059055.2.
DR AlphaFoldDB; A0A059C8G2; -.
DR EnsemblPlants; KCW74509; KCW74509; EUGRSUZ_E03224.
DR GeneID; 104445233; -.
DR Gramene; KCW74509; KCW74509; EUGRSUZ_E03224.
DR KEGG; egr:104445233; -.
DR eggNOG; ENOG502QQFC; Eukaryota.
DR InParanoid; A0A059C8G2; -.
DR OMA; SWWIWIF; -.
DR OrthoDB; 368831at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR InterPro; IPR004326; Mlo.
DR PANTHER; PTHR31942:SF72; MLO-LIKE PROTEIN; 1.
DR PANTHER; PTHR31942; MLO-LIKE PROTEIN 1; 1.
DR Pfam; PF03094; Mlo; 2.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|RuleBase:RU280816};
KW Membrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Pathogenesis-related protein {ECO:0000256|ARBA:ARBA00023265,
KW ECO:0000256|RuleBase:RU280816};
KW Plant defense {ECO:0000256|RuleBase:RU280816};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 526 AA; 60535 MW; 69AA04842245519E CRC64;
MSETSAESVE ELTLESTPTW AVATVCFVLI LVSVFLEHLI HLLAQYLQNK KKRSLIQALD
KIKSELMLLG FISLLLTVTE RWIANICIPK SVAETFLPCS TWESSEEEEE TKCLEQGKVS
LLSREGVRQL QYLIFVLAFF HSLSCMLTFA LGMAKMRKWE SWEAETRTLD YQFSNDPRRF
KLVHQTSFAR RHLTCWSDLR ILRWPGCFLR QFYNSVSKVD YMTLRHGFIM AHLSEGSTFD
FQKYIERALE KDFGVVVGIS FWIWIFLVIF IFFHAHVFYN YLWLPFIPLV MLLLVGTKLQ
GIITKMCIDS NDKSNVVRGT LLVRPSDHFF WFGRPKLLLH LMHFILFQNS FQVAFFTWTW
YKFGFRSCFH ERTEDIIIEF TMGALVQFLC GYVTLPLYAL VTQMGTSMSG AVFTENVREG
LKRWRATARK NLAPRDPYAA CLSLEASVTS LDASVTSLDA SVTSHDAYSP SFGHDAAFSI
DLDHPDLESS ISLDTVDGEN NSHLKTVEDR RKKGSFDGFV ISSTTR
//