ID   A0A059DC70_EUCGR        Unreviewed;       785 AA.
AC   A0A059DC70;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN   ORFNames=EUGRSUZ_A00488 {ECO:0000313|EMBL:KCW88069.1};
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:KCW88069.1};
RN   [1] {ECO:0000313|EMBL:KCW88069.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW88069.1};
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601577-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601577-2};
CC   -!- SIMILARITY: Belongs to the peptidase M8 family.
CC       {ECO:0000256|ARBA:ARBA00005860}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KK198753; KCW88069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059DC70; -.
DR   MEROPS; M08.A01; -.
DR   EnsemblPlants; KCW88069; KCW88069; EUGRSUZ_A00488.
DR   Gramene; KCW88069; KCW88069; EUGRSUZ_A00488.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.10.170.20; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.90.132.10; Leishmanolysin , domain 2; 1.
DR   Gene3D; 2.10.55.10; Leishmanolysin domain 3; 1.
DR   Gene3D; 2.30.34.10; Leishmanolysin domain 4; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR001577; Peptidase_M8.
DR   PANTHER; PTHR10942; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR   PANTHER; PTHR10942:SF0; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01457; Peptidase_M8; 1.
DR   PRINTS; PR00782; LSHMANOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601577-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|PIRSR:PIRSR601577-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2}.
FT   DOMAIN          638..670
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT   BINDING         380
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT   DISULFID        642..652
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        660..669
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   785 AA;  86316 MW;  28AF0BE6E36244EF CRC64;
     MEVTVRRRSS LAVPWLVADL RFAIVLVEIV LFLLCSEAVN ASIAEKPHQW HDPGEGSEKI
     VSHSCIHDQI LEQRRRPGHK VYLVTPQVYQ ESGVSKPLHR KGRGLLGLST SPFHQKDAKQ
     PIRIYLNYDA VGHSPDRDCR NVGDIVKLGE PPANSLPGGP SCNAHGEPPV FSDCLYNCTQ
     DDIAGDDKQR RLRKALGQTV DWFSRALAVE PVKGNLRLSG YSACGQDGGV QLPRDYVEGG
     VANSDLVLLV TTRPTTGNTL AWAVACERDQ WGRAIAGHVN VAPRHLTAEA ETLLSATLIH
     EVMHVLGFDP HAFAHFRDER MRRRSRVTEQ AMDEKLGRMV TRVVLPRVLM HSRFHYGAFS
     ENFTGLELED GGGRGTSGSH WEKRLLMNEI MTGSVDTRSV VSKMTLALLE DSGWYKANYS
     MADRLDWGRN QGTDFVTSPC NQWKGAYHCN TTQFSGCTYN REAEGYCPIV SYSGDLPQWA
     RYFPQANKGG QSSLADYCTY FVAYSDGSCT DTNSTRPPDK ILGEVRGSNS RCMASSLVRT
     GFLRGSMSQG NGCYRHRCVN NSLEVAVDGI WKVCPEAGGP VQFPGFNGEL ICPAYHELCS
     TGLPPLSGGH CPNSCNFNGD CIDGRCDCFL GFHGHDCSKR SCPGNCNGHG KCLRSGVCQC
     DDRYTGIDCS TEVCDEQCSL HGGVCDNGKC EFRCSDYAGY TCQNSSKLLS TLSVCQDVLE
     IGKSGQHCAP SEPSVLQQLE EVVVMPNYHR LFPGGARKLI NNLFNKQYDC DAAAKKLACW
     VSMAL
//