GenomeNet

Database: UniProt
Entry: A0A059DBF4_EUCGR
LinkDB: A0A059DBF4_EUCGR
Original site: A0A059DBF4_EUCGR 
ID   A0A059DBF4_EUCGR        Unreviewed;       863 AA.
AC   A0A059DBF4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN   ORFNames=EUGRSUZ_A00488 {ECO:0000313|EMBL:KCW88068.1};
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:KCW88068.1};
RN   [1] {ECO:0000313|EMBL:KCW88068.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW88068.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK198753; KCW88068.1; -; Genomic_DNA.
DR   RefSeq; XP_010026317.1; XM_010028015.2.
DR   AlphaFoldDB; A0A059DBF4; -.
DR   STRING; 71139.A0A059DBF4; -.
DR   MEROPS; M08.A01; -.
DR   EnsemblPlants; KCW88068; KCW88068; EUGRSUZ_A00488.
DR   GeneID; 104416623; -.
DR   Gramene; KCW88068; KCW88068; EUGRSUZ_A00488.
DR   KEGG; egr:104416623; -.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG2556; Eukaryota.
DR   InParanoid; A0A059DBF4; -.
DR   OMA; GICEFRC; -.
DR   OrthoDB; 24037at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0008233; F:peptidase activity; IBA:GO_Central.
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   863 AA;  94841 MW;  F8AE4A92374580A7 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
     ISIQKCDKDG DNRLRVCHSA CQSYNRACGA SLDCSDLTLF SGETEHGSQC TGSDETAHIK
     GLAMQGRSSK ALEALKQMFV LYR
//
DBGET integrated database retrieval system