ID A0A0D3FNN5_9ORYZ Unreviewed; 936 AA.
AC A0A0D3FNN5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
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:OBART03G33000.2};
RN [1] {ECO:0000313|EnsemblPlants:OBART03G33000.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART03G33000.2};
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:OBART03G33000.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0D3FNN5; -.
DR STRING; 65489.A0A0D3FNN5; -.
DR MEROPS; M08.A01; -.
DR PaxDb; 65489-OBART03G33000-2; -.
DR EnsemblPlants; OBART03G33000.2; OBART03G33000.2; OBART03G33000.
DR Gramene; OBART03G33000.2; OBART03G33000.2; OBART03G33000.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2556; Eukaryota.
DR HOGENOM; CLU_016637_0_0_1; -.
DR Proteomes; UP000026960; Chromosome 3.
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; 2.30.34.10; 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 SMART; SM00181; EGF; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..936
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002262370"
FT DOMAIN 723..755
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 404
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT DISULFID 727..737
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 745..754
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 936 AA; 101996 MW; 50B45C863D44D9EF CRC64;
MALPLVVLVA FTTKSTTSTP PPPHLTSSTS PRLRLLHPLS LLLAGVRWCG GGQPGGPRLG
GGAARRKEEG WWIRRGGGEV EEDGCGRGVA RGAVNGSGEG GWGCGRPYME DRASPGGGVC
GRVLRLASVQ IILILFLTQG ACSSSRDGKT SPPQGLDAGE KDIYLSHSCI HDEILHQRRR
AGRKEYSVMP QVYHERRENM ERLRGRHLLG VSSWHASQKN VKKPIRIYLN YDAVGHSPDR
DCKTVGDIVK LGEPPVPSIP GTPVCDPHGD PPLVGDCWYN CTVEDIAGED KKQRLRKALG
QTVEWFRKAL AVEPVKGNLR LSGYSACGQD GGVQLPHAYI EDGVANADLV LLVTTRPTTG
NTLAWAVACE RDQWGRAIAG HVNVAPRHLT AEAETLLSAT LIHEVMHVLG FDPHAFTHFR
DERKRRRSQV TSQILDEKLG RMVTRVVLPR VVMHSRHHYG AFSQNFTGLE LEDGGGRGTS
GSHWEKRLLM NEIMTGSVDT RSVVSKMTLA LLEDSGWYQA NYSMAEHLDW GRNQGTEFVI
SPCNLWKGAY RCNTTQLSGC TYNREAEGYC PIVSYSGDLP KWAQYFPQAN KDGSCTDVNS
ARAPDRMLGE VRGSNSRCMA STLVRTGFVR GSMTQGNGCY QHRCTNNSLE VAVDGIWKSC
PQTGGPVQFP GFNGELICPA YHELCNTVPV PVSGQCPKSC SFNGDCIDGT CHCFPGFHGH
DCSRRSCPAK CTGHGICKAN GICECESGWT GIDCSTAVCD EQCSLHGGVC DNGKCEFRCS
DYAGYTCQKG SAILPSLSMC HDVLVRDADG QHCAPSELSI LQQLEAVVLV PNYNRLMPSG
RTFLNFFNNA NCAAAAKRLA CWISIQRCDE DGDNRLRVCY SACELYNTAC GAGLDCSDQT
LFSKREEEEK GVPCTGYGEK KSFWLMTITS PGVSSL
//
