ID A0A1U7VDJ9_NICSY Unreviewed; 839 AA.
AC A0A1U7VDJ9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein LOC104212740 {ECO:0000313|RefSeq:XP_009760389.1};
GN Name=LOC104212740 {ECO:0000313|RefSeq:XP_009760389.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009760389.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009760389.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009760389.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_009760389.1; XM_009762087.1.
DR AlphaFoldDB; A0A1U7VDJ9; -.
DR SMR; A0A1U7VDJ9; -.
DR STRING; 4096.A0A1U7VDJ9; -.
DR GeneID; 104212740; -.
DR KEGG; nsy:104212740; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2556; Eukaryota.
DR OrthoDB; 24037at2759; -.
DR Proteomes; UP000189701; Unplaced.
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; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
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; IPR001577; Peptidase_M8.
DR PANTHER; PTHR10942; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR PANTHER; PTHR10942:SF0; LEISHMANOLYSIN-LIKE PEPTIDASE; 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:UP000189701};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2}.
FT DOMAIN 639..671
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT DISULFID 643..653
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 661..670
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 839 AA; 92373 MW; 39CADFF39F80EAB1 CRC64;
MELKIWCCRS SISRSTLSVH SKSSSSAKLR FAIFFPQVLL LLVCLKTSLA TLPDHELLRQ
EDKSTISHSC IHDQIIEQRK RPGLQVYSVT PQVYEESVVS NPPHHRGRAL LEIPKEQNDV
MQPIRIFLNY DAVGHSSERD CQKVGDIVKL GEPPGASFSG TSSCNPHGDP PVYGDCWYNC
TLDDIAGEDK RHRLRKALEQ TADWFRRALA VEPVRGNLRL SGYSACGQDG GVQLPRKYVE
EGVANADLVL LVTTRPTTGN TLAWAVACER DQWGRAVAGH VNVAPRHLTA EAETLLQATL
IHEVMHVLGF DPHAFSHFRD ERKRRRSQVT EQAMDEKLGR MVTRVVLPRV IMHARYHYGA
FSENFTGLEL EDGGGRGTSG SHWEKRLLMN EIMTGSVDTR SVVSKMTLAL LEDSGWYRAN
YSMADRLDWG RNQGSEFVTS PCNHWNGAYH CNTTQLSGCT YNREAEGYCP LVNYSGDLPQ
WARYFPQANR GGQSSLADYC TYFVAYSDGS CTDTNGARAP DRMLGEVRGS SSRCMASSLV
RTGFVRGSMT QGNGCYQHRC SNNSLEVAVD GIWKVCPKAG GPIQFPAFNG ELICPAYHEL
CDVDPVSLSS HCPNSCNFNG DCLGGKCQCF IGFGGHDCSK RSCPGNCSGH GKCLGSGVCE
CQNGYTGIDC STAVCDEQCS LHGGVCDNGV CEFRCSDYAG YTCQNSSMLL PSLSVCKDVL
QNDVSGQHCA PSELSILQQL EEVVVMPNYN RLFPAGPRKI LNIFRGRDCD GAAKRLACWI
SIQKCDNDGD NRLRVCHSAC QSYNVACGAS LDCSDQTLFS SEREGKGLCT GWGELDAWF
//
