ID A0A0B0ML75_GOSAR Unreviewed; 853 AA.
AC A0A0B0ML75;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KHF99680.1};
GN ORFNames=F383_08640 {ECO:0000313|EMBL:KHF99680.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHF99680.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHF99680.1}.
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; JRRC01089915; KHF99680.1; -; Genomic_DNA.
DR RefSeq; XP_017607368.1; XM_017751879.1.
DR AlphaFoldDB; A0A0B0ML75; -.
DR SMR; A0A0B0ML75; -.
DR MEROPS; M08.A01; -.
DR GeneID; 108453648; -.
DR KEGG; gab:108453648; -.
DR OrthoDB; 24037at2759; -.
DR Proteomes; UP000032142; Unassembled WGS sequence.
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 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:UP000032142};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2}.
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT DISULFID 631..641
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 649..658
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 853 AA; 94212 MW; 4F5F0B779CD8E0A6 CRC64;
MVTRFDFKLR FAVVIFEVLL ILLWFGAATS KFQRPHPQWE GPERGLGENI VSHSCIHDQI
IEQRRRPGRK VYSVTPQFYV HSSTSNSVLH KGRSLLEISE VLEHPKEAKQ PIRIYLNYDA
VGLSPDRDCR KVGDIVKLGE PPVSSSPGTR SCNPHGDPPI YGDCWYNCTL NDLSGQDKRH
RLHKALGQTA DWFKRALAVE SVKGNLRLSG YSACGQDGGV QLPRQYVEEG VADADLVLLV
TTRPTTGSTL AWAVACERDQ WGRAIAGHVN VAPRHLTAEA ETLLSATLIH EVMHVLGFDP
HAFMHFRDER KRRRSKVTEH IIDERLGRMV TRVVLPRVVM HSRHHYGAFS ENFTGLELED
GGGRGTSGSH WEKRLLMNEI MTGSVDTKSV VSKMTLALLE DSGWYQANYS MADHLDWGHN
QGTDFLTSPC NLWKGAYHCN TTNLSGCTYN REAEGYCPIV SYNTDLPQWT RYFPQANKGG
QSSLADYCTF FVAYSDGSCT DSNSARAPDR MLGEVRGSNS RCMASSLVRT GFVRGSMTQG
NGCYQHRCVN NSLEVAVDGI WKVCAKVGGP VQFPGFNGEL ICPAYHELCS AGPVPVSGQC
PNSCNFNGDC VSGKCRCFPG FHGHDCSKRY CPSNCNGHGT CLSNGVCGCE NGYTGIDCST
AVCDEQCSLH GGVCDNGVCE FRCSDYAGYT CQNSSTLLSS LSVCKNKLER VLSGQHCAPS
EASVLQQLEE VVIMPNYHRL FPSVAQKLFT NLFGTSYCES AAKRLACWIS IQKCDSDGDN
RLRVCHSACQ AYNLACGASL DCSDQTLFSS EEEGEGQCTG SGEMKVSWFN RFRNRLFSSN
SSLEGMYVKY SQL
//
