ID A0A0K0EBK6_STRER Unreviewed; 466 AA.
AC A0A0K0EBK6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000687810.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000687810.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
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; A0A0K0EBK6; -.
DR WBParaSite; SSTP_0000687810.1; SSTP_0000687810.1; SSTP_0000687810.
DR Proteomes; UP000035681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10127:SF780; ASTACIN-LIKE METALLOENDOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..274
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 269..309
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 118..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 273..283
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 299..308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 466 AA; 54711 MW; 4ABFB6675AA3FDB3 CRC64;
MKYIKFNILI YLYFTIIYCV KLINYEKNHD NFFNNNKKLK RSIPYQNNQK NFYNNVANNL
KKTSSVNNFN IEQNYRKKRM IASCFYGKWT FPIPYYVDAN VNQKMVDLAL LIIEKKTCVR
FTKHKTMTPG LTGLRYYYGS SCKSRVGKPY ENVWQNVSIG KNCDTIETIQ HETMHSLGFF
HVHSRIDRDQ YIYFRKKNIE KRFLSNLEKV CFLDSKTLGV PFDFSSVMMY DSAAYSKNGK
NTIYPRDKNY VKTVSASTKV TFTDVKLINL LYCQNICKEK IKCMNGGYQN PNNCSFCICV
KGFTGRWCQF LPSSTRECGE SVLIAKNKIA SLKSKGEKKC IYHIFCEKKK LLAIFIVKSI
FFLRDYYKCF RNNSLEIKYW KDKTPSGALF CGLDKNILII SESNHAMISY RSISTQNSFH
IFFKSVPTIY NQLNLKIEFK EEVEKYKRLK ASRGTSTSDD SDNIYY
//
