ID   A0A1I8A1S5_9BILA        Unreviewed;       444 AA.
AC   A0A1I8A1S5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g31818.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g31818.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- FUNCTION: Metalloprotease. {ECO:0000256|ARBA:ARBA00002657}.
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:PRU01005}.
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DR   AlphaFoldDB; A0A1I8A1S5; -.
DR   WBParaSite; L893_g31818.t1; L893_g31818.t1; L893_g31818.
DR   Proteomes; UP000095287; Unplaced.
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   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 1.10.10.1940; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF802; ZINC METALLOPROTEINASE NAS-10; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF01549; ShK; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00254; ShKT; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
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   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   DOMAIN          192..408
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          407..443
FT                   /note="ShKT"
FT                   /evidence="ECO:0000259|PROSITE:PS51670"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   444 AA;  49978 MW;  5C924E40FEDB815A CRC64;
     MRFCARNPDH PRCQGHPEFQ QQGGAPPPPP PKIGIPIVDE MFPDLTHFQL PPIPNINIPD
     VLAGVPDILK NFVPETILGE LNEIARRAIL STCQLTKTCT QQKREWLNQR ANIAEQEAAV
     RKLLSPGKPQ SQTDQEIELR LARTHQVKQA LLKEAGLSGQ VEASNDGTFQ HDMLLTEAQA
     NSLLNQIGKS RRRTKRSSLF LEMTPTQTWP ANKPIPYTFD QSMTSTDQQT VHNAVQEIQS
     KTCLRFAYTP TKPSTAHLYY VKAPSPTYCG LSYIGKVEPA NPIYLSFMCG TDWGVAIHET
     LHAVGLNHEQ LRGDRDQFLT INWENINPQN YDFFAIADSK QFTSYGVPYD YGSIMHYNAY
     IASQYPSKPS MTPKINPQVN TKLMGQRNGL SQRDIEIITK MYCMPGCVDN NVYCGAWALR
     DLCNTPAQKG WMLQNCKKSC GFCK
//