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Database: UniProt
Entry: A0A1I7ZA97_9BILA
LinkDB: A0A1I7ZA97_9BILA
Original site: A0A1I7ZA97_9BILA 
ID   A0A1I7ZA97_9BILA        Unreviewed;       736 AA.
AC   A0A1I7ZA97;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 25.
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_g24169.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g24169.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) 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:PRU01211}.
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DR   WBParaSite; L893_g24169.t1; L893_g24169.t1; L893_g24169.
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; 3.40.390.10; Collagenase (Catalytic Domain); 3.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF850; ZINC METALLOPROTEINASE NAS-29; 1.
DR   Pfam; PF01400; Astacin; 3.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 3.
DR   PROSITE; PS51864; ASTACIN; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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}; Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           21..736
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5009029991"
FT   DOMAIN          254..388
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          497..716
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   COILED          122..163
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   ACT_SITE        612
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         611
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         615
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         621
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   736 AA;  80187 MW;  FCA9EB37FEA31322 CRC64;
     MWIHSTLVLI ALLFVHPGWA LGYGKPAGGG QAPTLKARHS KKQQEHIDNI VNNLPKGADL
     QPLKGIDLMK QRGAKIFIKN GQDVTNLDQI KALLDANKGA LNQKRGAKIF IKNGQDVXXX
     XAIYQQHKDK IDSLKAEAQA AIYQQHKDKI DSLKAEAQNL NAKPRRDDDG QLSIHDINSA
     VGMTGLLHEG DMAFSTDDLT RRLTGALSGV VSGVTGTLGG ALGGLPLSRR RFQRAAPFRD
     SQYPDTIWTN GRAAPFRDSQ YPDTIWTNGV NWDFNSTLNQ AAQDAITAAI AFWQQTTCIT
     FNRVDAATAD PSMYPIVVFY PGDGCFSPVG RKGSADFQQV SIGNGCETVP IAAHEIAHSL
     GVFHEQSRYD RDDDVFVDLS NVQTDMAYXX XXTDDLTRRL TGALSGVVSG VTGTLGGALG
     GLPLSRRRFQ RAAPFRDSQY PATIWTNGVN WDFNSTLNQA AQDAITAAIA FWQQTTCITF
     NRVDAATADP SLYPIVVFYP GDGCFSPVGR KXXXXLSGVV SGVTGTLDQA AQDAITAAIA
     FWQQTTCITF NRVDAANADP SIAATADPSL YPIVVFYPGD GCFSPVGRKG SADFQQVSIG
     NGCETVPIAA HEIAHSLGVF HEQSRYDRDD NVFVDLSNVQ TDMAYNYNKE STATNYNYDI
     PYDYRSVMHY GPEDFAIDST KPVMFATNPA YQQSIGSQEL PTFADIAMLN LHYSCYGRPT
     EVGKKLSKEQ HRIATL
//
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