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
//