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Database: UniProt
Entry: A0A1I8AEU3_9BILA
LinkDB: A0A1I8AEU3_9BILA
Original site: A0A1I8AEU3_9BILA 
ID   A0A1I8AEU3_9BILA        Unreviewed;       587 AA.
AC   A0A1I8AEU3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Zinc metalloproteinase {ECO:0000256|PIRNR:PIRNR036365};
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_g473.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g473.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|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361183};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|PIRNR:PIRNR036365}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   AlphaFoldDB; A0A1I8AEU3; -.
DR   WBParaSite; L893_g473.t1; L893_g473.t1; L893_g473.
DR   Proteomes; UP000095287; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
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); 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR017050; Metallopeptidase_nem.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF892; ZINC METALLOPROTEINASE NAS-29; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361183};
KW   Protease {ECO:0000256|RuleBase:RU361183};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036365};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR036365};
KW   Zinc {ECO:0000256|RuleBase:RU361183};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT                   ECO:0000256|RuleBase:RU361183"
FT   CHAIN           23..587
FT                   /note="Zinc metalloproteinase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT                   ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5009030017"
FT   DOMAIN          188..393
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          440..548
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   REGION          24..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  64580 MW;  9BF7F9039FEE9E55 CRC64;
     MFHCVFTSSF LLLCHLAELG QAGNEQSAPA VPPGQEKLSG SEGLTRGQQN KLAEIVNGDP
     KGADNKPLKG KELMKKTGGK LFSTNGKEED LNEVASIIAA NIANVEAKLK KEYDDSYAKN
     KGLIDKARND ATKLNAKPLM DNHEELDIAH INAAHGMEQV LVHGDVSMPV EGLKKLFGVD
     GASRTKRQAY YDSLYPSTIW KTGVYWNFDA ALNQAARSAV LSAIAFWQQN TCIRFYQADP
     ATSVNRPVIV FYAGSGCFSP VGRSTSSSIQ YVSIGTGCES VNLWKVFPVM KESLGLWHAQ
     SRFDRSSFVT VDFTNIMAGM AHNYDAQTSS TNNNYGLTYD YRSVMHYRPG DFAANTSKPV
     MYSLNSAYQM SIGYQQLPSF TDIAVLNKHY SCYDKCNANA TVCYYGGFPN PNSCTVCQCP
     SGFGGNDCSQ RQPPSTGLTC GTILTSTTAW QYLTVNNTVG TGQYVIGNVT SPLHCTYHIT
     APTGYRIQYA VVTVGFDANP NALCYDSCYY GGLSVKGLDP SWRPEGMRFC CSSQYNQVLT
     TASNRLVLQP WNLYHYTDFK FDQFDGGGME RNVDYTLLVY LLSNKLM
//
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