ID   A0A0N5A6K3_PARTI        Unreviewed;       964 AA.
AC   A0A0N5A6K3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Peptidase M12B domain-containing protein {ECO:0000313|WBParaSite:PTRK_0001762700.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001762700.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001762700.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   AlphaFoldDB; A0A0N5A6K3; -.
DR   STRING; 131310.A0A0N5A6K3; -.
DR   WBParaSite; PTRK_0001762700.1; PTRK_0001762700.1; PTRK_0001762700.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1620.60; -; 2.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR   InterPro; IPR041645; ADAMTS_CR_2.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   PANTHER; PTHR13723:SF291; PEPTIDASE M12B DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF13688; Reprolysin_5; 1.
DR   Pfam; PF00090; TSP_1; 2.
DR   SMART; SM00209; TSP1; 3.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50092; TSP1; 3.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..964
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005892748"
FT   DOMAIN          322..526
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   ACT_SITE        479
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         478
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         482
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         488
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   964 AA;  109384 MW;  657F6E1762253236 CRC64;
     MMLRLILFSI FLSIFFIKKV NPINCYECTS GKGQDCRASA STCSYGLFGC AKITAYSGGV
     DKYGMFSNND RSIISEIRAC NVLPIGGVDA CQQQTLLGMR IVTCYCFNDY CNDANKFVTP
     IYNELSDKEK FHLFGKNGLK GKPIYDEVII NEFDGKRFDI ILEGKEIIFI LEDASLMLFD
     IGLHHNYNND SKDSLNEHIY YDMCNKVYKG KSINPKGNVI SLTGCRNNLR GLIITDDGEM
     HFIHPVPKRI KDGIHVIHKR SIEEALSPDN HDCIFNKKND PYPEDQIESD TLISHLRKIK
     TNPFIERIKR DSVINVNDDT EVIIEIAIFA DNLMIKHFYD IYGEEFHMKE LKRFVIATVN
     NVDSLYRHQT LNSKLHFRIK RIDVMEGQPP ELQSNRHDNG EVNKLLKSFC EYQQEKKPSN
     RNDPRYWDHA LLFTGFDIYG GAIKNIAGFA PVKGMCSEVR SCTINEGVDF GSVFVVTHEI
     GHNLGMYHDG QNECHTDCCI MAPSIGSGKT KWSTCSSTEM KIFVNKLGTE PTRPPNCLKT
     AAAKSKSIGV LPGQDYTVNE QCRLFHGKCW THGLRAHQTL EDICQMIWCT DGDEKFRTSH
     PALEGTYCGK DRVCFSGKCV PAKRDLIQVD GGWSKWTENS YCNPIDNGRC NECVMDGQLK
     LKKEYRYCEN PFPNNGGRYC TGENMRGIAC DVNSRCLVGK SIQKYIDSVC TEKAKLPKNI
     EIKMDKKGLH FEHDYCKVWC YIKESTSIRT VDDMPDGTSC GDNKYCLKGV CRLLTCNGTV
     LGGEANDCSK SGFKKEENKI QIISEWDNWQ PWSKCSSKNC TEIGSKIRKR ICKGSNCLGA
     NIEKTACKIE CSVVENQYSE WSEWLECSTS KCGEEGKQMR TRKCLSKICT GPEIESQSCK
     VVCIQNIGKL TEWSSWSKCN INIDCKIPSE RKRTRDCWSL LAPNPICEGK KEEVELCPRP
     NCKE
//