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Database: UniProt
Entry: A0A0N5A6Q6_PARTI
LinkDB: A0A0N5A6Q6_PARTI
Original site: A0A0N5A6Q6_PARTI 
ID   A0A0N5A6Q6_PARTI        Unreviewed;       419 AA.
AC   A0A0N5A6Q6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
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_0001767700.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001767700.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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   AlphaFoldDB; A0A0N5A6Q6; -.
DR   WBParaSite; PTRK_0001767700.1; PTRK_0001767700.1; PTRK_0001767700.
DR   Proteomes; UP000038045; 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   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
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:SF802; ZINC METALLOPROTEINASE NAS-10; 1.
DR   Pfam; PF01400; Astacin; 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.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01211};
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..16
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           17..419
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5005733328"
FT   DOMAIN          30..225
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        69..224
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   419 AA;  48980 MW;  2CB6ADE92C55DE01 CRC64;
     MNYILYIFIF VKLTQLHIFQ ESDYKSVFKK AILKNGYINW TFPIYYYIDK GVYRSKILSV
     IRYLEKSTCL RFEETQSKKG NMIKYMTSET QCNSLVGKLS RDKEHEIKLT NGCSRNYGDT
     AHETLHALGL SHEHARKDRD KYITILKGNI DDNLYRNFLK DHDGFTFFDI HYDYSSIMQY
     PKGAFSKNDR NTMEAKNVEP YNEMMGQSDM ITFNDIKHLN YYYCKCHYFN GQCKNGGYVK
     EPLCGHCICP KEFTGDKCER IADRSENCNL KVYNVTETEN LFKGSGNKRC IYHFKTDKDS
     RIFLNLTYVQ TRYRSPCISD VGLEIKYLDD KGTTGLCLCG VYKNILLYSQ GNEVVITYTG
     LESNSQGNEV VITYTGLESS NWFYGYYKKV LKSIKKEDEI CYKGKCFIEQ DKKITGNTR
//
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