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Database: UniProt
Entry: A0A0V1BPP1_TRISP
LinkDB: A0A0V1BPP1_TRISP
Original site: A0A0V1BPP1_TRISP 
ID   A0A0V1BPP1_TRISP        Unreviewed;       384 AA.
AC   A0A0V1BPP1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   Name=nas-5 {ECO:0000313|EMBL:KRY38944.1};
GN   ORFNames=T01_4558 {ECO:0000313|EMBL:KRY38944.1};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY38944.1, ECO:0000313|Proteomes:UP000054776};
RN   [1] {ECO:0000313|EMBL:KRY38944.1, ECO:0000313|Proteomes:UP000054776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS3 {ECO:0000313|EMBL:KRY38944.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY38944.1}.
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DR   EMBL; JYDH01000022; KRY38944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1BPP1; -.
DR   Proteomes; UP000054776; Unassembled WGS sequence.
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   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361183};
KW   Protease {ECO:0000256|RuleBase:RU361183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   DOMAIN          176..373
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   REGION          92..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   384 AA;  44284 MW;  70DC98472A6E61A0 CRC64;
     MAAAGFNGIV KFDIKQPSID QWETNFTDYQ CLHHRDFLKR MSEFNSVKAD ACTMYRLARD
     SSLTIHFFCF LILTALHICG CLNSSDKSFL RNSSSTEKPK PDENASVVDN PKNTTINDNA
     KPDGNVDDDK ISSDENTEPE NIDDIEYLPG NIIKLHEQEF GFHDGDIAGV VYTGEEYITG
     FKYVIRKWPD HKIPYIIDPS YSDKERRFIE SSMRTVEKDT CIKFVNRTNE PYFLRVTNTK
     KGCYSYVGNQ QTIGGQILSL ESSADRSCMD RKVISHVLLH AVGFWHEHNR VGRKKKLSIK
     YQSVRPVLDP EYDPFHYLRY DQNSIMHYPP YAWGKPEQST MLPSNFLASA WIGKTRYMTN
     DDKYKVKQLY GCLKYPKITS EQAA
//
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