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Database: UniProt
Entry: A0A090N0G1_STRRB
LinkDB: A0A090N0G1_STRRB
Original site: A0A090N0G1_STRRB 
ID   A0A090N0G1_STRRB        Unreviewed;       402 AA.
AC   A0A090N0G1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   ORFNames=SRAE_2000525300 {ECO:0000313|EMBL:CEF70628.2,
GN   ECO:0000313|WBParaSite:SRAE_2000525300.1,
GN   ECO:0000313|WormBase:SRAE_2000525300};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF70628.2};
RN   [1] {ECO:0000313|EMBL:CEF70628.2, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_2000525300.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF70628.2};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_2000525300.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) 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   EMBL; LN609529; CEF70628.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090N0G1; -.
DR   EnsemblMetazoa; SRAE_2000525300.1; SRAE_2000525300.1; WBGene00265513.
DR   WBParaSite; SRAE_2000525300.1; SRAE_2000525300.1; WBGene00265513.
DR   WormBase; SRAE_2000525300; SRP10808; WBGene00265513; -.
DR   OrthoDB; 2890824at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
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; IPR000742; EGF-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; 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.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW   Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           19..402
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5015017762"
FT   DOMAIN          54..249
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        93..248
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   402 AA;  47974 MW;  653FAA3FCD921B74 CRC64;
     MIYVFFFIIL FNNYFTIEEN ITKKNFKRSV DQINNFVLNF PELTNSKINS RKKRKIITNT
     RFKWPLTIQY YYKSPINFDA IKNVVKVIEK ETCFKFRKSR STYFDSPGIH YNYTGKCSSA
     IGNIQKEAWQ KIEIGPRCNN FEGILHETLH ALGLYHEQCR FDRDFFVKIY KENMLQNETA
     SCKKHTAYEG FHYHLSYDYG SIMHSAVNVF AKGNLKTIIP TDPLYETTMG QTKKLSFIDI
     KALNLHYCTH PNCPFKRHCY NYGYQDPHNC HLCKCIDGFI GSQCELFKKR QESCWKTMIF
     PDRKRRSFYL DGKRKCVIHF IVNKTSRIKF NIVKVSMFPN TYPTCQYENT IEVKYWMDKS
     VTGARFCRQT ENKIIFSHNN HIIYHHRSTQ RNNFAIIYYN EI
//
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