ID A0A090MZS4_STRRB Unreviewed; 400 AA.
AC A0A090MZS4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=SRAE_2000408800 {ECO:0000313|EMBL:CEF69439.1,
GN ECO:0000313|WBParaSite:SRAE_2000408800.1,
GN ECO:0000313|WormBase:SRAE_2000408800};
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:CEF69439.1};
RN [1] {ECO:0000313|EMBL:CEF69439.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000408800.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF69439.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000408800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {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; CEF69439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090MZS4; -.
DR STRING; 34506.A0A090MZS4; -.
DR EnsemblMetazoa; SRAE_2000408800.1; SRAE_2000408800.1; WBGene00264316.
DR WBParaSite; SRAE_2000408800.1; SRAE_2000408800.1; WBGene00264316.
DR WormBase; SRAE_2000408800; SRP07424; WBGene00264316; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:SF879; METALLOENDOPEPTIDASE-RELATED; 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 22..400
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5015017759"
FT DOMAIN 51..243
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
SQ SEQUENCE 400 AA; 46022 MW; B2492C806568F62F CRC64;
MRLPFILIFK LSLIFFIKTS AIENSENDLN VASTFTKDDI DLPMQSLRMK RAMSTELKYE
WKFPIKFYIA DDINTTAVRV GLKRFEKYTC LRFKEECFEL GRHQGIRFFR GKGCASSLGK
VFENEPQGLS LAYTCDTPGT VQQTMGHALG MLREQRRIDN DKYVRRLLWN INTTYLGKFM
KKNASDTYGV PYDIGSGMHS GRYDYSVNKK DTILPLDKSF IKTIGQIEFS FNDYKLLNIY
YCNNQCPVKL KCLNYGYTDP NNCNICRCPT FYGGKYCHKR RISDEGCPPA EIQLNQRETS
FTIIGKKTCF FYITTDEKKK IRVNLGPSTK MYVNPLSKDW CPVGKGLEIR HITDKGSTGA
MFCGKMKGSV TLSEANYTNI KYVGTSDDDR LHLILLREPN
//