ID A0A090N6B5_STRRB Unreviewed; 422 AA.
AC A0A090N6B5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=SRAE_2000290110 {ECO:0000313|EMBL:CEG06135.1,
GN ECO:0000313|WBParaSite:SRAE_2000290110.1,
GN ECO:0000313|WormBase:SRAE_2000290110};
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:CEG06135.1};
RN [1] {ECO:0000313|EMBL:CEG06135.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000290110.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEG06135.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000290110.1}
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; CEG06135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090N6B5; -.
DR STRING; 34506.A0A090N6B5; -.
DR EnsemblMetazoa; SRAE_2000290110.1; SRAE_2000290110.1; WBGene00263117.
DR WBParaSite; SRAE_2000290110.1; SRAE_2000290110.1; WBGene00263117.
DR WormBase; SRAE_2000290110; SRP10101; WBGene00263117; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
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:SF888; ZINC METALLOPROTEINASE NAS-38; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 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.
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}; Hydrolase {ECO:0000256|RuleBase:RU361183};
KW Membrane {ECO:0000256|SAM:Phobius};
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|RuleBase:RU361183};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..262
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DISULFID 106..261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 422 AA; 50426 MW; 6D1EA44B46948AFE CRC64;
MINLKKLFLY LVIYILYIFP YIIYSTNFSS NDEYIKKRNI KRSIEETNNF KYDIRNIDEI
STNNRKKRDM TIIQYKWTSP IFYYVNYRLN FNTVKKALNL LEEYTCLKFS NPKNLFQIPT
GIRFLPSNKC SASLGKIVDK GWLMIYVGKE CENTLGIIRL IIRSLGIIYE HCRMDRNFFI
KVYEKNIAQS SKEDFQIFKE TYIKQIFLPY EYGSLMHFGM YTGSKNKMIT LTPKDIHYKH
TVGQQDFLTF NNVKALNMHY CSKICKKSIR CYNFGYQNPN NCDKCICIEG FDGIYCESYA
KSAAWCGPKE LYAKDRPIYF RIQGKKKCFY HILSTRNRQI EIVILKMRME PTHTQTCSIH
RSLEIKFWLD KSVAGARFCF QKYSKIIKSQ SNHVILYYRS NDHRSYVYLY FKEASQINIH
RE
//