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Database: UniProt
Entry: A0A1I7ZE19_9BILA
LinkDB: A0A1I7ZE19_9BILA
Original site: A0A1I7ZE19_9BILA 
ID   A0A1I7ZE19_9BILA        Unreviewed;       616 AA.
AC   A0A1I7ZE19;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   10-APR-2019, entry version 16.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g2551.t1};
RN   [1] {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g2551.t1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26392177; DOI=10.1186/s13059-015-0746-6;
RA   Dillman A.R., Macchietto M., Porter C.F., Rogers A., Williams B.,
RA   Antoshechkin I., Lee M.M., Goodwin Z., Lu X., Lewis E.E.,
RA   Goodrich-Blair H., Stock S.P., Adams B.J., Sternberg P.W.,
RA   Mortazavi A.;
RT   "Comparative genomics of Steinernema reveals deeply conserved gene
RT   regulatory networks.";
RL   Genome Biol. 16:200-200(2015).
RN   [2] {ECO:0000313|WBParaSite:L893_g2551.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) 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.
CC       {ECO:0000256|RuleBase:RU361183};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   WBParaSite; L893_g2551.t1; L893_g2551.t1; L893_g2551.
DR   Proteomes; UP000095287; Whole Genome Shotgun Assembly.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR000859; CUB_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   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   PROSITE; PS01180; CUB; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000095287};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS01008102};
KW   Hydrolase {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973787};
KW   Metal-binding {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973795};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS01068076};
KW   Protease {ECO:0000256|RuleBase:RU361183,
KW   ECO:0000256|SAAS:SAAS00973825};
KW   Zinc {ECO:0000256|RuleBase:RU361183, ECO:0000256|SAAS:SAAS00973802}.
FT   DOMAIN      423    528       CUB. {ECO:0000259|PROSITE:PS01180}.
SQ   SEQUENCE   616 AA;  69126 MW;  AD8C5E3612C65F83 CRC64;
     MTPLALLMFQ HVYYTFTLLV PQRAETSAIS AHLAISKWNE LVQVQAALAS SWSLQIESAP
     YCLRRCAKIS YVDRGRMAPE LTQRRFARGD SQSRPAAFSG DVFWSQGVSG LEAGRRIASA
     KCRIKSALAL NLLRRLRHRS FRLFLPPGME SMSSGNETHF TIIENVSRTK FHRHRRQAIA
     GPMYNWPSSE IPFQIWGGDF NFQQLIRRGI RMWEEHTCLR FRENAQRHDG IRFVLENGES
     CFTEHIGHKV GFQDIIIGSE CAEDYVVAHE IAHALGFWHT HQRPDREKFI TINWNNVLEE
     ATASFIPFRS MLQAFGIRQV SNQRLPYDYG SLMHYNAVAH AVKTSDYTIV PKELKYLTTM
     GTEKIAFLDA KIINDIYCPN ICTGRQQLRC QGGGYPNPNN CNVCRCPEGL GGAQCDQLQP
     STCGEEIRAT GQWQTLSSPP GKTIHCYWRI SVPEGSRVRF RLSDGEFPCT YGCQSYVEIK
     HKMDVRLTGF RSCCWRPKEA TVSEGNQIFV IYHPNGKKAG FSLRSFANFH TVGHGLNGTA
     VAGDGVHGQE GAVADVVVLS VEHLPAEAAD VVLRSVLHEA RGVVGVVEPF LQLDDALDEA
     VFGFRSLADP VLAQGI
//
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