GenomeNet

Database: UniProt
Entry: Q8MY59_BRUMA
LinkDB: Q8MY59_BRUMA
Original site: Q8MY59_BRUMA 
ID   Q8MY59_BRUMA            Unreviewed;       393 AA.
AC   Q8MY59; A0A0K0JAH4;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 114.
DE   SubName: Full=Aspartic protease BmAsp-1 {ECO:0000313|EMBL:BAC05688.1, ECO:0000313|WBParaSite:Bm3492a.1};
DE   SubName: Full=Bm3492 {ECO:0000313|EMBL:CDP98437.2};
GN   Name=asp-1 {ECO:0000313|EMBL:BAC05688.1};
GN   Synonyms=Bma-hrg-7 {ECO:0000313|WBParaSite:Bm3492a.1};
GN   ORFNames=Bm3492 {ECO:0000313|EMBL:CDP98437.2}, BM_Bm3492
GN   {ECO:0000313|EMBL:CDP98437.2};
OS   Brugia malayi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6279 {ECO:0000313|EMBL:BAC05688.1};
RN   [1] {ECO:0000313|EMBL:BAC05688.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Athauda S.B., Nomura H., Inoue H., Takahashi K.;
RT   "Cloning, expression and histochemical analyses of aspartic proteinases of
RT   filarial parasite Brugia malayi.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDP98437.2, ECO:0000313|Proteomes:UP000006672}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FR3 {ECO:0000313|EMBL:CDP98437.2,
RC   ECO:0000313|Proteomes:UP000006672};
RX   PubMed=17885136; DOI=10.1126/science.1145406;
RA   Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA   Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA   Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA   Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA   Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA   Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA   Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA   Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA   McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA   Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA   Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA   Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA   Blaxter M.L., Scott A.L.;
RT   "Draft genome of the filarial nematode parasite Brugia malayi.";
RL   Science 317:1756-1760(2007).
RN   [3] {ECO:0000313|EMBL:CDP98437.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FR3 {ECO:0000313|EMBL:CDP98437.2};
RA   Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA   Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|WBParaSite:Bm3492a.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2019) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; AB078419; BAC05688.1; -; mRNA.
DR   EMBL; LN856998; CDP98437.2; -; Genomic_DNA.
DR   RefSeq; XP_001898394.1; XM_001898359.1.
DR   AlphaFoldDB; Q8MY59; -.
DR   STRING; 6279.Q8MY59; -.
DR   MEROPS; A01.053; -.
DR   EnsemblMetazoa; Bm3492a.1; Bm3492a.1; WBGene00223753.
DR   GeneID; 6101837; -.
DR   KEGG; bmy:BM_BM3492; -.
DR   WBParaSite; Bm3492a.1; Bm3492a.1; WBGene00223753.
DR   CTD; 6101837; -.
DR   InParanoid; Q8MY59; -.
DR   OrthoDB; 2875862at2759; -.
DR   Proteomes; UP000006672; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF8; ASPARTIC PROTEASE 1-RELATED; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:BAC05688.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006672};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..393
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013535897"
FT   DOMAIN          69..390
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        312..350
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   393 AA;  44217 MW;  2C22469C908C107E CRC64;
     MKTAVVLIVL YHITFIVDAA VSRVTVKRTH SIRQQLLRAG KLKEYNRLVQ PVLRETGMTG
     FLEYMDNIYL INITIGSPPQ NLKVVPDTGS SDLWVISIDC KSNSCIEGGN MHTKNRFDPS
     KSSTYSSYGQ NFSITYALGY SKGILGIDQL SFADLTVANQ IFGLANHIAI SFGNFSMDGI
     MGLAWPALSS FQVTPPMQNI ISELDFPIMT VYLSPYLETS MDETDGGVIT FGNFDFDNCE
     TVERWVQITS QTFWQFTIKG VKVNLHETTS WQQAISDTGT SYLQIPSFLM KLMVQNINAT
     YSFDYEAYIV NCVMQDIGPN IEINIDGIYY SILPDQYIQK YLNEHGQPVC IFAALENYGV
     GFNPSWILGD VFIRSYCNVY DFANDRIGFA EIL
//
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