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
//