ID W2TMJ2_NECAM Unreviewed; 380 AA.
AC W2TMJ2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:ETN82237.1};
GN ORFNames=NECAME_08060 {ECO:0000313|EMBL:ETN82237.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN82237.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI658525; ETN82237.1; -; Genomic_DNA.
DR RefSeq; XP_013304464.1; XM_013449010.1.
DR AlphaFoldDB; W2TMJ2; -.
DR STRING; 51031.W2TMJ2; -.
DR MEROPS; A01.A69; -.
DR EnsemblMetazoa; NECAME_08060; NECAME_08060; NECAME_08060.
DR GeneID; 25348090; -.
DR KEGG; nai:NECAME_08060; -.
DR CTD; 25348090; -.
DR OMA; IACRMHN; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000053676; 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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF40; ASPARTIC PROTEASE 3; 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 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:ETN82237.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..380
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004825258"
FT DOMAIN 70..374
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 380 AA; 41713 MW; BA46487F3D2563AF CRC64;
MTHFLLLLLS ACVAVESFLR VPMHKTTYER NAYKVSSIAE YLKQKYIKGY KFDSNLAYNE
GLSDYSNAQY YGTVQIGTPP QTFQLLFDTG SSNLWFNCKK SSTCTETNQP FEIQYGSGSM
KGVVDNDVVC FGSDHKWCTD KTQGLACATQ EPGLAFVGAK FDGILGMGWD RISVNNIPQP
MDQIFANKAL CAEPVFAFWL NRDLNNNAAG GEMTLCGTDP AHYKGSIAWE PLVSEDYWRI
KLGSVTIDGT TYTNGPVDSI VDTGTSLLTG PTDAIKKIQK KIGAFAIFNG EYEIDCKRIP
QLPPITFNLG GQDFVLQGSD YILQVAQNGQ TTCISGFMGL DIPAPNGPLW ILGDVFIGKF
YSVFDNGNKR IGFAISANSN
//
