ID W2TW95_NECAM Unreviewed; 388 AA.
AC W2TW95;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:ETN85272.1};
GN ORFNames=NECAME_06498 {ECO:0000313|EMBL:ETN85272.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Bunostominae; Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN85272.1, 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}.
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DR EMBL; KI657772; ETN85272.1; -; Genomic_DNA.
DR RefSeq; XP_013307499.1; XM_013452045.1.
DR AlphaFoldDB; W2TW95; -.
DR MEROPS; A01.A75; -.
DR EnsemblMetazoa; NECAME_06498; NECAME_06498; NECAME_06498.
DR GeneID; 25346530; -.
DR KEGG; nai:NECAME_06498; -.
DR CTD; 25346530; -.
DR OMA; SQGFWQV; -.
DR OrthoDB; 2874784at2759; -.
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 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF45; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:ETN85272.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..388
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004826818"
FT DOMAIN 70..383
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 101..106
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 388 AA; 42576 MW; 704AC3183EBEAE28 CRC64;
MKLTLALLAL VGCTMAAVYK SHVTKIESAR MRMIREGTWS EYIKKRDAYR TAMRGDVIPQ
VAHDYNDVTY VGNITLGTPE QTFTVVLDTG SSNLWVPDAS CHVPVCSKKN KFDQSGSSTY
KENGERWEIR YGTGSAAGIL AEETLRFGDQ GTQQLVVPET VFGQAQMLAP FFNTQPLDGI
LGLGFPELAV NGVLPPFHRA VKQGLLDQPI FTVFLKHVGN QVNVPGGVYT YGGLDNENCG
EVIAYEPLSS ATYWQFNIEG YGAGSFSTNQ RTEGMSDTGT SFMGVADALL RPLIRGLGAQ
YDSRTGVFYM PCDADPNLDF IIGGKTYSIK AENLLLYGDG HFCMLPLFGK DAMGFGPAWV
LGDPFIRQFC NIHDIEKKQI GFAESKQQ
//