ID W2T7M3_NECAM Unreviewed; 395 AA.
AC W2T7M3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:ETN77166.1};
GN ORFNames=NECAME_03266 {ECO:0000313|EMBL:ETN77166.1};
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:ETN77166.1, 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; KI660189; ETN77166.1; -; Genomic_DNA.
DR RefSeq; XP_013299393.1; XM_013443939.1.
DR AlphaFoldDB; W2T7M3; -.
DR MEROPS; A01.053; -.
DR EnsemblMetazoa; NECAME_03266; NECAME_03266; NECAME_03266.
DR GeneID; 25343303; -.
DR KEGG; nai:NECAME_03266; -.
DR CTD; 25343303; -.
DR OMA; TKATFDW; -.
DR OrthoDB; 2875862at2759; -.
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: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 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:ETN77166.1};
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..395
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004825863"
FT DOMAIN 69..388
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..348
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 395 AA; 42731 MW; 7C0C1D002090EC38 CRC64;
MRTLVVLAAL VAVLYAKTFT METRSSGSLR ARLIAANLYQ KFLEDEHLRR AQILASGSQP
FIDYADDFYL GNVTLGTPPQ TTTLVLDTGS SNLWVIDAAC KTAACNGEPN SGYTKHKFDT
TKSSTFTKET RTFSIQYGSG SCNGYLGTDT ISFGGLTIKT QEFGVATHLA AVFGYQPVDG
ILGLGWPALA VDSVVPPMQN LLSTLDQPLF TVWMDRKLTI SNGGNAGLIT YGAIDTKNCQ
SQINYVPLSA ETYWQFPIQG FSIGSYSESK KEQVISDTGT SWIGAPTTAV NAVVKQTGAK
YDSLNELYTV DCSTMKTQPD LIFTINGVTY NVPSVEYVLD LGLGNGKCAL TFFAMGSGSF
GPAWILGDTW IRTYCNIYDI GQKRIGFAKA NHSGI
//
