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Database: UniProt
Entry: E2A3T9_CAMFO
LinkDB: E2A3T9_CAMFO
Original site: E2A3T9_CAMFO 
ID   E2A3T9_CAMFO            Unreviewed;       151 AA.
AC   E2A3T9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Lysosomal aspartic protease {ECO:0000313|EMBL:EFN71900.1};
GN   ORFNames=EAG_01254 {ECO:0000313|EMBL:EFN71900.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN71900.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; GL436479; EFN71900.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2A3T9; -.
DR   STRING; 104421.E2A3T9; -.
DR   MEROPS; A01.057; -.
DR   InParanoid; E2A3T9; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1960; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EFN71900.1};
KW   Protease {ECO:0000313|EMBL:EFN71900.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT   DOMAIN          1..151
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   151 AA;  17019 MW;  55B3640528F22CAD CRC64;
     MTPVFSNMIQ QGLASAGIFS FYLNRNTSSN FGGKLIFGGS DPAYYEGNFT YVPVSVQGYW
     QIIIDRISYM PTIKFNLGGK AFNLTGKDYT IRDQDNDSLC VSLFMKHPDS LDEGDVELVK
     LWVLGMPFIG RYYTEFDMER GRVGFALAKN V
//
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