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Database: UniProt
Entry: E2AA94_CAMFO
LinkDB: E2AA94_CAMFO
Original site: E2AA94_CAMFO 
ID   E2AA94_CAMFO            Unreviewed;       227 AA.
AC   E2AA94;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Lysosomal aspartic protease {ECO:0000313|EMBL:EFN69674.1};
DE   Flags: Fragment;
GN   ORFNames=EAG_12012 {ECO:0000313|EMBL:EFN69674.1};
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:EFN69674.1, 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; GL438030; EFN69674.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2AA94; -.
DR   STRING; 104421.E2AA94; -.
DR   InParanoid; E2AA94; -.
DR   OMA; VECYRIF; -.
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; 2.40.70.10; Acid Proteases; 2.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:EFN69674.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT   DOMAIN          1..224
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        149..186
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFN69674.1"
SQ   SEQUENCE   227 AA;  25558 MW;  AF4245FE91D1A220 CRC64;
     NGYDSRNSST YIVNSTSVYR EYPILSIHGF LSTDRVNIAG LNVDNQTFIE VTDMSNRDLF
     QTALFDGVLG LRFNTSVFHN IVNQGLVSSP IFSYYLNRIQ INRNNLCTNS CQAIVGTGSG
     VTIGPISDIE KINELIITTN VNGEERVECY RIFELPTIRF ILGGKAFDLT ANDYIVRVNH
     KKNTICASGF LGRNLRTLDW ILGDAFIGKY YTEFDMENNR MGFALTK
//
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