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Database: UniProt
Entry: E2AZX9_CAMFO
LinkDB: E2AZX9_CAMFO
Original site: E2AZX9_CAMFO 
ID   E2AZX9_CAMFO            Unreviewed;       263 AA.
AC   E2AZX9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Cathepsin D {ECO:0000313|EMBL:EFN61010.1};
GN   ORFNames=EAG_01016 {ECO:0000313|EMBL:EFN61010.1};
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:EFN61010.1, 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, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; GL444282; EFN61010.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2AZX9; -.
DR   STRING; 104421.E2AZX9; -.
DR   InParanoid; E2AZX9; -.
DR   Proteomes; UP000000311; 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; 2.60.40.1960; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT   DOMAIN          37..263
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   263 AA;  30225 MW;  380F55078110067E CRC64;
     MDFLPFILEK ADIKLQKVPS VQNFPSVRLT NIDNVIYYGT ISIGIPPQEF KVVFDSGSPY
     FWIFPKKSTN PVALTRSQYD NTSSNPYIPN NTSFHVLLYR YLDYNVTGFL STDTVNVANL
     NVERQTFLKA VNISNEHMLE SYLNKSDRKY DGLLGLSYQQ TFEPFSVIEN MIHQGLMSSG
     IFSFYLNNIP VGEIKPVFYN MIQQKLVSSG IFSFYLNRNA SADFGGKLLF GGSDPAYYEG
     DFTYIPVTNR KYWQFTIDRF VIF
//
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