GenomeNet

Database: UniProt
Entry: A0A158NDQ6_ATTCE
LinkDB: A0A158NDQ6_ATTCE
Original site: A0A158NDQ6_ATTCE 
ID   A0A158NDQ6_ATTCE        Unreviewed;       380 AA.
AC   A0A158NDQ6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   Name=105618739 {ECO:0000313|EnsemblMetazoa:XP_012055664.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012055664.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012055664.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; ADTU01001088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012055664.1; XM_012200274.1.
DR   STRING; 12957.A0A158NDQ6; -.
DR   EnsemblMetazoa; XM_012200274.1; XP_012055664.1; LOC105618739.
DR   GeneID; 105618739; -.
DR   KEGG; acep:105618739; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; A0A158NDQ6; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000005205; 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; 2.
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; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT   DOMAIN          59..377
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        90..99
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        255..259
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        299..337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   380 AA;  43377 MW;  DF8ABD9E4D25EEC5 CRC64;
     MFRHLVVIAT LVVFNVSFRR ILLHKINSRR RAIDINFDRL TRAADIARQP LFSDGDIAYY
     GNITIGTPPQ VFNVLIDTGS PDLWIPSIIC TFKLSSRACM THNNYDNRKS STYRPDGRSF
     GIRYGNGAVG GYLSTDVMNI AGLDVQNQTF GEVTEQYGRS FEYAKYDGIL GLSYPILSPE
     GVIPLFSNMI NQQLVKNPIF SFYIKQQKSX WDGELILGGS DNRLYLGDFT YVDVTQKGYW
     QFTLDKIKME DKILCENSCQ AIVDTGTSLI IGPSTDITII NRRIGADHNN FTRGIFVNCN
     KTYNLPIIDF IVSGFRKLRL SSEDYIIKEI YNNEMVCMSA FVSDYQYKGD PAWILGDVFL
     RRYYTEFDMK HDRIGFVCIV
//
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