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Database: UniProt
Entry: F0XXL8_AURAN
LinkDB: F0XXL8_AURAN
Original site: F0XXL8_AURAN 
ID   F0XXL8_AURAN            Unreviewed;       212 AA.
AC   F0XXL8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE   Flags: Fragment;
GN   ORFNames=AURANDRAFT_4422 {ECO:0000313|EMBL:EGB12328.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB12328.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; GL833121; EGB12328.1; -; Genomic_DNA.
DR   RefSeq; XP_009032841.1; XM_009034593.1.
DR   AlphaFoldDB; F0XXL8; -.
DR   EnsemblProtists; EGB12328; EGB12328; AURANDRAFT_4422.
DR   GeneID; 20222044; -.
DR   KEGG; aaf:AURANDRAFT_4422; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; F0XXL8; -.
DR   OMA; THSITCE; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000002729; 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; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002729}.
FT   DOMAIN          1..212
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        205
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        32..36
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGB12328.1"
FT   NON_TER         212
FT                   /evidence="ECO:0000313|EMBL:EGB12328.1"
SQ   SEQUENCE   212 AA;  22452 MW;  0CDF90921136B89F CRC64;
     YYGSIALGTP PQPLEVIFDT GSADFWVASK GCDASCAGLD VFDSAASATY EADGKAFSIN
     YIDGDAVHGA RAYDTMTWAG LEVPHQAFAE IEGMGDFYVC GGEDGLLGLA FGSLSHLKAA
     TPLENILPQL DAPIFAFHVP NGGDDDAGEL TLGGVDPAKF RGNLTWVDLA PPHHRNRRDY
     WDVPLEGVTF GDLALPTDRS RAVVDTGTTL IV
//
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