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Database: UniProt
Entry: A0A024FU92_9STRA
LinkDB: A0A024FU92_9STRA
Original site: A0A024FU92_9STRA 
ID   A0A024FU92_9STRA        Unreviewed;       457 AA.
AC   A0A024FU92;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=BN9_082530 {ECO:0000313|EMBL:CCI10234.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI10234.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI10234.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI10234.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCI10234.1}.
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DR   EMBL; CAIX01000160; CCI10234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024FU92; -.
DR   STRING; 65357.A0A024FU92; -.
DR   InParanoid; A0A024FU92; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..366
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   457 AA;  50377 MW;  05D51D6664B2DBED CRC64;
     MRSLGSRYEK VQLIEKRIQP EISTKSTRFL QATNAEKILL RTYQQVIYMA KMQIADSSFV
     VMVDTGSSDL WVSCSFVKNS GCSRTCPKSN IVIRYGSGDV CVVPKSARIK LGSLEIDEYT
     FGIAHGSNVL DTGNIRSKLL VGDSQGLLGL AYGSISSYQS RAGQLIDYLT SFSIFLGQEH
     NNESFLLLNG VDTALIEQQR WQPYVINLKR SAHWTIGMTG FRVGKEKSIF PCADDIPFSG
     SSSSCDTIVD TGTSLIYMPN LVYEGFTRNY LKPIGCVLDD TSSTYICPSS KELPRLEFTF
     DNASFTLSAS EYSLPASPSH VYIEIQPIST SMITVSPLDN SWIIGATFLR KYYSSYEVNR
     SVTFYCEAGQ CGSNNTISTP AFGYPTSGSD LLPNTGALMS PATVMRTLYI LLVILGVVGI
     FSVILSCLRR CSYKRRPLGT NGEYGANYNA GFTPRRI
//
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