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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//