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Database: UniProt
Entry: F4PET9_BATDJ
LinkDB: F4PET9_BATDJ
Original site: F4PET9_BATDJ 
ID   F4PET9_BATDJ            Unreviewed;       473 AA.
AC   F4PET9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=BATDEDRAFT_28688 {ECO:0000313|EMBL:EGF76308.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF76308.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF76308.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; GL882898; EGF76308.1; -; Genomic_DNA.
DR   RefSeq; XP_006683071.1; XM_006683008.1.
DR   AlphaFoldDB; F4PET9; -.
DR   GeneID; 18239718; -.
DR   HOGENOM; CLU_037528_0_0_1; -.
DR   InParanoid; F4PET9; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000007241; 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   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   PANTHER; PTHR47965:SF12; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
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:UP000007241};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..424
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   473 AA;  51614 MW;  DA4A70B6CCC17399 CRC64;
     MYQIQPIFIT ILDTMLITLE CVILALQTVS AVRLALESPI GTTSQSNNRL SKRSPVVLDG
     DIKKCYTIKV NADGVNLDLY VDSTMSDTIV PLPSSSNDVG LTPQHTPSGE PVTIDYKGDE
     YSGVSSNAVV TIPGTSITDI NLPVVAVQKQ SPDLVGINPN LDGVFGFAYS SLSKHHPQTT
     AMDVLYNGGV IPNNEIGLQL CPYEMTSNSF INIGNTDVTA KCGTDGTSVA WVQSPSDDQF
     TVNIKSILVN DEPVDLPEEF QKTIMENGRI LYSSVETCFL HMRFPEVVVD VLINAILDSG
     AITVNINIFS DKLGKVMVKK IFSQNYAMLE SGFDIDWGKL PTLSITMFAQ NPVTDANRNS
     VVTIKLGPKD YIQRVDSKNC KYLTIVCIRF AIKAGSNDKA VLGIPFMTQL GLTFDLQNKR
     IGFGAVCGCK VSTSKYPTIS NSYRVLWPLP RVRLPEQPST SGSSGTFIRR RKP
//
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