ID   F4P6H5_BATDJ            Unreviewed;       458 AA.
AC   F4P6H5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=BATDEDRAFT_89959 {ECO:0000313|EMBL:EGF79350.1};
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:EGF79350.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF79350.1, 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; GL882886; EGF79350.1; -; Genomic_DNA.
DR   RefSeq; XP_006680113.1; XM_006680050.1.
DR   AlphaFoldDB; F4P6H5; -.
DR   GeneID; 18243700; -.
DR   HOGENOM; CLU_037528_0_0_1; -.
DR   InParanoid; F4P6H5; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..458
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003312705"
FT   DOMAIN          52..401
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          430..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  50182 MW;  DB10DFA8483AB535 CRC64;
     MLITLECVIL ALQTVAAVRL ALESPSGTSS QSSNRLSKRS PVELGGDAYQ CYTMKFNVHG
     TDLNLRVDSA MSDIIVPLPS SSSDIGLAPQ HTPSGEPVTI GYKGKEYKGV TSTAVVTIPG
     TRITDISLPI LAVRKQSADL VGISSNFDGV FGFAYSSLSK HHPPATAMDV LYTSDVIPSN
     EIGIQLCPYE MISDSFINIG NTDVTAKCGT NGRSVAWVQS PSDDYFTVNI KSILVNGKRV
     ELPAGFQKKV EHGRTLYSVM ETCFTYMQFP KVVVAALVDA IVDSNAIAID IFNFKYRLNN
     LQIENLYWKN HLMPEKYFSI NWGKLPSLSI VMHAETPVTD DNYNSVVTIR LGPRDYIQRV
     DSKNFVFAIK AGLNDKATLG MSFMSRLGLT FDRAHTRIGF GAGCGCEVST SKYPTILNSD
     QVLWPLPRVR LPKPTTSGSD GTFIRRRKSK TTRSSSRT
//