ID   F4NYI5_BATDJ            Unreviewed;       514 AA.
AC   F4NYI5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=BATDEDRAFT_23274 {ECO:0000313|EMBL:EGF82030.1};
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:EGF82030.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF82030.1, 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; GL882881; EGF82030.1; -; Genomic_DNA.
DR   RefSeq; XP_006677240.1; XM_006677177.1.
DR   AlphaFoldDB; F4NYI5; -.
DR   GeneID; 18238170; -.
DR   HOGENOM; CLU_037528_0_0_1; -.
DR   InParanoid; F4NYI5; -.
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}.
FT   DOMAIN          90..443
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          470..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  56179 MW;  D8D3265F8D15F623 CRC64;
     MCYIVECICQ ELLNCEGIGI KTRVDDEKLY GIFINLDMST AMEECVILAL QAVAAVRLAL
     ESPIGATGQS NNRLSKRSPV ELGDDVAQCY TIKSNVDGVD LDLRVDSSVS GIMVPLPSSS
     NDVGSTPESI SSGKPVTIKY KGNEYRGISS TAVVTIPSTR ITGINLPVLS VEKQSAGLVG
     IGGNPDQGVF GFGYTSLSNH HSRVTAIDAL YNGGVIPKNE VSIQLCPYEM LSKSSINIGS
     TDVTPKCGTN GKSVAWIQSP SDDQFTVNIK SILVNGKQVE LPEEFQKNQG KNGRILYSYI
     HTCFVYMRFP ETVVAALVDA IVGSNAITVK KTKSEHKRKL SETEIGKIFW ENRLIPKSKL
     NINWGRLPSL TITMFAENPV TDDNRDSVVT IKLGPKDYLH KYDSKHARFT VKSGPNDKAV
     LGIPFMTRLR LIFDQTHKRI GFGPGCGCET ATDGYPIISN NDQVLWPSSH VRLPKQPSGS
     SSGRTSTLRR SFSRLGSIRR SSRRSKVSYE KLED
//