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Database: UniProt
Entry: F4P8D4_BATDJ
LinkDB: F4P8D4_BATDJ
Original site: F4P8D4_BATDJ 
ID   F4P8D4_BATDJ            Unreviewed;       477 AA.
AC   F4P8D4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   03-MAY-2023, entry version 48.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=BATDEDRAFT_26425 {ECO:0000313|EMBL:EGF78601.1};
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:EGF78601.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF78601.1, 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; GL882888; EGF78601.1; -; Genomic_DNA.
DR   RefSeq; XP_006680664.1; XM_006680601.1.
DR   AlphaFoldDB; F4P8D4; -.
DR   GeneID; 18239029; -.
DR   HOGENOM; CLU_037528_0_0_1; -.
DR   InParanoid; F4P8D4; -.
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:SF12; ASPARTIC PROTEINASE 3-RELATED; 1.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 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..477
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003319011"
FT   DOMAIN          52..401
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          432..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  52464 MW;  A1152A8077EF49F7 CRC64;
     MLITLECVIL ALQAVSAVRL ALHPPVGIDS QSSNRLSKRS PVELGGDINK CYTIKVNVHG
     TDLGLRVDSD ASNIMVPLPS SSNDVSLASE STPSGEPVTI NYRRKQYKGL TSTAAVTIPG
     TRITDINLPV LAVEKQSPDI VGISSKFDGV FGFGHPYLLN RHSRITAMDV LYTNNVIPNN
     EVSLQLCPYD ILHESSINIG NTDITAKCGT DGSSVAWVES PTNNQFTVNI KSILVNGEQV
     DLPDEFQKRV ENGHTLYSVI QTCFRYMVFP ETVVAALIDA IVGSNAITIK NILFRNRLGK
     IAVKNILQKN HPMSKFEFKI KWEKLPSLSI TMFAKNPITD ENHDSVVTIK LGPRDYLQRV
     DSDEFEFIVA AGPNDNVILG IPFMNRLAVT FDRTHKRIGF GPGCGCEVMA DGYPTISNAD
     QVLWPLSHVR LPEQPSTSSS DGTSTLRRSL SRLGSTLRGS RRSKMTYRDS NGYWPLN
//
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