ID F4NYC6_BATDJ Unreviewed; 476 AA.
AC F4NYC6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 08-NOV-2023, entry version 50.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=BATDEDRAFT_87185 {ECO:0000313|EMBL:EGF81998.1};
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:EGF81998.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF81998.1, 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; EGF81998.1; -; Genomic_DNA.
DR RefSeq; XP_006677600.1; XM_006677537.1.
DR AlphaFoldDB; F4NYC6; -.
DR GeneID; 18242702; -.
DR HOGENOM; CLU_037528_0_0_1; -.
DR InParanoid; F4NYC6; -.
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 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; 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..476
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003318731"
FT DOMAIN 52..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 476 AA; 51955 MW; 5CF3ECD8E24052E4 CRC64;
MLITLECILL ALQAVAAVRL ALESPFEITS PSSNRLSKRS PVELGGDITK CYTIKVNVHG
VDLDLQVNSA MSDIVVPLSS SSNDIGLAPE STPSGQPVTI NYKGKEYRGI SSTADVTIPG
TSITDINLPV LSVEKQSADL VGISPNLDGV FGFAYSSLSK HHPPITAMDV LYSNGVIPSN
EIGLQLCPYD MTSDSFINIG NTDVTAKCGT DGKSIAWVKS PSADYFTVNI KSILVNGKRV
NLPEEFQKRV EHGRTLYSIV ETCFRYMYFP KVVVAALVDA IVGSGAITIK RIKLKRKLYP
EEIDDVFWKD GLMAESSFSI DWGKLPTVSI TIFAENPVTV ENRNSVVAIK LGPKDYIQRY
DSKNFEFAVK AGSNDKAVLG ISFMTRLTMT FDRAHKRIGF GPGCGCEVMA DGYPTISNGY
QMLWPSSQLP EQPTTSGSDG TFIRRRKPIT TTDQVAVPEN THHAVKSYKQ TLNKLD
//