ID F4P0R9_BATDJ Unreviewed; 393 AA.
AC F4P0R9;
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=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=BATDEDRAFT_24209 {ECO:0000313|EMBL:EGF81328.1};
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:EGF81328.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF81328.1, 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 S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; GL882882; EGF81328.1; -; Genomic_DNA.
DR RefSeq; XP_006677935.1; XM_006677872.1.
DR AlphaFoldDB; F4P0R9; -.
DR STRING; 684364.F4P0R9; -.
DR GeneID; 18238411; -.
DR HOGENOM; CLU_020120_2_1_1; -.
DR InParanoid; F4P0R9; -.
DR OMA; RVENNGY; -.
DR OrthoDB; 2159919at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0012501; P:programmed cell death; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007241}.
FT DOMAIN 302..335
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 42419 MW; A05C7C7A260C9279 CRC64;
MPRLLTPSQV NAYNTSSIHE PVHSDQVLQP NHNPQPHSRK SSTSGGAFIA DAVEKVIESV
VNLSVETEVT SFFGNKTLVS SGSGFFVTTD GKILTNAHVV ADMNEDSKLW VTAADGLRYP
AKVHSLDTLS DLAIVRIQPR SSPHKWQPVQ FGTNHHLRPG DWVIAIGSPF GLQNTVTAGV
VSSRSRRSIE IGTKDTRVEY IQTDCVVHSG SSGGPLVNLD GQVVGINTTR AESEGISFAI
RVDNAMDMIH QLVVDGRVTR PWLGIRMITL TPHVRSQLNP DSHYTSSFQN TPNMILPHVT
SGVLVASVEA KSPASDGGLK DGDVIVAVDG VGIRSSQELL KLVGLRVGEP FAMRIKRCVP
NHLDEITEEE RVVNVTPGAL DMFVHSNGGS EIL
//
