ID F4P2R0_BATDJ Unreviewed; 656 AA.
AC F4P2R0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=BATDEDRAFT_24795 {ECO:0000313|EMBL:EGF80062.1};
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:EGF80062.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF80062.1, 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 S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR EMBL; GL882884; EGF80062.1; -; Genomic_DNA.
DR RefSeq; XP_006678926.1; XM_006678863.1.
DR AlphaFoldDB; F4P2R0; -.
DR GeneID; 18238596; -.
DR HOGENOM; CLU_417952_0_0_1; -.
DR InParanoid; F4P2R0; -.
DR OMA; TDQQFVQ; -.
DR OrthoDB; 7264at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 45..258
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 445..654
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 656 AA; 73572 MW; 6FA4B4B0AD898DBA CRC64;
MAVTRLVWQA ATPSSMHRFK FKTVVYFSYQ SRLSSSKVVH ALPRRIDPLS SLEDWDEQAV
SQETARTRIL QGKLSRFSRT LRDEMRRIYP RTRAFPCTDI VDGYEYRTSF ENGAMVVSRQ
KTNTAGSCEI VLDSRWLGWG SRGKTVSKAV VSDDHNKIAF LQTRPQDEQG SLVIRTLNSN
APAMFTYSQS IPNVFNFVWA NNSKTIYFTR LDDVLRSSKV YRIDVDSPHE ETVVYSEMDI
LYFVDLARSK DKDSLFLLHN YASTELKLYR TSLSTVLTGK AINLESDTSI VAAPGYEESI
DDVEIFPSHA VLTMKRQGQP FIRSIDLVNM LANDVFLSDS SGVISPEPNI DLTSNTFRFS
YSSPFVIQAV YELNLVLGKL INWQDIRPCM DTNNFVIEKQ TIPSRDGTCN IPITILKNKN
ISHSPSNPCV ILVYGSYGYC IETSFRVELL PALSRGVTVV FAHVRGGGEL GNSWYHKGRA
ENKLCSFTDL EDVADMLIYK KYTSSERLGG IGTSAGGMLL ADLFKALVLR VSFLDPLTTM
LDPNSSLSAG EVLEWGNPLK DSAAYQLMSS YSPYDNLDGK LRTAVLATAG SDDQRVPPWH
ALKYIVRMHE LAQHSGTASN GYFKLYADRG HNQGSGDNID EHAFEYAFLL SKLGCK
//
