ID   A0A0M8ZQY4_9HYME        Unreviewed;       493 AA.
AC   A0A0M8ZQY4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=Peroxisomal leader peptide-processing protease {ECO:0000256|PIRNR:PIRNR037989};
DE            EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR037989};
GN   ORFNames=WN51_06878 {ECO:0000313|EMBL:KOX67833.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX67833.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX67833.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX67833.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX67833.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peroxisomal protease that mediates both the removal of the
CC       leader peptide from proteins containing a PTS2 target sequence and
CC       processes several PTS1-containing proteins. Catalyzes the processing of
CC       PTS1-proteins involved in the peroxisomal beta-oxidation of fatty
CC       acids. {ECO:0000256|PIRNR:PIRNR037989}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|PIRNR:PIRNR037989}.
CC   -!- PTM: The full-lengh TYSND1 is the active the proteolytic processing of
CC       PTS1- and PTS2-proteins and in self-cleavage, and intermolecular self-
CC       cleavage of TYSND1 down-regulates its protease activity.
CC       {ECO:0000256|PIRNR:PIRNR037989}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family.
CC       {ECO:0000256|PIRNR:PIRNR037989}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ435969; KOX67833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8ZQY4; -.
DR   STRING; 166423.A0A0M8ZQY4; -.
DR   OrthoDB; 7519at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0016485; P:protein processing; IEA:InterPro.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR039245; TYSND1/DEG15.
DR   PANTHER; PTHR21004:SF0; PEROXISOMAL LEADER PEPTIDE-PROCESSING PROTEASE; 1.
DR   PANTHER; PTHR21004; SERINE PROTEASE-RELATED; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037989};
KW   Peroxisome {ECO:0000256|PIRNR:PIRNR037989};
KW   Protease {ECO:0000256|PIRNR:PIRNR037989, ECO:0000313|EMBL:KOX67833.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW   Serine protease {ECO:0000256|PIRNR:PIRNR037989}.
SQ   SEQUENCE   493 AA;  54795 MW;  6AC5B8E87652BEB9 CRC64;
     MISYGCSGIL IARDWVLAHG SILDPVLFRS PDFLRFFTVL NPGELITIQT SEGLIDDLTF
     QVHRNHSLKK SAKLVAVWRC PLLKETLDNS LRNFTFKNQH GSDHLLSSVF LVIKCKSFET
     TAETKERESD KTKIGQILFQ LAKQAAIGKL TKGAIVELIS TPFGNPFFID STSHGIVGNL
     LGVNECLILI DVTSFPGCEG SPIFLTNDRG EKNICGMVIA SSIQYHGEWM NCTFAANLLP
     SLKLILRSRA LNFRDFQYSS YAILPYTLEK SVAIVKCGPN RGTGTLVDEQ TGTFITCAHV
     VTMAPERRIK LATSHADRYE WFAEANLIYK TSNGQPYDIA VLKIDRKFKE SYLFLSMKAI
     KLADRDAQKG EQILSIGFPI SLKGRPTVSS GVVSKSWKHM FQTNCCVYSG VSGGPIVRRA
     NFEMLGIVVC NVTLSNDSLL YPRLCMAIPT VVLKNPLDDY LRTADPRALE ALTQYDESVA
     ATWNFCPFLL SNI
//