ID A0A087R312_APTFO Unreviewed; 192 AA.
AC A0A087R312;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 03-MAY-2023, entry version 36.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|ARBA:ARBA00012915, ECO:0000256|PROSITE-ProRule:PRU10076};
DE EC=3.4.19.3 {ECO:0000256|ARBA:ARBA00012915, ECO:0000256|PROSITE-ProRule:PRU10076};
DE Flags: Fragment;
GN ORFNames=AS27_02360 {ECO:0000313|EMBL:KFM07866.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM07866.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM07866.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM07866.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline. {ECO:0000256|ARBA:ARBA00002280}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal pyroglutamyl group from a
CC polypeptide, the second amino acid generally not being Pro.;
CC EC=3.4.19.3; Evidence={ECO:0000256|ARBA:ARBA00001770,
CC ECO:0000256|PROSITE-ProRule:PRU10076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
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DR EMBL; KL226068; KFM07866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R312; -.
DR STRING; 9233.A0A087R312; -.
DR MEROPS; C15.010; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00501; Peptidase_C15; 1.
DR Gene3D; 3.40.630.20; Peptidase C15, pyroglutamyl peptidase I-like; 1.
DR InterPro; IPR000816; Peptidase_C15.
DR InterPro; IPR016125; Peptidase_C15-like.
DR InterPro; IPR036440; Peptidase_C15-like_sf.
DR InterPro; IPR033694; PGPEP1_Cys_AS.
DR InterPro; IPR033693; PGPEP1_Glu_AS.
DR PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR PANTHER; PTHR23402:SF16; PYROGLUTAMYL-PEPTIDASE 1; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR PRINTS; PR00706; PYROGLUPTASE.
DR SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 1.
DR PROSITE; PS01334; PYRASE_CYS; 1.
DR PROSITE; PS01333; PYRASE_GLU; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 83
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10076"
FT ACT_SITE 147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10077"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM07866.1"
FT NON_TER 192
FT /evidence="ECO:0000313|EMBL:KFM07866.1"
SQ SEQUENCE 192 AA; 21101 MW; 671B105267C63EDC CRC64;
HHCGFTSLPG FGPFGEHAVN ASWIAVQELE KLGLRDDVDL HVYEVPVEYQ TVQRLIPALW
KKHSPQLVVH VGVSGMATTV TLEKCGHNVG YKGLDNCRFC PGSQCCVEGG PECIDSIIDM
DTVCKRVSAL GLDVTVTISK DAGRYLCDFT YYTSLYQSRG RSAFVHVPPL GKPYTAEQLG
RALQAIIEEM LD
//
