ID A0A0D9XJQ7_9ORYZ Unreviewed; 723 AA.
AC A0A0D9XJQ7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00012917};
DE EC=3.4.19.1 {ECO:0000256|ARBA:ARBA00012917};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR10G07230.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR10G07230.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR10G07230.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR10G07230.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC terminus of a polypeptide.; EC=3.4.19.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000721};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; A0A0D9XJQ7; -.
DR STRING; 77586.A0A0D9XJQ7; -.
DR EnsemblPlants; LPERR10G07230.1; LPERR10G07230.1; LPERR10G07230.
DR Gramene; LPERR10G07230.1; LPERR10G07230.1; LPERR10G07230.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_014230_1_1_1; -.
DR Proteomes; UP000032180; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR045550; AARE_N.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF30; ACYLAMINO-ACID-RELEASING ENZYME 1; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF19283; APEH_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180}.
FT DOMAIN 25..299
FT /note="Acylamino-acid-releasing enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19283"
FT DOMAIN 537..688
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 178..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 79258 MW; 017756077AFC2A3C CRC64;
MTTAQASEAA TEKELPVGMD ASMLDEYASQ SKLLQEFVKI PTIGKAWIFN SKNENTSRVM
VSVGQADLLA NKRKRFLLNS HISKNASNNS VDFQWSPFPI EMSGVSAIVP SPSGKKLLLV
RNSEDDSPTK LEVWGPCQLE NEIHIAQSVH GSVYADEWFE GISWNQEETL VAYVAEEPPQ
PKPEFNDSGY KKADSSEKDC KSWKGKGDWE ETWGETYSKK RIPALFVVNI SSGEVRAVKG
IPRTLSVGQV IWAPSSSYSL VFVAWSSDNG FQKTPGKLGI KYCYNRPCAL YAVPDPFMEE
AQKPSINVSK VDTAPTIKLT SDLNSAFFPR FSLGHTSQLW GLLLYSPDGK YLVFISAKSA
VDSGAHNATN SMHKIDWPAD GKLKDLSVAD VVPIVMCPQD GCFPGLYCSG ILRNPWLSDG
QTMILSSVWG SKEVILSVNV VSCEVSRVTP QDSDYSWNIL ALDKDNILAV SSSLITVPQM
FYGSEVCPTG KSSQWQWQEI STPFLNPSDK ISAILTDHKF SILKVPINNA SDKLTDGSLG
FGEEALQSLP GNIGSQDVND VLTALDFVIK KGLIDASKVA VVGGSHGGFL TTHLIGQAPG
TFLAAAARNP VCNLSLMVGT TDIPDWCFVE IYGKEGKNYY SESPSVDSIC QFLQKSPISH
ISKVITPTIF LLGAQDLRVP VSNGLQCICN NRLNQPSFPL RRPQSDFESF LNIGVWFKKH
LSR
//