ID A0A0E0MLZ2_ORYPU Unreviewed; 453 AA.
AC A0A0E0MLZ2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00012568};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC12G09460.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC12G09460.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC12G09460.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- SUBUNIT: Homohexamer (dimer of homotrimers).
CC {ECO:0000256|ARBA:ARBA00011867}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR AlphaFoldDB; A0A0E0MLZ2; -.
DR STRING; 4537.A0A0E0MLZ2; -.
DR EnsemblPlants; OPUNC12G09460.1; OPUNC12G09460.1; OPUNC12G09460.
DR Gramene; OPUNC12G09460.1; OPUNC12G09460.1; OPUNC12G09460.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_5_2_1; -.
DR OMA; HGFKRVC; -.
DR Proteomes; UP000026962; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 3.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 2.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT DOMAIN 62..188
FT /note="Peptidase M17 leucyl aminopeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02789"
FT DOMAIN 224..285
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00883"
FT DOMAIN 329..445
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00883"
SQ SEQUENCE 453 AA; 47714 MW; 8D6A27B0182ECD1A CRC64;
MEGHTAAAAA PTLGLTMPNV VDPPQVAFAV KDVDLTEWEG DILAVLVTEN NLSTATSSSR
FTNAAALAKL DGELGGLLSE ASAEEDFTGR AGQSVALRLP TAPGRHGFKR VCLIGVGNNT
PSSAAAYRSL GETVAAAAKS AQARTAAVAL AFPPPDWIHQ EDHRLNAAAA VASGLVLGLH
EDSRYKSESK KLHLKQVDFI GSDYGDELDT KLKYANHVSS AVIFAKELVN SPANVLTPAA
LAEEASKIAS TYSDVLTATI LDEEKCRELK MGSYLAVAAA SANPPHGGYN IKIGAVTTIE
LMKKDMGGSA AVFGAAKALG QIKPPGVEII DLATLTGYCR IALGPSIAGI LTPSDELDKE
VAAAYEASGE KFWRLPLEET YWEQMKSSVA DMLNTGSPLG GAITAGLFLK QFVDEKVQWM
HIDMAGPVWN YKKQQATGFG VSTLVEWVLI NSS
//
