ID J3LHZ1_ORYBR Unreviewed; 529 AA.
AC J3LHZ1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0000259|PROSITE:PS00631};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB02G42580.1};
RN [1] {ECO:0000313|EnsemblPlants:OB02G42580.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB02G42580.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB02G42580.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
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; J3LHZ1; -.
DR STRING; 4533.J3LHZ1; -.
DR MEROPS; M17.A03; -.
DR EnsemblPlants; OB02G42580.1; OB02G42580.1; OB02G42580.
DR Gramene; OB02G42580.1; OB02G42580.1; OB02G42580.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_5_1_1; -.
DR OMA; HSFLMIA; -.
DR Proteomes; UP000006038; Chromosome 2.
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 CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
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; 1.
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.
DR PROSITE; PS00631; CYTOSOL_AP; 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:UP000006038}.
FT DOMAIN 381..388
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 529 AA; 55151 MW; BA85FADD37A71336 CRC64;
MTCGDPQLPV PPVSEVHESS VDLRVSFAAK DVEFSDWKGD VLAIAVTEKD LIKGSDSQFE
NAVLKKLDGQ LGGLLSEASA EEDFTGKAGQ SVVLRLPGQG FKRVGLIGLG QNAPSTTAAC
KGIGESIASV AKSVQASSAA IVFASGGGIQ EDFKLTAAAA IASGTVLGLH EDSRYKSESK
KVHLKQVDLI GFGSGPEVDK KLKYANDLSS GVIFGKELVN SPANVLTPAV LAEEASKIAS
EYSDVITATI LDVEKCKELK MGSYLAVAAA SANPPHFIHL CYKPPGGNAK RKLAIVGKGL
TFDSGGYNIK TGPGCSIELM KFDMGGSAAV FGAAKALGQI KPAGVEVHFI VAACENMISG
TGMRPGDIVT ASNGKTIEVN NTDAEGRLTL ADALVYACNQ GVDKIIDLAT LTGACVVALG
PSIAGIFTPS DELAKEVAAA SEVSGEKFWR LPLEESYWES MKSGVADMVN TGGRQGGSIT
AALFLKQFVD EKVQWMHIDM AGPVWNDKKR GATGFGVSTL VEWVLKNSS
//
