ID K3YSU9_SETIT Unreviewed; 416 AA.
AC K3YSU9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00012568};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL31903, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EnsemblPlants:KQL31903, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL31903,
RC ECO:0000313|Proteomes:UP000004995};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EnsemblPlants:KQL31903}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL31903};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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 EMBL; AGNK02000585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K3YSU9; -.
DR MEROPS; M17.002; -.
DR EnsemblPlants; KQL31903; KQL31903; SETIT_016718mg.
DR Gramene; KQL31903; KQL31903; SETIT_016718mg.
DR HOGENOM; CLU_013734_5_2_1; -.
DR Proteomes; UP000004995; Chromosome I.
DR ExpressionAtlas; K3YSU9; baseline.
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; 1.
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; 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.
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:UP000004995}.
FT DOMAIN 107..240
FT /note="Peptidase M17 leucyl aminopeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02789"
FT DOMAIN 277..410
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00883"
SQ SEQUENCE 416 AA; 42991 MW; 73515DD656BC9342 CRC64;
MATAASTSAA AAVLASRLLR RSPRLLRRLS LSRAAPAALS SSSRPLAPLA RQPLGHRARM
GHTAAAAAAA GPALGLTKPN AVEPPQITFS AKDFEFSEWK GDILAVAVTE KDLSKDSDSK
FENAVLKKLD SQLGGLLSEA AAEEDFTGKA GQSVVLRVAG QGFKRVGLIG LGQNAPSTAA
ACRGLGESVA SVAKAAQASS AAIVFASPSG IQEEFKLTAA AAIASGTVLG SYEDSRYKSE
SKKVHLKQVD IIGLGSGPEV DQKLKYANDL SSGVIFGREL VNSPANVLTP AVLAEEASKI
ASTYSDVFTA TILDEEKCKE LKMGSYLAVA AASANPPHFI HLCYKPTDGN VKRKLAIVGK
GLTFDSGGYN IKTGPGCSIE LMKFDMGGSA AVFGAAKALG QIKPPGVEVL QLQILI
//
