ID   A0A1D6HN63_MAIZE        Unreviewed;       603 AA.
AC   A0A1D6HN63;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Leucine aminopeptidase 2 chloroplastic {ECO:0000313|EMBL:AQK75740.1};
GN   ORFNames=ZEAMMB73_Zm00001d018370 {ECO:0000313|EMBL:AQK75740.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK75740.1};
RN   [1] {ECO:0000313|EMBL:AQK75740.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK75740.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CM000781; AQK75740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6HN63; -.
DR   SMR; A0A1D6HN63; -.
DR   IntAct; A0A1D6HN63; 11.
DR   STRING; 4577.A0A1D6HN63; -.
DR   InParanoid; A0A1D6HN63; -.
DR   OMA; MPLWKYF; -.
DR   ExpressionAtlas; A0A1D6HN63; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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   ECO:0000313|EMBL:AQK75740.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          446..453
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   603 AA;  62729 MW;  1607817DEF44763D CRC64;
     MATAAASTTT SAAVLAFRLL RRLPRRLSVS RAPPAALASS SSSSSRRLPS LARHPLGHRT
     RMGHTAAAAA AAAEPALGLT KPNAVEPPQV TFSAKDIEFS EWKGDILAVA VTEKDLSKDA
     DSKFENAVLK KLDGQLGGLL SEAAAEEDFT GKTGQSVVLR LAGQGFKRVG LIGLGQSAPS
     TAAASRGLGE SVASVAKAAQ ASSAAIVLAS PSGIQEEFKL TAAAAVASGT VLGLYEDSRY
     KSESKKVHLK QVDIIGLGSG AEVDQKLKYA NDLSSGVIFG RELVNSPANV LTPAVLAEEA
     SKIASTYSDV FTATVLDVEK CKELKMGSYL GVAAASANPP HFIHLCYKPT DGNVKRKLAI
     VGKGLTFDSG GYNIKTGPGC SIELMKFDMG GSAAVFGAAK ALGQIKPPGV EVHFIVAACE
     NMISGTGMRP GDIVTASNGK TIEVNNTDAE GRLTLADALV YACNQGVEKV MKLHLEIIDL
     ATLTGACVVA LGPSIAGIFT PSDELAKEVA AASEVSGEKF WRLPLEESYW ESMKSGVADM
     VNTGGRQGGS ITAALFLKQF VDDKVQWMHI DMAGPVWSDK KRAATGFGVS TLVEWVLNNS
     SSS
//