GenomeNet

Database: UniProt
Entry: J3ND54_ORYBR
LinkDB: J3ND54_ORYBR
Original site: J3ND54_ORYBR 
ID   J3ND54_ORYBR            Unreviewed;       552 AA.
AC   J3ND54;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
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:OB12G19120.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB12G19120.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB12G19120.1};
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:OB12G19120.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; J3ND54; -.
DR   STRING; 4533.J3ND54; -.
DR   MEROPS; M17.A03; -.
DR   EnsemblPlants; OB12G19120.1; OB12G19120.1; OB12G19120.
DR   Gramene; OB12G19120.1; OB12G19120.1; OB12G19120.
DR   eggNOG; KOG2597; Eukaryota.
DR   HOGENOM; CLU_013734_5_1_1; -.
DR   OMA; HGFKRVC; -.
DR   Proteomes; UP000006038; 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   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          404..411
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   552 AA;  57016 MW;  078C5BFD05F2A8E0 CRC64;
     MGGHAVAVDV AAAATPSLGL TVPNAAADNP LQVTFAAKDM ELTEWEGDIL AVLVPESGVS
     GATPPSSTFA NAAALARLDG QLGGLLSEAS AEEDFSGKAG QLVALRLPAA TGSHGFKRVC
     LVGVGKVDAP RSAAAAAACR SAGESVAAAA RAAQAHSAAV ALGSPKPGWG HGEDFRPEAA
     AAVASGIIVL GLHEDSRYKS ESKKVHLERV DFIGFGAGDE VESKLQYAND VSSGVILCKE
     LVNSPANVLT PAALAEEASK IASTYSDVLT ATILDQGKCR ELKMGSYLAV AAASANPPHF
     IHLCYKPPGG NVKRKLAIVG KGLTFDSGGY NIKIGAATNI ELMKKDMGGA AAVFGAAKAL
     GQIKPPGVEV HFISAACENM ISGTGMRPGD IVTASNGKTI EVDNTDAEGR LTLADALIYA
     CKQGVDKILD LATLTGYCRI ALGPSIAGVL TPSDELAKEV AAAYEASGEK FWRLPMEESY
     WEQMKSSVAD MINTGSPLGG AITAALFLKQ FVDEEVQWMH IDMAGPVWNY KKKEATGFGV
     STLVEWVLMN SS
//
DBGET integrated database retrieval system