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Database: UniProt
Entry: M5WBQ5_PRUPE
LinkDB: M5WBQ5_PRUPE
Original site: M5WBQ5_PRUPE 
ID   M5WBQ5_PRUPE            Unreviewed;       488 AA.
AC   M5WBQ5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Aspartyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PRUPE_5G153700 {ECO:0000313|EMBL:ONI08023.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI08023.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI08023.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CM007655; ONI08023.1; -; Genomic_DNA.
DR   RefSeq; XP_007209960.1; XM_007209898.1.
DR   AlphaFoldDB; M5WBQ5; -.
DR   STRING; 3760.M5WBQ5; -.
DR   MEROPS; M18.A01; -.
DR   EnsemblPlants; ONI08023; ONI08023; PRUPE_5G153700.
DR   GeneID; 18776372; -.
DR   Gramene; ONI08023; ONI08023; PRUPE_5G153700.
DR   KEGG; pper:18776372; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   HOGENOM; CLU_019532_2_0_1; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000006882; Chromosome g5.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF16; ASPARTYL AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   488 AA;  53848 MW;  63B1B8CF3DB029ED CRC64;
     MAKQEPNCEG SSVVSDLINF LNASPTAFHA VDEAKKRLQN AGYEPVSERE DWKLEAGKKY
     FFTRNYSTIV AFAIGKKYVA GNGFHIVGAH TDSPCLKLKP VSKVVKGGYL EVGVQTYGGG
     LWHTWFDRDL TIAGRVIVRE EKDGSVSYSH KLVRIEEPIM RIPTLAIHLD RDVRDAFKVN
     TQSHLLPVLA TSIKAELNKV VAENGQADSD AQTHGKKSNE RNTSNNSKHH SLLLQLLADQ
     LGCEPEHISD FELQACDTQP SVVAGATKEF IFSGRLDNLC MSFCSLKALI ESSESNLEDE
     TGVRLVALFD HEEVGSDSAQ GAGSPAMLNT LSRITNSFTA DSKLLEKAIQ RSFLVSADMA
     HALHPNYMDK HEDNHQPKLH GGLVIKHNAN QRYATNAVTS LIFREIARNH NLPVQDFAVR
     NDMACGSTIG PILASGVGIR TVDVGAPQLS MHSIREMCAV DDVQYSYEHF KAFFQEFSHL
     DEKIKVDA
//
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