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Database: UniProt
Entry: A0A1S3CGZ8_CUCME
LinkDB: A0A1S3CGZ8_CUCME
Original site: A0A1S3CGZ8_CUCME 
ID   A0A1S3CGZ8_CUCME        Unreviewed;       200 AA.
AC   A0A1S3CGZ8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE            EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN   Name=LOC103500820 {ECO:0000313|RefSeq:XP_008462471.1};
GN   Synonyms=103500820 {ECO:0000313|EnsemblPlants:MELO3C024465.2.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008462471.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|EnsemblPlants:MELO3C024465.2.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_008462471.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000256|RuleBase:RU004168}.
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DR   RefSeq; XP_008462471.1; XM_008464249.2.
DR   EnsemblPlants; MELO3C024465.2.1; MELO3C024465.2.1; MELO3C024465.2.
DR   GeneID; 103500820; -.
DR   Gramene; MELO3C024465.2.1; MELO3C024465.2.1; MELO3C024465.2.
DR   KEGG; cmo:103500820; -.
DR   eggNOG; KOG3360; Eukaryota.
DR   InParanoid; A0A1S3CGZ8; -.
DR   OrthoDB; 620705at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   Proteomes; UP000596662; Unplaced.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   PANTHER; PTHR47268; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW   Reference proteome {ECO:0000313|Proteomes:UP000089565}.
FT   DOMAIN          112..200
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   200 AA;  22328 MW;  74EFC5AA36B7DF16 CRC64;
     MASASSSSSA AFAVGPLIRN RSTRFLPCRN LHHKWSFKDA GSHSRLSLFN YYNSSPLLPS
     LPIRHRLLLP HPPLHLLLRS RSPSFRYPLP LMASTVPHQA GPETPQSNPT KTVRVVIKGR
     VQGVFYRDWT VENATELGLK GWVRNRRDGS VEALFSGRPE SVTEMEQRCR RGPPAAMVTG
     FQVFPSSDDP GPGFERLRTA
//
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