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Database: UniProt
Entry: G5C1L0_HETGA
LinkDB: G5C1L0_HETGA
Original site: G5C1L0_HETGA 
ID   G5C1L0_HETGA            Unreviewed;        99 AA.
AC   G5C1L0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520, ECO:0000256|RuleBase:RU000553};
DE            EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520, ECO:0000256|RuleBase:RU000553};
GN   ORFNames=GW7_01442 {ECO:0000313|EMBL:EHB15421.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB15421.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB15421.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
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         ECO:0000256|RuleBase:RU000553};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000256|RuleBase:RU004168}.
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DR   EMBL; JH172853; EHB15421.1; -; Genomic_DNA.
DR   RefSeq; XP_004837231.1; XM_004837174.2.
DR   RefSeq; XP_004837232.1; XM_004837175.2.
DR   RefSeq; XP_004837233.1; XM_004837176.2.
DR   RefSeq; XP_012922636.1; XM_013067182.1.
DR   AlphaFoldDB; G5C1L0; -.
DR   STRING; 10181.G5C1L0; -.
DR   Ensembl; ENSHGLT00100059274; ENSHGLP00100054060; ENSHGLG00100016768.
DR   GeneID; 101720710; -.
DR   CTD; 97; -.
DR   eggNOG; KOG3360; Eukaryota.
DR   InParanoid; G5C1L0; -.
DR   OrthoDB; 126107at2759; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
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; PTHR10029; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR10029:SF21; ACYLPHOSPHATASE-1; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 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   ECO:0000256|RuleBase:RU000553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813}.
FT   DOMAIN          9..99
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   99 AA;  11248 MW;  81DDFEA3F078FED2 CRC64;
     MAEGDSLVSV DYEVFGKVQG VFFRKYTQAE GKKLGLVGWV RNTDRGTVQG QLQGPTSKVR
     HMQEWLETKG SPKSHIERAN FNNEKAILKL DYSDFQIVK
//
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