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
//