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ADAL_DROME
ID   ADAL_DROME              Reviewed;         337 AA.
AC   Q9VHH7; A8E767;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Adenosine deaminase-like protein;
DE            EC=3.5.4.-;
GN   Name=Ada; ORFNames=CG11994;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA   Celniker S.E.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of the free cytosolic methylated
CC       adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol
CC       monophosphate (IMP) and methylamine. Is required for the catabolism of
CC       cytosolic N6-mAMP, which is derived from the degradation of mRNA
CC       containing N6-methylated adenine (m6A). {ECO:0000250|UniProtKB:Q6DHV7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine;
CC         Xref=Rhea:RHEA:16001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:59338, ChEBI:CHEBI:144842;
CC         Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16002;
CC         Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q6DHV7};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6DHV7}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
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DR   EMBL; AE014297; AAF54337.1; -; Genomic_DNA.
DR   EMBL; BT031009; ABV82391.1; -; mRNA.
DR   RefSeq; NP_649866.1; NM_141609.3.
DR   AlphaFoldDB; Q9VHH7; -.
DR   SMR; Q9VHH7; -.
DR   STRING; 7227.FBpp0081451; -.
DR   PaxDb; Q9VHH7; -.
DR   PRIDE; Q9VHH7; -.
DR   DNASU; 41092; -.
DR   EnsemblMetazoa; FBtr0081971; FBpp0081451; FBgn0037661.
DR   GeneID; 41092; -.
DR   KEGG; dme:Dmel_CG11994; -.
DR   CTD; 100; -.
DR   FlyBase; FBgn0037661; Ada.
DR   VEuPathDB; VectorBase:FBgn0037661; -.
DR   eggNOG; KOG1097; Eukaryota.
DR   GeneTree; ENSGT00950000183113; -.
DR   HOGENOM; CLU_039228_3_0_1; -.
DR   InParanoid; Q9VHH7; -.
DR   OMA; RPQFKPY; -.
DR   OrthoDB; 981145at2759; -.
DR   PhylomeDB; Q9VHH7; -.
DR   Reactome; R-DME-2161541; Abacavir metabolism.
DR   Reactome; R-DME-74217; Purine salvage.
DR   BioGRID-ORCS; 41092; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 41092; -.
DR   PRO; PR:Q9VHH7; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0037661; Expressed in saliva-secreting gland and 23 other tissues.
DR   Genevisible; Q9VHH7; DM.
DR   GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0062154; F:N6-mAMP deaminase activity; IEA:RHEA.
DR   GO; GO:0006154; P:adenosine catabolic process; IBA:GO_Central.
DR   GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11409; PTHR11409; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT   CHAIN           1..337
FT                   /note="Adenosine deaminase-like protein"
FT                   /id="PRO_0000285094"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P03958"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         16
FT                   /ligand="N(6)-methyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144842"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         18
FT                   /ligand="N(6)-methyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144842"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         66
FT                   /ligand="N(6)-methyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144842"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         98..101
FT                   /ligand="N(6)-methyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144842"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         171
FT                   /ligand="N(6)-methyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144842"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         201
FT                   /ligand="N(6)-methyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144842"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         276
FT                   /ligand="N(6)-methyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144842"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   BINDING         277
FT                   /ligand="N(6)-methyl-AMP"
FT                   /ligand_id="ChEBI:CHEBI:144842"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT   SITE            221
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03958"
SQ   SEQUENCE   337 AA;  37576 MW;  72FB9041DBE857C6 CRC64;
     MEQFLKGLPK VELHAHLNGS LGIKSLCDLG ERLYGTSCKD FLKLCAHFSR FEKDMDACFE
     KFAFVHELTS TREGLRFATE LAIRDFAEDN VQYVEMRTTP KANENYSRRD YLQIVIDAIK
     AASETYPEIT VKLLPSINRA EPVDVAEETV SLAVELARAH PNLILGIDLS GNPGKGRFSD
     FAPILAQARD KGLKLAIHCA EIENPSEVKE MLHFGMSRCG HGTFLTPEDI GQLKQRNIAI
     ECCLTSNVKS GTVPSLEEHH LKRIMEADAP KVICTDDSGV FDTTLTKEFL IAAETFGLTR
     EQCIDLTLEA VHHSFASEQE QIQMADRVGN YADILVK
 
 
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