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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionSubName: Full=Zgc:110366 {ECO:0000313|Ensembl:ENSDARP00000015634};
MyHits logo
MyHits synonymsA8DZH9_DANRE , A8DZH9 , 03DF2D0D22F949A1
match map segment
ipat:ALDOKETO_REDUCTASE_3 ipat:ALDOKETO_REDUCTASE_2 ipfam:Aldo_ket_red  
Legends: 1, ACT_SITE Proton donor. {ECO:0000256|PIRSR:PIRSR000097-1}; 2, BINDING Substrate. {ECO:0000256|PIRSR:PIRSR000097-2}; 3, SITE Lowers pKa of active site Tyr. {ECO:0000256|PIRSR:PIRSR000097-3}; 4, ipat:ALDOKETO_REDUCTASE_3 [T]; 5, ipat:ALDOKETO_REDUCTASE_2 [T].
ID   A8DZH9_DANRE            Unreviewed;       289 AA.
AC   A8DZH9;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   10-MAY-2017, entry version 74.
DE   SubName: Full=Zgc:110366 {ECO:0000313|Ensembl:ENSDARP00000015634};
GN   ORFNames=zgc:110366 {ECO:0000313|Ensembl:ENSDARP00000015634,
GN   ECO:0000313|ZFIN:ZDB-GENE-050417-302};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000015634, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000015634, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000015634,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000015634}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000015634};
RG   Ensembl;
RL   Submitted (AUG-2013) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSDARP00000015634}.
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DR   EMBL; AL953893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001017779.2; NM_001017779.2.
DR   UniGene; Dr.89849; -.
DR   ProteinModelPortal; A8DZH9; -.
DR   STRING; 7955.ENSDARP00000015634; -.
DR   PaxDb; A8DZH9; -.
DR   PeptideAtlas; A8DZH9; -.
DR   Ensembl; ENSDART00000012119; ENSDARP00000015634; ENSDARG00000004167.
DR   GeneID; 550476; -.
DR   KEGG; dre:550476; -.
DR   ZFIN; ZDB-GENE-050417-302; zgc:110366.
DR   eggNOG; KOG1577; Eukaryota.
DR   eggNOG; COG0656; LUCA.
DR   GeneTree; ENSGT00850000132445; -.
DR   HOGENOM; HOG000250272; -.
DR   HOVERGEN; HBG000020; -.
DR   InParanoid; A8DZH9; -.
DR   TreeFam; TF315922; -.
DR   Proteomes; UP000000437; Chromosome 2.
DR   Bgee; ENSDARG00000004167; -.
DR   ExpressionAtlas; A8DZH9; baseline.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06660; Aldo_ket_red; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR020471; Aldo/keto_reductase.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   PANTHER; PTHR11732; PTHR11732; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:A8DZH9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT   DOMAIN       27    274       Aldo_ket_red. {ECO:0000259|Pfam:PF00248}.
FT   ACT_SITE     60     60       Proton donor.
FT                                {ECO:0000256|PIRSR:PIRSR000097-1}.
FT   BINDING     118    118       Substrate.
FT                                {ECO:0000256|PIRSR:PIRSR000097-2}.
FT   SITE         85     85       Lowers pKa of active site Tyr.
FT                                {ECO:0000256|PIRSR:PIRSR000097-3}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       244    259       ipat:ALDOKETO_REDUCTASE_3 [T]
FT   MYHIT       140    157       ipat:ALDOKETO_REDUCTASE_2 [T]
FT   MYHIT        27    274       ipfam:Aldo_ket_red [T]
SQ   SEQUENCE   289 AA;  32492 MW;  03DF2D0D22F949A1 CRC64;
     MVTKPTSCTA LSCPAVPLHN GLNIPILGLG TSHYGGYSHE AVLYALQECG IRHIDTAKRY
     GCEEALGKAV TESGVQREEL WITTKLWPGD YGYQSTKQAC RDSCARLGVD YLDLYLMHWP
     DSMVPGRSSQ EVRLETWRAL EELYDEGLCR AIGVSNFLIP HLNELKDCGG IVPHVNQVEF
     HPFQQPMKLV EHCRKENIVF EGYCPLAKGQ ALTHPHILEL AKKYGRSASQ ICIRWSIQNG
     VVTIPKSTKP DRIYENCQVF GFRLEDSEMA ALSTLHDGRH VSWDPTHVE
//