GenomeNet

Database: UniProt
Entry: E9HV92_DAPPU
LinkDB: E9HV92_DAPPU
Original site: E9HV92_DAPPU 
ID   E9HV92_DAPPU            Unreviewed;       443 AA.
AC   E9HV92;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFX64342.1};
GN   ORFNames=DAPPUDRAFT_334303 {ECO:0000313|EMBL:EFX64342.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX64342.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX64342.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
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DR   EMBL; GL732844; EFX64342.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9HV92; -.
DR   STRING; 6669.E9HV92; -.
DR   EnsemblMetazoa; EFX64342; EFX64342; DAPPUDRAFT_334303.
DR   KEGG; dpx:DAPPUDRAFT_334303; -.
DR   eggNOG; KOG0807; Eukaryota.
DR   eggNOG; KOG3379; Eukaryota.
DR   HOGENOM; CLU_030130_12_1_1; -.
DR   InParanoid; E9HV92; -.
DR   OMA; GWHNKKR; -.
DR   PhylomeDB; E9HV92; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IBA:GO_Central.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IBA:GO_Central.
DR   CDD; cd01275; FHIT; 1.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR   Gene3D; 3.30.428.10; HIT-like; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR039383; FHIT.
DR   InterPro; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   InterPro; IPR001110; UPF0012_CS.
DR   PANTHER; PTHR23088:SF27; DEAMINATED GLUTATHIONE AMIDASE; 1.
DR   PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF01230; HIT; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
DR   PROSITE; PS01227; UPF0012; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000305}.
FT   DOMAIN          8..257
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   DOMAIN          296..404
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   MOTIF           389..393
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        391
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         393
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   SITE            409
FT                   /note="Important for induction of apoptosis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ   SEQUENCE   443 AA;  49385 MW;  8ABE93AD0820B766 CRC64;
     MTDSSKPSLI AIVQMTATSN KADNFAVTKE KIEEASSLGA KVVFLPEACD YIADSHAQSL
     ELAENMDGTL IKNYSELAVQ NRIWISIGGF HNKSSSIDKM FNTHVLINSD GQIAGRYDKT
     HLFDVEIPEK KIKLKESDYI EKGGSIASPV ESPVGKIGLG ICYDVRFPEF SLSLARMGAD
     IITYPSAFTV ATGLAHWESI LRARAIETQC FVVAAAQTGI HNSKRSSYGH AMVIDPWGTV
     IAQCREGTSL ALAAIDLEYL RKVRREMPVF THRRQDVYQL PTCGVLPVSP LPPDEATFNF
     GQVTIKGWAV FYQSRHSLAF VNRKCVVPGH VLVMPLKASR RIPDMQPDEL SDLFLTSQIV
     QRGMELFHGV SSSNVAVQDG PDAGQSIQHV HVHILPRRPK DFKENDQVYD ELNNHDKGPN
     VEWRQEEEMK REATELRLFF AKL
//
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