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RIH_DICDI
ID   RIH_DICDI               Reviewed;         340 AA.
AC   Q7KWM9; Q558T2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable ribonucleoside hydrolase {ECO:0000305};
DE            EC=3.2.2.1 {ECO:0000305};
DE            EC=3.2.2.8 {ECO:0000305};
GN   Name=iunH; ORFNames=DDB_G0272738;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond of purine
CC       and/or pyrimidine nucleosides into ribose and the base. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine D-ribonucleoside + H2O = a purine nucleobase + D-
CC         ribose; Xref=Rhea:RHEA:23344, ChEBI:CHEBI:15377, ChEBI:CHEBI:26386,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:142355; EC=3.2.2.1;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a pyrimidine ribonucleoside + H2O = a pyrimidine nucleobase +
CC         D-ribose; Xref=Rhea:RHEA:56816, ChEBI:CHEBI:15377, ChEBI:CHEBI:26432,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:141014; EC=3.2.2.8;
CC         Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P83851};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC   -!- SIMILARITY: Belongs to the IUNH family. {ECO:0000305}.
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DR   EMBL; AAFI02000008; EAL71006.1; -; Genomic_DNA.
DR   RefSeq; XP_644984.1; XM_639892.1.
DR   AlphaFoldDB; Q7KWM9; -.
DR   SMR; Q7KWM9; -.
DR   STRING; 44689.DDB0231227; -.
DR   PaxDb; Q7KWM9; -.
DR   EnsemblProtists; EAL71006; EAL71006; DDB_G0272738.
DR   GeneID; 8618661; -.
DR   KEGG; ddi:DDB_G0272738; -.
DR   dictyBase; DDB_G0272738; iunH.
DR   eggNOG; KOG2938; Eukaryota.
DR   HOGENOM; CLU_036838_2_0_1; -.
DR   InParanoid; Q7KWM9; -.
DR   OMA; HAPDIHG; -.
DR   PhylomeDB; Q7KWM9; -.
DR   UniPathway; UPA00606; -.
DR   PRO; PR:Q7KWM9; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; ISS:dictyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008477; F:purine nucleosidase activity; IBA:GO_Central.
DR   GO; GO:0050263; F:ribosylpyrimidine nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006152; P:purine nucleoside catabolic process; IBA:GO_Central.
DR   GO; GO:0008655; P:pyrimidine-containing compound salvage; ISS:dictyBase.
DR   GO; GO:0006218; P:uridine catabolic process; ISS:dictyBase.
DR   Gene3D; 3.90.245.10; -; 1.
DR   InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR   InterPro; IPR023186; IUNH.
DR   InterPro; IPR036452; Ribo_hydro-like.
DR   PANTHER; PTHR12304; PTHR12304; 1.
DR   Pfam; PF01156; IU_nuc_hydro; 1.
DR   SUPFAM; SSF53590; SSF53590; 1.
PE   3: Inferred from homology;
KW   Calcium; Glycosidase; Hydrolase; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..340
FT                   /note="Probable ribonucleoside hydrolase"
FT                   /id="PRO_0000328284"
FT   ACT_SITE        259
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q27546"
FT   BINDING         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  37993 MW;  2C8D6346C51C687A CRC64;
     MLNEELLPIW LDHDCGHDDA FAMLLAFHSK IFNILGISSV HGNQTVDKTT INALITLEII
     GKSNCGYEVV KGVRSPMCRP EQVCSEIHGE TGLDCPTAEL PKPTQLPITD RPAIQVMFEK
     ISKFYTDNQQ KQKVIIVATG SLTNVALLFA VYPQIKPMVE VSLLGGSINF GNISPAAEYN
     ILVDPEAAKV VFESGVKVIM VPLECSHKAL VNEKILERIS DIEKADGKQT QFIKIIKGLL
     LFFADNYKST FDFDHPPLHD PLAVAYLIDP TIFKCKLMRV DIETSSHLCL GRTVVDLFSM
     SKLQKNVHVC TDINVDKFWD LMINAIDNCY NHLYKSNILK
 
 
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