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GS1_DROME
ID   GS1_DROME               Reviewed;         231 AA.
AC   Q94529; O02536; Q494L7; Q9VR01;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Probable pseudouridine-5'-phosphatase;
DE            EC=3.1.3.96;
DE   AltName: Full=GS1-like protein;
DE   AltName: Full=Pseudouridine-5'-monophosphatase;
DE            Short=5'-PsiMPase;
GN   Name=Gs1l; ORFNames=CG15441;
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 [GENOMIC DNA / MRNA].
RC   STRAIN=Canton-S; TISSUE=Embryo;
RX   PubMed=9055824; DOI=10.1016/s0378-1119(96)00656-7;
RA   Soehnge H., Huang X., Becker M., Conover D., Stern M.;
RT   "Cloning and sequencing of ribosomal protein L27a and a gene similar to
RT   human GS1 in Drosophila.";
RL   Gene 185:257-263(1997).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dephosphorylates pseudouridine 5'-phosphate, a potential
CC       intermediate in rRNA degradation. {ECO:0000250|UniProtKB:Q08623}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + psi-UMP = phosphate + pseudouridine;
CC         Xref=Rhea:RHEA:10944, ChEBI:CHEBI:15377, ChEBI:CHEBI:17802,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58380; EC=3.1.3.96;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC47471.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAC47474.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U66355; AAC47473.1; -; Genomic_DNA.
DR   EMBL; U66355; AAC47474.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U66356; AAC47470.1; -; mRNA.
DR   EMBL; U66356; AAC47471.1; ALT_INIT; mRNA.
DR   EMBL; AE014134; AAF51007.1; -; Genomic_DNA.
DR   EMBL; BT023759; AAZ41767.1; -; mRNA.
DR   PIR; JC6201; JC6201.
DR   RefSeq; NP_477228.1; NM_057880.5.
DR   AlphaFoldDB; Q94529; -.
DR   SMR; Q94529; -.
DR   STRING; 7227.FBpp0077143; -.
DR   PaxDb; Q94529; -.
DR   PRIDE; Q94529; -.
DR   DNASU; 33653; -.
DR   EnsemblMetazoa; FBtr0077453; FBpp0077143; FBgn0019982.
DR   GeneID; 33653; -.
DR   KEGG; dme:Dmel_CG15441; -.
DR   CTD; 33653; -.
DR   FlyBase; FBgn0019982; Gs1l.
DR   VEuPathDB; VectorBase:FBgn0019982; -.
DR   eggNOG; KOG2914; Eukaryota.
DR   GeneTree; ENSGT00390000014753; -.
DR   HOGENOM; CLU_045011_13_0_1; -.
DR   InParanoid; Q94529; -.
DR   OMA; DSERVYT; -.
DR   PhylomeDB; Q94529; -.
DR   Reactome; R-DME-73614; Pyrimidine salvage.
DR   BioGRID-ORCS; 33653; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33653; -.
DR   PRO; PR:Q94529; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0019982; Expressed in adult Malpighian tubule (Drosophila) and 25 other tissues.
DR   ExpressionAtlas; Q94529; baseline and differential.
DR   Genevisible; Q94529; DM.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:1990738; F:pseudouridine 5'-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042060; P:wound healing; HMP:FlyBase.
DR   CDD; cd07529; HAD_AtGPP-like; 1.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR045228; Gpp1/Gpp2-like.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   Pfam; PF13419; HAD_2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..231
FT                   /note="Probable pseudouridine-5'-phosphatase"
FT                   /id="PRO_0000108069"
FT   ACT_SITE        15
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        17
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   VARIANT         176..177
FT                   /note="FE -> VQ (in strain: Canton-S)"
SQ   SEQUENCE   231 AA;  25785 MW;  3D4421C9665B69D4 CRC64;
     MANKVLRKVT HCVFDMDGLL LDTERLYTVA TEMILEPYGK TYPFEIKEQV MGLQTEPLAR
     FMVEHYELPM SWEEYARQQR ANTEILMRNA QLMPGAERLL RHLHANKVPF CLATSSGADM
     VELKTAQHRE LFSLFNHKVC GSSDKEVVNG KPAPDIFLVA AGRFGVPPKP SDCLVFEDSP
     NGVTAANSAG MQVVMVPDPR LSQEKTSHAT QVLASLADFK PEQFGLPAFT D
 
 
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