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SLIMP_DROME
ID   SLIMP_DROME             Reviewed;         464 AA.
AC   Q95T19;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Serine--tRNA synthetase-like protein Slimp {ECO:0000305};
DE   AltName: Full=Seryl-tRNA synthetase-like insect mitochondrial protein {ECO:0000312|FlyBase:FBgn0051133};
DE   Flags: Precursor;
GN   Name=Slimp {ECO:0000312|FlyBase:FBgn0051133};
GN   ORFNames=CG31133 {ECO:0000312|FlyBase:FBgn0051133};
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 {ECO:0000312|EMBL:AAL25413.1};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAL25413.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAL25413.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAL25413.1};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=20870726; DOI=10.1074/jbc.m110.167486;
RA   Guitart T., Leon Bernardo T., Sagales J., Stratmann T., Bernues J.,
RA   Ribas de Pouplana L.;
RT   "New aminoacyl-tRNA synthetase-like protein in insecta with an essential
RT   mitochondrial function.";
RL   J. Biol. Chem. 285:38157-38166(2010).
CC   -!- FUNCTION: Essential protein which may play a role in mitochondrial
CC       morphogenesis and function. Has transfer RNA (tRNA)-binding activity
CC       and can bind tRNA(Ser) but does not have serine--tRNA ligase activity
CC       and does not bind ATP. {ECO:0000269|PubMed:20870726}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20870726}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from late embryogenesis with expression
CC       continuing in larva, pupa and adult (at protein level).
CC       {ECO:0000269|PubMed:20870726}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
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DR   EMBL; AE014297; AAN13983.1; -; Genomic_DNA.
DR   EMBL; AY060374; AAL25413.1; -; mRNA.
DR   RefSeq; NP_732958.1; NM_170125.3.
DR   AlphaFoldDB; Q95T19; -.
DR   SMR; Q95T19; -.
DR   IntAct; Q95T19; 1.
DR   STRING; 7227.FBpp0083968; -.
DR   PaxDb; Q95T19; -.
DR   PRIDE; Q95T19; -.
DR   DNASU; 318604; -.
DR   EnsemblMetazoa; FBtr0084583; FBpp0083968; FBgn0051133.
DR   GeneID; 318604; -.
DR   KEGG; dme:Dmel_CG31133; -.
DR   UCSC; CG31133-RA; d. melanogaster.
DR   CTD; 318604; -.
DR   FlyBase; FBgn0051133; Slimp.
DR   VEuPathDB; VectorBase:FBgn0051133; -.
DR   eggNOG; KOG2509; Eukaryota.
DR   GeneTree; ENSGT00940000153792; -.
DR   HOGENOM; CLU_031998_0_0_1; -.
DR   InParanoid; Q95T19; -.
DR   OMA; YQTHHEQ; -.
DR   OrthoDB; 1558033at2759; -.
DR   PhylomeDB; Q95T19; -.
DR   BioGRID-ORCS; 318604; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 318604; -.
DR   PRO; PR:Q95T19; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0051133; Expressed in anterior ectoderm anlage (Drosophila) and 33 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR   GO; GO:0140715; C:serine-tRNA ligase complex; IPI:FlyBase.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IDA:FlyBase.
DR   GO; GO:0070158; P:mitochondrial seryl-tRNA aminoacylation; IDA:FlyBase.
DR   GO; GO:0032543; P:mitochondrial translation; IDA:FlyBase.
DR   GO; GO:1903632; P:positive regulation of aminoacyl-tRNA ligase activity; IDA:FlyBase.
DR   Gene3D; 1.10.287.40; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR   InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR   InterPro; IPR042103; SerRS_1_N_sf.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR11778; PTHR11778; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
PE   1: Evidence at protein level;
KW   Mitochondrion; Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305|PubMed:20870726"
FT   CHAIN           ?..464
FT                   /note="Serine--tRNA synthetase-like protein Slimp"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436150"
SQ   SEQUENCE   464 AA;  52916 MW;  BA25758EED8CB40F CRC64;
     MLSLRSVLKH CLSAKKTCSR NISALYITGD KANENYVTLQ PYMDFNKTFG ERQFLEQSIS
     SRGLDIRLET VLSKYEKYKT HHAQLSKVAE ERERVTKRLK ELTKSGSSAV QLEELKEHGK
     SLRNELKALK QTLYPIEDDF IHDYLHLPNL LHVQCPVGGE EKLLYRHGIP KSENKTTSHL
     ARQELVHFVD NNRYYLMEQA ALFDVNAMQS LARYFVNHGH FIQTANPDFV RCVLLEANAT
     PLSDYHLVQE EHLQNKINTA YLTGGASFES YLGAMTKLCV YPSVLPLRYV CCGRSYNRAE
     ADLYGPIPSL YTATQTNAVQ IFVATQTDNE ADSQLEHILN LATDFYKALD IPFRISYATA
     ADLTPAESIR AVIEVYAPSL QRYVCVGRIS NYGDFVSKRI LFSTRREKHY DFLHMVGGPV
     LYTSRLIAAL VEHGVRLEDC KLLGSISQKP VHQQDLQQFK DLFT
 
 
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