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MTG1_DROME
ID   MTG1_DROME              Reviewed;         323 AA.
AC   Q9VCU5; Q4V5C0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Mitochondrial ribosome-associated GTPase 1;
DE   AltName: Full=Mitochondrial GTPase 1 {ECO:0000250|UniProtKB:Q9BT17};
DE   Flags: Precursor;
GN   ORFNames=CG17141;
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] {ECO:0000312|EMBL:AAF56060.2}
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   [2] {ECO:0000312|EMBL:AAF56060.2}
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   [3] {ECO:0000312|EMBL:AAY55152.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA   Park S., Wan K., Yu C., Celniker S.E.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-320, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo {ECO:0000269|PubMed:18327897};
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Plays a role in the regulation of the mitochondrial ribosome
CC       assembly and of translational activity (By similarity). Displays
CC       mitochondrial GTPase activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BT17}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9BT17}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9BT17}; Matrix side
CC       {ECO:0000250|UniProtKB:Q9BT17}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; AE014297; AAF56060.2; -; Genomic_DNA.
DR   EMBL; BT022736; AAY55152.1; -; mRNA.
DR   RefSeq; NP_651094.2; NM_142837.4.
DR   AlphaFoldDB; Q9VCU5; -.
DR   SMR; Q9VCU5; -.
DR   BioGRID; 67646; 2.
DR   IntAct; Q9VCU5; 4.
DR   STRING; 7227.FBpp0083715; -.
DR   iPTMnet; Q9VCU5; -.
DR   PaxDb; Q9VCU5; -.
DR   PRIDE; Q9VCU5; -.
DR   DNASU; 42697; -.
DR   EnsemblMetazoa; FBtr0084322; FBpp0083715; FBgn0039020.
DR   GeneID; 42697; -.
DR   KEGG; dme:Dmel_CG17141; -.
DR   UCSC; CG17141-RA; d. melanogaster.
DR   FlyBase; FBgn0039020; CG17141.
DR   VEuPathDB; VectorBase:FBgn0039020; -.
DR   eggNOG; KOG2485; Eukaryota.
DR   GeneTree; ENSGT00500000044923; -.
DR   HOGENOM; CLU_011106_0_2_1; -.
DR   InParanoid; Q9VCU5; -.
DR   OMA; GVLWPKF; -.
DR   OrthoDB; 583045at2759; -.
DR   PhylomeDB; Q9VCU5; -.
DR   BioGRID-ORCS; 42697; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 42697; -.
DR   PRO; PR:Q9VCU5; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0039020; Expressed in antenna and 14 other tissues.
DR   Genevisible; Q9VCU5; DM.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR016478; GTPase_MTG1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PIRSF; PIRSF006230; MG442; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   1: Evidence at protein level;
KW   GTP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT17, ECO:0000255"
FT   CHAIN           ?..323
FT                   /note="Mitochondrial ribosome-associated GTPase 1"
FT                   /id="PRO_0000409875"
FT   DOMAIN          31..208
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   BINDING         78..81
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O31743"
FT   BINDING         152..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O31743"
FT   BINDING         204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O31743"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         320
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   323 AA;  36545 MW;  A3E10B70B6A97DD4 CRC64;
     MAAQLNPFRN AFRLPSKQRI NWFPGHMTKG MRQIQQKLRN VDCIVEIHDA RIPLAGRNSQ
     FFDTITGSGV KPHILVLNKV DLLGAKQQKS VLQQLRRQQP ELQHILFTNC KDQRNNGVLD
     ILPLATRLVS ESSRFNRTQA AEHNLMIIGV PNVGKSSVIN VLRNVHLKKK SAARVGAEAG
     ITRSVGERIK IQENPPVYMI DTPGILQPSI KDDEMGMKLA LVGCLPDHIV GEDLIADYLL
     YWLNSHRKYD YVEMLKLSSG PSDDISAVLA EYAHREELFH KVKQYDGRVE VMTNLLAAAR
     KFIHFFRSGQ LGHMNLDEPS GFR
 
 
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