ID B4Q4F6_DROSI Unreviewed; 844 AA.
AC B4Q4F6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=GD21631 {ECO:0000313|EMBL:EDX05753.1};
GN Name=Dsim\GD21631 {ECO:0000313|EMBL:EDX05753.1};
GN ORFNames=Dsim_GD21631 {ECO:0000313|EMBL:EDX05753.1}, Dsimw501_GD21631
GN {ECO:0000313|EMBL:KMY91369.1};
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX05753.1, ECO:0000313|Proteomes:UP000000304};
RN [1] {ECO:0000313|EMBL:EDX05753.1, ECO:0000313|Proteomes:UP000000304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mixed {ECO:0000313|EMBL:EDX05753.1}, and mosaic
RC {ECO:0000313|Proteomes:UP000000304};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [2] {ECO:0000313|EMBL:EDX05753.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mixed {ECO:0000313|EMBL:EDX05753.1}, and W501
RC {ECO:0000313|EMBL:KMY91369.1};
RG FlyBase;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KMY91369.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W501 {ECO:0000313|EMBL:KMY91369.1};
RX PubMed=22936249; DOI=10.1101/gr.141689.112;
RA Hu T.T., Eisen M.B., Thornton K.R., Andolfatto P.;
RT "A second-generation assembly of the Drosophila simulans genome provides
RT new insights into patterns of lineage-specific divergence.";
RL Genome Res. 23:89-98(2013).
RN [4] {ECO:0000313|EMBL:KMY91369.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W501 {ECO:0000313|EMBL:KMY91369.1};
RA Hu T., Eisen M.B., Thornton K.R., Andolfatto P.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CM000361; EDX05753.1; -; Genomic_DNA.
DR EMBL; CM002910; KMY91369.1; -; Genomic_DNA.
DR RefSeq; XP_002080168.1; XM_002080132.2.
DR AlphaFoldDB; B4Q4F6; -.
DR SMR; B4Q4F6; -.
DR STRING; 7240.B4Q4F6; -.
DR EnsemblMetazoa; FBtr0221541; FBpp0220033; FBgn0193055.
DR GeneID; 6733091; -.
DR KEGG; dsi:Dsimw501_GD21631; -.
DR HOGENOM; CLU_002794_11_2_1; -.
DR OMA; NRHNRFY; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000000304; Chromosome 2l.
DR Proteomes; UP000035880; Chromosome 2L.
DR Bgee; FBgn0193055; Expressed in embryo and 3 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR CDD; cd03700; EF2_snRNP_like_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000000304}.
FT DOMAIN 17..348
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 844 AA; 94475 MW; 388EA43C654E3A31 CRC64;
MVNFTVDEIR GLMDKKRNIR NMSVIAHVDH GKSTLTDSLV SKAGIIAGAK AGETRFTDTR
KDEQERCITI KSTAISMYFE VEEKDLVFIT HPDQREKECK GFLINLIDSP GHVDFSSEVT
AALRVTDGAL VVVDCVSGVC VQTETVLRQA IAERIKPILF MNKMDRALLE LQLDAEELYQ
TFQRIVENVN VIIATYNDDG GPMGEVRVDP SKGSVGFGSG LHGWAFTLKQ FSEMYSEKFK
IDVVKLMNRL WGENFFNAKT KKWQKQKEAD NKRSFCMYIL DPIYKVFDAI MNYKKEEIGT
LLEKIGVTLK HEDKDKDGKA LLKTVMRTWL PAGEALLQMI AIHLPSPVVA QKYRMEMLYE
GPHDDEAALA VKSCDPDGPL MMYISKMVPT SDKGRFYAFG RVFAGKVATG QKCRIMGPNY
TPGKKEDLYE KAIQRTILMM GRYVEAIEDV PSGNICGLVG VDQFLVKTGT ITTFKDAHNM
KVMKFSVSPV VRVAVEPKNP ADLPKLVEGL KRLAKSDPMV QCIIEESGEH IIAGAGELHL
EICLKDLEED HACIPLKKSD PVVSYRETVS EESDQMCLSK SPNKHNRLLM KALPMPDGLP
EDIDNGDVSS KDEFKARARY LSEKYDYDVT EARKIWCFGP DGTGPNFILD CTKSVQYLNE
IKDSVVAGFQ WASKEGILAD ENLRGVRFNI YDVTLHADAI HRGGGQIIPT TRRCLYAAAI
TAKPRLMEPV YLCEIQCPEV AVGGIYGVLN RRRGHVFEEN QVVGTPMFVV KAYLPVNESF
GFTADLRSNT GGQAFPQCVF DHWQVLPGDP SEPSSKPYAI VQDTRKRKGL KEGLPDLSQY
LDKL
//
