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Database: UniProt
Entry: Q54WF2_DICDI
LinkDB: Q54WF2_DICDI
Original site: Q54WF2_DICDI 
ID   Q54WF2_DICDI            Unreviewed;      1164 AA.
AC   Q54WF2;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   SubName: Full=Elongation factor Tu domain-containing protein {ECO:0000313|EMBL:EAL67619.1};
GN   Name=eftud1 {ECO:0000313|EMBL:EAL67619.1};
GN   ORFNames=DDB_G0279689 {ECO:0000313|EMBL:EAL67619.1};
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL67619.1, ECO:0000313|Proteomes:UP000002195};
RN   [1] {ECO:0000313|EMBL:EAL67619.1, ECO:0000313|Proteomes:UP000002195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4 {ECO:0000313|EMBL:EAL67619.1,
RC   ECO:0000313|Proteomes:UP000002195};
RX   PubMed=15875012; DOI=10.1038/nature03481;
RG   The Dictyostelium discoideum Sequencing Consortium;
RA   Eichinger L., Pachebat J.A., Glockner 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., 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., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K., 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., 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., Spiegler S., Tivey A., Sugano S.,
RA   White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA   Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA   Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA   Noegel A.A., Barrell B., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL67619.1}.
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DR   EMBL; AAFI02000032; EAL67619.1; -; Genomic_DNA.
DR   RefSeq; XP_641601.1; XM_636509.1.
DR   AlphaFoldDB; Q54WF2; -.
DR   SMR; Q54WF2; -.
DR   STRING; 44689.Q54WF2; -.
DR   PaxDb; 44689-DDB0235191; -.
DR   GeneID; 8622177; -.
DR   KEGG; ddi:DDB_G0279689; -.
DR   dictyBase; DDB_G0279689; eftud1.
DR   eggNOG; KOG0467; Eukaryota.
DR   HOGENOM; CLU_002794_3_1_1; -.
DR   InParanoid; Q54WF2; -.
DR   OMA; FARCDIQ; -.
DR   PhylomeDB; Q54WF2; -.
DR   PRO; PR:Q54WF2; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; 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:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042256; P:cytosolic ribosome assembly; IBA:GO_Central.
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   Gene3D; 3.30.230.10; -; 2.
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; 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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR   PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 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   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; 2.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000313|EMBL:EAL67619.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:EAL67619.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002195}.
FT   DOMAIN          17..368
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          380..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..925
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1164 AA;  130130 MW;  D2C3E7453CDA4857 CRC64;
     MPSISPNLLA SLQDHTKNIR NICVLAHVDH GKTTLSDCLI SSNGIISPEM AGKLRYLDFL
     EDEQEREITM KASAISLLFQ QPSSSSSSND KESFLINLID SPGHVDFSSE VSTAVRITDG
     ALVLVDAVEG VCIQTHAVLK QAYQEKVKPC LVLNKIDRLI LELHMTPLEA YQHLSKIIEQ
     VNVITGTLTS EEIILKESSE DYIESSDDSN LNFNENIGTE YYFSPQKGNV AFTTAFDGWG
     FTIKQFIDLC YKKTGIKKEI LEKCLWGEYY YHPKEKKIYK SPKGNLMPMF VTFILNSVWE
     VVKTIVGTPE WIDRDRLDKM ISVLNITVGA RDLASKDQKI VLKSVLHAWL PLSEAVLSMV
     CDKLPDPIEG QARRMEKIFK PSKSLSTSSS SSSSSSNQSN VELIEKQKQL LYDTITCNSS
     DDCEIVAYVA KVFAHNKRGG VQTSTIHRPV PPRRVQPSAV PSQNRQQQLH QDEKDILKID
     NMFISSAPST TNDSTTTTKT TTTSPSSPIT STAKPLDLST IPTGPIKANN NDEEFIAVVR
     VFSGVLKKGK TIYVMGPRYD PMNPTHDVYK VEITHLYLLM GSSLEPIDKV PAGNVCGVGG
     GVGNLVLKSA TISSSLMCPP ISNMMFVSSP IVKVALEPEN ISDLPKLLHG LKLLNQADPL
     VEVYVQETGE HVIVASGELH LERCIRDLKE SFAKINVHVS SPIVPFRETI ITPTITTPTT
     SSTITSSSST TAAATATTTN NSGQQSPPLK EIITVKTANK KVSVKIRAIP LPKNITNLIE
     QRSQQLRDLF LGGKNTNKEL SDNKITKREA EQAEREDFQK ELEEELEKSG GDWKNEIKNI
     WSFGPRHIGP NLLLNHIPGY NLSPYWKHSL QRGIQKKLKK LQKQQQQEKE EIKEEEEEKE
     EEEKEDEEDE DEKEIEEEEI QEEENSNSEV GSIKLLDGDD KFKRISELDN SIVSGFQLAT
     IAGPLCDEPM MGVCLIVEDI DIIREEGDQQ NSDSYGPLSG QMISTVKEGC RMAFQIKPQR
     LMEALYLCEI QVTSTALGKM YSVLSSRRAQ IQKEGVKEGT QIFCIQARLP VVESFGFSQQ
     IMIKTSGAAS TQLFFDNYWE TIEQDPYYEP TTEEELEDNG VNIASLGNNI ARQYMNMIRK
     RKGLFVEEKL VEHADKQRTL KKNK
//
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