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Database: UniProt
Entry: A0A0L0BX67_LUCCU
LinkDB: A0A0L0BX67_LUCCU
Original site: A0A0L0BX67_LUCCU 
ID   A0A0L0BX67_LUCCU        Unreviewed;       681 AA.
AC   A0A0L0BX67;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=FF38_01408 {ECO:0000313|EMBL:KNC29223.1}, FF38_07441
GN   {ECO:0000313|EMBL:KNC24642.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC24642.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC24642.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC24642.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC24642.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
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}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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:KNC24642.1}.
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DR   EMBL; JRES01001202; KNC24642.1; -; Genomic_DNA.
DR   EMBL; JRES01000681; KNC29223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0BX67; -.
DR   STRING; 7375.A0A0L0BX67; -.
DR   EnsemblMetazoa; KNC24642; KNC24642; FF38_07441.
DR   EnsemblMetazoa; KNC29223; KNC29223; FF38_01408.
DR   OMA; CFETEHR; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd16267; HBS1-like_II; 1.
DR   CDD; cd04093; HBS1_C_III; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR015033; HBS1-like_N.
DR   InterPro; IPR037189; HBS1-like_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   Pfam; PF08938; HBS1_N; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF109732; HBS1-like domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          256..479
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          62..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  75538 MW;  5E835151B6CAA994 CRC64;
     MSRHRIVRTM DYNDEYDGYD DVYGHSVDDD NCISPTDAQQ WLYDRARGQN SMSAFMRDNK
     DIAEEEEEGE EDADKSYDKT RRDSDNFQMP VLNDMEQAQL TSCIDEVRSV VGDAVSEKRI
     VETSIKFSYD INKILDEILN DECENKAKRI QQEVPNLQPK GHGPRKLAMG DMDKCSGSVP
     IVKVTAAQGE VKRGFDISSP LLQSSPAASG RNTPVDISED SAKKLPADAA SVFKVSKEQA
     QRDNKQLYSK ERSDQKHHFH MIVIGHVDAG KSTLMGHLLF DTGNVSQRVM HKHEQESKKM
     GKQSFMYAWV LDETGEERAR GITMDVGHFR FETDSKVITL LDAPGHKDFI PNMISGATQA
     DVALLVIDAT RGEFESGFDL GGQTREHALL VRSLGVNQLG VVINKLDTVG WSKERFDEIV
     QKLKGFLKQA GFKESDVSYT PCSGLTGENL TKPATEEALT SWYKGPHLLA VIDSFKIPER
     SIDKPFRMSV SDIYKGTGAG FCISGRIETG VLAVNDKVLV GALREQAQVK SLLIDEMPQN
     TVFAGDQVAV TLSGIDANNI MVGNIICDPQ HPIPVTSRFQ ARILVFNVKV PITIGYPVLL
     HHQSLIEPAV ICKLNAQIHK GTGEVVKKKP RCLGNNSCAL VELETTRPIC IERYADFKEL
     GRVMLRVSGV TIAAGMITKI R
//
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