ID G1X6B2_ARTOA Unreviewed; 1018 AA.
AC G1X6B2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=AOL_s00054g406 {ECO:0000313|EMBL:EGX51336.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX51336.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX51336.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX51336.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADOT01000085; EGX51336.1; -; Genomic_DNA.
DR RefSeq; XP_011120024.1; XM_011121722.1.
DR AlphaFoldDB; G1X6B2; -.
DR STRING; 756982.G1X6B2; -.
DR GeneID; 22890945; -.
DR eggNOG; KOG0467; Eukaryota.
DR HOGENOM; CLU_002794_3_1_1; -.
DR InParanoid; G1X6B2; -.
DR OMA; FARCDIQ; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 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 Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
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; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
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 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; 1.
DR SUPFAM; SSF50447; Translation proteins; 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 Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT DOMAIN 1..217
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 145..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 113013 MW; 59E20BAE8996084E CRC64;
MESSAISLYF QSLKPPVPPS TTPSLQDYLI NLIDSPGHID FSSEVSTASR LCDGALVLVD
AVEGVCSQTV TVLRQTWLEH LRPVLVINKI DRLITEWKMS PTEANVHLGK LLEQVNAVMG
SFFAGERMED DLKWREQMEL RQRQRAARRE SASKTAEEAE AEKLGLEDGY EEKDDEDLYF
SPEKFNVIFA SAIDGWAFTV KDFAAIHEKK LGVKRSVLEK ILWGDFYLDP KTKRVLKKRH
LKGRNLKPMF VQFALDNIWA IYDNILRKDR DQEKVEKIVQ TLGIKVLPRD LKSKDSRALL
STILMQWLPL SRAVLGTVVS QLPSPPAAQK QRVTNLIENS PGGAELIAPE IKNAMENLNV
NEEAIVAYVS KMISVPEKDL PRNQREKLTA EQLRELGRIK RQEMARALAA AAASETASLG
GQSTADSDLE QVVLDMGNSN LETTDTDGKT AAPVDPDKEN LIGFARLYSG TISVGQTLHV
LGPKYDPRQP DQHVSSITVT DLYLMMGREL VSLEKVPAGN VFGIGGLEGK VLKNATLCST
VTGGVNLASV ASMGAAPIVR VALEPKNPGQ LQQMIRGLKL LEQSDPCMEY LVQSNGEHVI
LTAGELHLER CLKDLRERFA KIEIEASKPI VPYRETILSV PEMPPPKNQN LPRGTVVIST
PGKHVTFKLR VRPLPSKAVE YLEENVGTLK KFFAEKQTER DADDLMLLTA GADAKDCLPI
EEFEKGFQAV LIAGATKDTK NVWTDVVSKI SSFGPRRAGP NILIDNANIL RRILRENDES
ETPQNDGNAD EGHESASLQI TIKDFRDKII TAFQNATFQG PLCNEPMQGV AVFLDEVKVE
IADEEVEALR MKIGQLIGEV ITGMTSAIRQ GFLDWSPRLL LAMYSCEIQA SSEVLGKVYG
VITRRRGRIV AEEMKEGTPF YTINSLLPVV ESFGFADEIR TKTSGAASPQ LIFSGFENIL
DEDPFWVPHT EDELEDLGEL ADRENVAKRY MDGVRVRKGL FVAKKMLAGA EKQSTRKK
//
