ID I4YAY1_WALMC Unreviewed; 496 AA.
AC I4YAY1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=WALSEDRAFT_32857 {ECO:0000313|EMBL:EIM21123.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM21123.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM21123.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; JH668234; EIM21123.1; -; Genomic_DNA.
DR RefSeq; XP_006958800.1; XM_006958738.1.
DR AlphaFoldDB; I4YAY1; -.
DR STRING; 671144.I4YAY1; -.
DR GeneID; 18471572; -.
DR KEGG; wse:WALSEDRAFT_32857; -.
DR eggNOG; KOG0458; Eukaryota.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; I4YAY1; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000005242; 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 CDD; cd16267; HBS1-like_II; 1.
DR CDD; cd04093; HBS1_C_III; 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; 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 PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal 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 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242}.
FT DOMAIN 52..278
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 53594 MW; 4870ADDF02C7B707 CRC64;
MNTAQLGKDL TSQLKLSGST PASSRPSTPQ LQESKKLIPR KELLEKVQQT QNEDISLCVV
GHVDAGKSTI LGRLLVDLGE MTSKDHEKNV RNSDKSGKSS FAYAWAMDDL VEERERGVTL
DYAVTSLRTS NGKVLNIVDT PGHAHLVHNM ISGAQQADAA LLIIDARKGE FEAGFSPRGQ
TREHALLIRS LGVRDLGVVV NKIDSVGYSK ERFDEIVAAL TPFLLKSGFN KERISFVPCA
AMTGENVTKR SHKVLESWYN GQTVAQVLDQ FEAPRRPFEA GLRLPVHNIF KGQTAIASGV
GVSGRLCAGV IQVGEKVRCM PGDEFAIVKM IEVDNDSVPF ASAGTNVTVY LANIDPINLS
IGSVLCSPTD LVPLASKFIA QILLFDINIP ILPGTTFEAF IHSINTSASV SKLIETVDRN
TGAVLKSKPR VLTGNSAARV EMSIGSQSLT SQSGSNTPSN NSIPVEKFTD NKDMGRILLR
HEGQTVAAGI IVDYMR
//
