ID A8Q6L9_MALGO Unreviewed; 484 AA.
AC A8Q6L9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=MGL_3004 {ECO:0000313|EMBL:EDP42804.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP42804.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP42804.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EDP42804.1}.
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DR EMBL; AAYY01000010; EDP42804.1; -; Genomic_DNA.
DR RefSeq; XP_001730018.1; XM_001729966.1.
DR AlphaFoldDB; A8Q6L9; -.
DR STRING; 425265.A8Q6L9; -.
DR GeneID; 5854325; -.
DR KEGG; mgl:MGL_3004; -.
DR VEuPathDB; FungiDB:MGL_3004; -.
DR InParanoid; A8Q6L9; -.
DR OMA; CFETEHR; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000008837; 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; cd01883; EF1_alpha; 1.
DR CDD; cd16267; HBS1-like_II; 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; IPR031157; G_TR_CS.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008837}.
FT DOMAIN 49..274
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 52740 MW; 6DF9998AAEC11233 CRC64;
MKVNIGSQSP SSTSLSSSST RSQLPPTPKL AFSREQILQE LRVREQSQHR EIGLVVVGHV
DAGKSTLMGR MLVELGNITE REHNQNVRSS SKAGKSSFAY AWSLDSSEEE RARGVTIDVA
HDTFRTKHTL FHLLDAPGHK DFVPNMISGA AQADAGLLVV DSITGEFEAG FSPQGQTREH
ATLLRSLGLQ QLIVVINKLD AMNYSQQRFD EIVSTLSPFL SQLGFDVNKC VQFVPCAAMM
GENLRARSEE ASLSRWYTGV TVAEALDRLE QPSRMYESPF RLSVNNVFKG GSLVSSGLGV
SGRILSGFVQ AGEVVRVLPG DAWGIVKMIE CENDARPWAA AGTIVTLYLT HIEPNEVSVG
SFLCPPTALV PLCKEIVVQL LTFSLVYPIL PGTTVEVFHH SAEIPGQIVE LINLLDRASG
DVIRSHPRVM SRDAAGTVRV TLGRRGRDGS GFPIEEFKTN KGMARVLFRM RGETVAAGIV
LEAK
//
