ID A8PRA3_MALGO Unreviewed; 390 AA.
AC A8PRA3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=tRNA-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGL_0006 {ECO:0000313|EMBL:EDP45017.1};
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:EDP45017.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP45017.1, 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 -!- 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:EDP45017.1}.
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DR EMBL; AAYY01000001; EDP45017.1; -; Genomic_DNA.
DR RefSeq; XP_001732231.1; XM_001732179.1.
DR AlphaFoldDB; A8PRA3; -.
DR STRING; 425265.A8PRA3; -.
DR GeneID; 5856542; -.
DR KEGG; mgl:MGL_0006; -.
DR VEuPathDB; FungiDB:MGL_0006; -.
DR InParanoid; A8PRA3; -.
DR OMA; VANDACF; -.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd10289; GST_C_AaRS_like; 1.
DR CDD; cd02799; tRNA_bind_EMAP-II_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR PANTHER; PTHR11586; TRNA-AMINOACYLATION COFACTOR ARC1 FAMILY MEMBER; 1.
DR PANTHER; PTHR11586:SF33; TYROSINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 11..151
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 213..319
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT REGION 137..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 42153 MW; 7C9085C156C7F719 CRC64;
MAQRSRQLLA EVYTRLISDQ ASLNALRTSN KPLRTYAHEL AALTSKPAAV LGETDDDVKN
TEQWLDQVEG ISGDLGSLDK KLEPITFLSG NAPTAADYSL FASLYDVVST MPPATQHAHP
SLVRYFSHMS HLSASTNVEP PFKPFEPAYE GFPKIERKAE PKKEKKEKKM KDEGGTAAEA
SAPTPSKKDK KSKDKATGGS GPGSGVPSDS GPLPSMVDLR VGKIVKVDRH PDADSLYLEQ
VDFGEADGPR TILSGLVNFV PIEEMRDRWV VGVCNLKPVS MRGIKSFGMI LCATAKEGKE
GGVQPVAPPA GSELGDRVYV EGYEGMEPLE QMNPKKKVFE AIQPNYQTTD AKECVWFGSL
PNGPADEKAP RRLCTSRGIC TAPFAGATLS
//
