ID A8PXY7_MALGO Unreviewed; 251 AA.
AC A8PXY7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=S5 DRBM domain-containing protein {ECO:0000259|PROSITE:PS50881};
GN ORFNames=MGL_1554 {ECO:0000313|EMBL:EDP44157.1};
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:EDP44157.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44157.1, 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 -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000256|ARBA:ARBA00008945, ECO:0000256|RuleBase:RU003823}.
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:EDP44157.1}.
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DR EMBL; AAYY01000004; EDP44157.1; -; Genomic_DNA.
DR RefSeq; XP_001731371.1; XM_001731319.1.
DR AlphaFoldDB; A8PXY7; -.
DR STRING; 425265.A8PXY7; -.
DR GeneID; 5855678; -.
DR KEGG; mgl:MGL_1554; -.
DR VEuPathDB; FungiDB:MGL_1554; -.
DR InParanoid; A8PXY7; -.
DR OMA; PYEEWSD; -.
DR OrthoDB; 1214284at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR000851; Ribosomal_uS5.
DR InterPro; IPR005324; Ribosomal_uS5_C.
DR InterPro; IPR005711; Ribosomal_uS5_euk/arc.
DR InterPro; IPR013810; Ribosomal_uS5_N.
DR InterPro; IPR018192; Ribosomal_uS5_N_CS.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01020; uS5_euk_arch; 1.
DR PANTHER; PTHR13718:SF4; 40S RIBOSOMAL PROTEIN S2; 1.
DR PANTHER; PTHR13718; RIBOSOMAL S SUBUNIT; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|PROSITE-
KW ProRule:PRU00268};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|PROSITE-
KW ProRule:PRU00268}.
FT DOMAIN 72..135
FT /note="S5 DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50881"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 27277 MW; CC9B3F873D330CF5 CRC64;
MAERGRGGFG RDRGRGGRGR RGARKDEKEE WVPVTSLGRL VKDGKIKSME EIYLFSLPIK
EYQVVDILLP KLTDEVMKIT PVQKQTRAGQ RTRFKAFVAI GDSDGHLGLG VKCAKEVASA
IRGAMIMAKI SIIPVRRGYW GSALGKPHTV PAKVSGKSAS VMCRLVPAPR GIGIVAAPAP
KRLLQLAGID DVYTQSKGQT ATMGNFLKAT FEAVAKTYAI LTPNLWEEVP VPPTPYVEHA
THLARAGKKL H
//
