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Database: UniProt
Entry: A0A0J0XGU7_9TREE
LinkDB: A0A0J0XGU7_9TREE
Original site: A0A0J0XGU7_9TREE 
ID   A0A0J0XGU7_9TREE        Unreviewed;       305 AA.
AC   A0A0J0XGU7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   08-NOV-2023, entry version 36.
DE   RecName: Full=S5 DRBM domain-containing protein {ECO:0000259|PROSITE:PS50881};
GN   ORFNames=CC85DRAFT_158755 {ECO:0000313|EMBL:KLT40315.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT40315.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT40315.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT40315.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000256|ARBA:ARBA00008945, ECO:0000256|RuleBase:RU003823}.
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DR   EMBL; KQ087237; KLT40315.1; -; Genomic_DNA.
DR   RefSeq; XP_018276806.1; XM_018419634.1.
DR   AlphaFoldDB; A0A0J0XGU7; -.
DR   STRING; 879819.A0A0J0XGU7; -.
DR   GeneID; 28980237; -.
DR   OrthoDB; 1407097at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; IPR013810; Ribosomal_uS5_N.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR   PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 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; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611};
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          121..185
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50881"
FT   REGION          14..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  33768 MW;  9EBB6F94B5291874 CRC64;
     MSLVRPARRL LARAPLARAA STSTSTPTPA DQPKAVGNLS PKDIANLTRP LMPHYTVARS
     PDFPNYYKDA PQHRIYNFPN NTFPPLPESQ HPTALGENMA AKNRRVLSAI TGYTREELEG
     LYRYPVDVRR VVNMTKKGKM PSWFSVMVVG DPKRGLVGIG HGKNEAIQLA HQRAFNQAVL
     NMDAVPRFEN RTLYGQGADL RVKWRATTVI MRARPPGFGL QVPHVLHRIF SACGIRDASA
     QILGSTNKTQ VVKAALQIIH GGALPPGSGT GKSKARRENK GAGMRTLREL ERMRGRYGID
     MNRHL
//
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