ID A0A166U4E8_9AGAM Unreviewed; 267 AA.
AC A0A166U4E8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 26.
DE RecName: Full=40S ribosomal protein S3 {ECO:0000256|ARBA:ARBA00035408};
GN ORFNames=FIBSPDRAFT_46583 {ECO:0000313|EMBL:KZP31302.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP31302.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP31302.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP31302.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000256|ARBA:ARBA00010761, ECO:0000256|RuleBase:RU003624}.
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DR EMBL; KV417490; KZP31302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166U4E8; -.
DR STRING; 436010.A0A166U4E8; -.
DR OrthoDB; 5472739at2759; -.
DR Proteomes; UP000076532; 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:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd02413; KH-II_40S_S3; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.30.1140.32; Ribosomal protein S3, C-terminal domain; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR001351; Ribosomal_uS3_C.
DR InterPro; IPR018280; Ribosomal_uS3_CS.
DR InterPro; IPR005703; Ribosomal_uS3_euk/arc.
DR NCBIfam; TIGR01008; uS3_euk_arch; 1.
DR PANTHER; PTHR11760; 30S/40S RIBOSOMAL PROTEIN S3; 1.
DR PANTHER; PTHR11760:SF32; 40S RIBOSOMAL PROTEIN S3; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR SUPFAM; SSF54821; Ribosomal protein S3 C-terminal domain; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003624};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003624};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00118}.
FT DOMAIN 21..92
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 219..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 267 AA; 29380 MW; 99B0C73389BF671C CRC64;
MSAQISKKRK FVADGVFRAE LNEFFTRELA EEGYSGCDVR VTHARTEIII RATHTQEVLG
EKGRRIRELT ALVQKRFKFP ENSLELYAEK VQYRGLSAVA QCESLRYKLL GGLAVRRACY
GVLRFVMESN AKGCEVVVSG KLRAARAKSM KFTDGFMIHS GQPARDFVDY AVRHVLLKQG
VLGIKVKIMK GWDPEGQTGP KNPLPDSVQI LDPPVDKIVS EPSSEQREPA AIPAPAAPAE
EAYAAPQEGY AAPDAYAAEA PAAQPVF
//
