ID A0A165J519_9BASI Unreviewed; 281 AA.
AC A0A165J519;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE RecName: Full=40S ribosomal protein S3 {ECO:0000256|ARBA:ARBA00035408};
GN ORFNames=CALCODRAFT_549257 {ECO:0000313|EMBL:KZT61382.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT61382.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT61382.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT61382.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV423923; KZT61382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165J519; -.
DR STRING; 1353952.A0A165J519; -.
DR InParanoid; A0A165J519; -.
DR OrthoDB; 5472739at2759; -.
DR Proteomes; UP000076842; 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:UP000076842};
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 52..123
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 31328 MW; C65237220E62B4DB CRC64;
MRVHGIKIRA SLPRPQRSPG HRLASTHSPL EDSAVVIRVQ NFVADGVFRA ELGEFFTREL
AEEGYSGCEV RVTHARTEII IRATHTQEVL GDKGRRIREL TSLVQKRFKF PENSLELYAE
KVQNRGLSAV AQCESLRYKL LGGLAVRRAC YGVLRFVMES GAKGCEVVVS GKLRAARAKS
MKFTDGFMIH SGQPARDFVD YAVRHVLLRQ GVLGIKVKIM KGWDPEGRLG PRKPLPDTVT
IIEPPIDKLI TEPLSEQKGP QEQAIPPPAP QQPLEEQPVV E
//