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Database: UniProt
Entry: A0A2J6TTY7_9HELO
LinkDB: A0A2J6TTY7_9HELO
Original site: A0A2J6TTY7_9HELO 
ID   A0A2J6TTY7_9HELO        Unreviewed;       259 AA.
AC   A0A2J6TTY7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   RecName: Full=40S ribosomal protein S3 {ECO:0000256|ARBA:ARBA00035408};
GN   ORFNames=K444DRAFT_517191 {ECO:0000313|EMBL:PMD66489.1};
OS   Hyaloscypha bicolor E.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX   NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD66489.1, ECO:0000313|Proteomes:UP000235371};
RN   [1] {ECO:0000313|EMBL:PMD66489.1, ECO:0000313|Proteomes:UP000235371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E {ECO:0000313|EMBL:PMD66489.1,
RC   ECO:0000313|Proteomes:UP000235371};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ613743; PMD66489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6TTY7; -.
DR   STRING; 1095630.A0A2J6TTY7; -.
DR   InParanoid; A0A2J6TTY7; -.
DR   OrthoDB; 5472739at2759; -.
DR   Proteomes; UP000235371; 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:UP000235371};
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          26..97
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50823"
FT   REGION          195..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   259 AA;  28269 MW;  6147797E1522A66F CRC64;
     MASGVPGAAI SKRRKFVADG VFYAELNEFF QRELAEEGYS GVEVRVTPTV TDIIIRATHT
     QEVLGEQGRR IRELTSLIQK RFKFPENSVS LYAAKVQNRG LSAVAQCESL RYKLLNGLAV
     RRACYGVLRF IMESGAKGCE VVVSGKLRAA RAKSMKFTDG FMIHSGQPAK DFIDHATRHV
     LLRQGVLGIK VKIMRGSDPE GKSGPQKSLP DSVTVIEPKE EQSVVQPMSQ DYGAKAAAAQ
     AAAEAQRATE QAEEAPAEE
//
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