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Database: UniProt
Entry: A0A395NBY2_TRIAR
LinkDB: A0A395NBY2_TRIAR
Original site: A0A395NBY2_TRIAR 
ID   A0A395NBY2_TRIAR        Unreviewed;       200 AA.
AC   A0A395NBY2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=60S ribosomal protein L6 {ECO:0000256|RuleBase:RU000662};
GN   ORFNames=TARUN_8861 {ECO:0000313|EMBL:RFU73401.1};
OS   Trichoderma arundinaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU73401.1, ECO:0000313|Proteomes:UP000266272};
RN   [1] {ECO:0000313|EMBL:RFU73401.1, ECO:0000313|Proteomes:UP000266272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU73401.1,
RC   ECO:0000313|Proteomes:UP000266272};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL6 family.
CC       {ECO:0000256|ARBA:ARBA00010592, ECO:0000256|RuleBase:RU000662}.
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:RFU73401.1}.
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DR   EMBL; PXOA01000654; RFU73401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395NBY2; -.
DR   STRING; 490622.A0A395NBY2; -.
DR   Proteomes; UP000266272; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd13156; KOW_RPL6; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   InterPro; IPR000915; 60S_ribosomal_eL6.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR049633; Ribosomal_eL6_CS.
DR   InterPro; IPR041997; Ribosomal_eL6_KOW.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR10715; 60S RIBOSOMAL PROTEIN L6; 1.
DR   PANTHER; PTHR10715:SF0; 60S RIBOSOMAL PROTEIN L6; 1.
DR   Pfam; PF01159; Ribosomal_L6e; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS01170; RIBOSOMAL_L6E; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000266272};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU000662};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000256|RuleBase:RU000662}.
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   200 AA;  22171 MW;  3AF1205C8671A17F CRC64;
     MSAKPTTKQF GKSTREVPAS ADQAKKWYPA DDENEPKKVR KAVRAWAPRK TLQPGTVLIL
     LAGRFRGKRV VLLKTLDQGV LLVTGPFKIN GVPLRRVNSR YVIATSYKVD ISGLDAAKIE
     EISQPKYFTA EKAKEKAGAE AFFKQGEKPQ KKEINSSRAA DQKAVDKALI ASIKKVDLLA
     SYLASTFSLR KGDKPHEMAW
//
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