ID A0A318ZE67_9EURO Unreviewed; 94 AA.
AC A0A318ZE67;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE RecName: Full=Ribosomal protein L37 {ECO:0000256|RuleBase:RU000576};
GN ORFNames=BP01DRAFT_60769 {ECO:0000313|EMBL:PYH44917.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH44917.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH44917.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH44917.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000256|RuleBase:RU000576}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family.
CC {ECO:0000256|ARBA:ARBA00009805, ECO:0000256|RuleBase:RU000576}.
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DR EMBL; KZ821234; PYH44917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZE67; -.
DR STRING; 1450539.A0A318ZE67; -.
DR OrthoDB; 5471297at2759; -.
DR Proteomes; UP000248349; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 2.20.25.30; -; 1.
DR HAMAP; MF_00547; Ribosomal_L37e; 1.
DR InterPro; IPR001569; Ribosomal_eL37.
DR InterPro; IPR011331; Ribosomal_eL37/eL43.
DR InterPro; IPR018267; Ribosomal_eL37_CS.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR10768; 60S RIBOSOMAL PROTEIN L37; 1.
DR PANTHER; PTHR10768:SF0; RIBOSOMAL PROTEIN L37; 1.
DR Pfam; PF01907; Ribosomal_L37e; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS01077; RIBOSOMAL_L37E; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000576};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU000576};
KW Ribosomal protein {ECO:0000256|RuleBase:RU000576,
KW ECO:0000313|EMBL:PYH44917.1}; RNA-binding {ECO:0000256|RuleBase:RU000576};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730,
KW ECO:0000256|RuleBase:RU000576};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000576};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT REGION 50..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 94 AA; 10680 MW; 8B6922EFC6A499B9 CRC64;
MTKGTSSFGK RHNKTHTLCR RCGKRSFHIQ KSTCANCGYP SAKTRKFNWS EKAKRRKTTG
TGRMRHLKEV HRRFHNGFQT GTPKGARGPS TSSN
//
