ID A0A1L7XFW6_9HELO Unreviewed; 94 AA.
AC A0A1L7XFW6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=Ribosomal protein L37 {ECO:0000256|RuleBase:RU000576};
GN ORFNames=PAC_13828 {ECO:0000313|EMBL:CZR63931.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR63931.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR63931.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR63931.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-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; FJOG01000025; CZR63931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7XFW6; -.
DR STRING; 576137.A0A1L7XFW6; -.
DR OrthoDB; 5471297at2759; -.
DR Proteomes; UP000184330; 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:UP000184330};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU000576};
KW Ribosomal protein {ECO:0000256|RuleBase:RU000576,
KW ECO:0000313|EMBL:CZR63931.1}; 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 53..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; 10632 MW; 54C0AE08E49CB687 CRC64;
MTKGTSSFGK RHNKTHTLCR RCGRRSLHIQ KHTCSSCGYP AAKIRQYNWG EKAKRRKTTG
TGRMRHMKGV PRKFKNGFQT GAPKDSRGPA TKAE
//