ID A0A094EU50_9PEZI Unreviewed; 124 AA.
AC A0A094EU50;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 20.
DE RecName: Full=Ribosomal protein L37 {ECO:0000256|RuleBase:RU000576};
GN ORFNames=V499_01145 {ECO:0000313|EMBL:KFY79948.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY79948.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY79948.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY79948.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY79948.1}.
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DR EMBL; JPKB01000135; KFY79948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EU50; -.
DR HOGENOM; CLU_150908_2_0_1; -.
DR Proteomes; UP000029295; 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 Ribonucleoprotein {ECO:0000256|RuleBase:RU000576};
KW Ribosomal protein {ECO:0000256|RuleBase:RU000576};
KW 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 104..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 124 AA; 14069 MW; D4370E49429052DA CRC64;
MFLRGFDALI VHHDKNNDNQ PADKFLFKMT KGTGSFGKRH NKSHVLCRRC GRRSLHVQKH
TCSSCGYPAA KIRGYNWSEK AKRRKTTGSG RMRYLKTVSR KFKNGFQTGV PKDSRGPAAA
PKTE
//