ID A0A0K9Q3G7_ZOSMR Unreviewed; 94 AA.
AC A0A0K9Q3G7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ribosomal protein L37 {ECO:0000256|RuleBase:RU000576};
GN ORFNames=ZOSMA_11G00800 {ECO:0000313|EMBL:KMZ75057.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ75057.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ75057.1}.
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DR EMBL; LFYR01000216; KMZ75057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9Q3G7; -.
DR STRING; 29655.A0A0K9Q3G7; -.
DR OMA; WSAKAER; -.
DR OrthoDB; 5471297at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:UP000036987};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU000576};
KW Ribosomal protein {ECO:0000256|RuleBase:RU000576,
KW ECO:0000313|EMBL:KMZ75057.1}; 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 73..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 94 AA; 10691 MW; 31A075E72B8D76CA CRC64;
MGKGTGSFGK RRNKTHTLCV RCGRRSFHLQ KSRCASCGYP AARIRKYNWS VKALRRKTTG
TGRMRHLRHL PRRFKSGFRE GSEAAPKNRS ATVA
//
