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Database: UniProt
Entry: A0A1H9YAM2_9GAMM
LinkDB: A0A1H9YAM2_9GAMM
Original site: A0A1H9YAM2_9GAMM 
ID   A0A1H9YAM2_9GAMM        Unreviewed;       201 AA.
AC   A0A1H9YAM2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000256|ARBA:ARBA00035244, ECO:0000256|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000256|HAMAP-Rule:MF_01328};
GN   ORFNames=SAMN02583745_00148 {ECO:0000313|EMBL:SES65908.1};
OS   Thorsellia anophelis DSM 18579.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Thorselliaceae; Thorsellia.
OX   NCBI_TaxID=1123402 {ECO:0000313|EMBL:SES65908.1, ECO:0000313|Proteomes:UP000242642};
RN   [1] {ECO:0000313|Proteomes:UP000242642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18579 {ECO:0000313|Proteomes:UP000242642};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC       {ECO:0000256|HAMAP-Rule:MF_01328}.
CC   -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC       initially binds near the 5'-end of the 23S rRNA. It is important during
CC       the early stages of 50S assembly. It makes multiple contacts with
CC       different domains of the 23S rRNA in the assembled 50S subunit and
CC       ribosome. {ECO:0000256|HAMAP-Rule:MF_01328}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01328}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000256|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}.
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DR   EMBL; FOHV01000001; SES65908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9YAM2; -.
DR   STRING; 1123402.SAMN02583745_00148; -.
DR   OrthoDB; 9803201at2; -.
DR   Proteomes; UP000242642; 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:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1370.10; -; 1.
DR   HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR   InterPro; IPR002136; Ribosomal_uL4.
DR   InterPro; IPR013005; Ribosomal_uL4-like.
DR   InterPro; IPR023574; Ribosomal_uL4_dom_sf.
DR   NCBIfam; TIGR03953; rplD_bact; 1.
DR   PANTHER; PTHR10746:SF6; 39S RIBOSOMAL PROTEIN L4, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10746; 50S RIBOSOMAL PROTEIN L4; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; Ribosomal protein L4; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000242642};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01328};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01328}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}.
FT   REGION          46..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  22218 MW;  788F8E7A4978456B CRC64;
     MELVIKDANR QLSVSEATFG REFNEALVHQ VVVAYAAGAR QGTRAQKTRA EVAGTGKKPW
     RQKGTGRARA GNAKSPIWRS GGVTFAARPQ DHSQKVNKKM YRGAILSILS ELVRQDRLIV
     VENFAVEAPK TKLLAQKLKD MSLNDVLIVT HEFDENLFLA ARNLYKVDVR DTAGIDPVSL
     IAFDKVVMTA DAVKQIEEML A
//
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