ID A0A094IP66_9GAMM Unreviewed; 214 AA.
AC A0A094IP66;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000256|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000256|HAMAP-Rule:MF_01325};
GN ORFNames=IDAT_06790 {ECO:0000313|EMBL:KFZ28897.1};
OS Pseudidiomarina atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ28897.1, ECO:0000313|Proteomes:UP000053718};
RN [1] {ECO:0000313|EMBL:KFZ28897.1, ECO:0000313|Proteomes:UP000053718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ28897.1,
RC ECO:0000313|Proteomes:UP000053718};
RA Du J., Lai Q., Shao Z.;
RT "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003906}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L19. {ECO:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003906}.
CC -!- PTM: Methylated by PrmB. {ECO:0000256|HAMAP-Rule:MF_01325}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000256|ARBA:ARBA00006540, ECO:0000256|HAMAP-Rule:MF_01325,
CC ECO:0000256|RuleBase:RU003905}.
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:KFZ28897.1}.
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DR EMBL; JPIN01000006; KFZ28897.1; -; Genomic_DNA.
DR RefSeq; WP_034732166.1; NZ_JPIN01000006.1.
DR AlphaFoldDB; A0A094IP66; -.
DR STRING; 1517416.IDAT_06790; -.
DR eggNOG; COG0087; Bacteria.
DR OrthoDB; 9806135at2; -.
DR Proteomes; UP000053718; 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; 3.30.160.810; -; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR InterPro; IPR000597; Ribosomal_uL3.
DR InterPro; IPR019927; Ribosomal_uL3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_uL3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR03625; L3_bact; 1.
DR PANTHER; PTHR11229:SF8; 39S RIBOSOMAL PROTEIN L3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11229; 50S RIBOSOMAL PROTEIN L3; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 3: Inferred from homology;
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW ECO:0000256|RuleBase:RU003906};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01325,
KW ECO:0000256|RuleBase:RU003906}.
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01325"
SQ SEQUENCE 214 AA; 22713 MW; 11A104864EA7E154 CRC64;
MAIGLVGRKV GMTRVFQEDG ASVPVTVIEV TANRVTQVKT EETDGYRALQ VTTGDKKANR
VNKPAAGHFA KAGVEAGRGL WEFRLEDGEG DDFAVGSEIT VEIFADTKKV DVTGISKGKG
FQGAIKRWNF RTQDATHGNS LSHRAPGSIG QNQSPGRVFK GKKMAGQMGN KQITVQTLDV
VRVDAERGLL LIRGAVPGAT GGDVIIKPAV KAKA
//
