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Database: UniProt
Entry: A0A238DWJ5_9BURK
LinkDB: A0A238DWJ5_9BURK
Original site: A0A238DWJ5_9BURK 
ID   A0A238DWJ5_9BURK        Unreviewed;       234 AA.
AC   A0A238DWJ5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Large ribosomal subunit protein uL1 {ECO:0000256|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000256|HAMAP-Rule:MF_01318,
GN   ECO:0000313|EMBL:SCC95836.1};
GN   ORFNames=THIX_90611 {ECO:0000313|EMBL:SCC95836.1};
OS   Thiomonas sp. X19.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=1050370 {ECO:0000313|EMBL:SCC95836.1, ECO:0000313|Proteomes:UP000250096};
RN   [1] {ECO:0000313|EMBL:SCC95836.1, ECO:0000313|Proteomes:UP000250096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X19 {ECO:0000313|EMBL:SCC95836.1,
RC   ECO:0000313|Proteomes:UP000250096};
RA   Regsiter A., william w.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC       the ribosome, and is involved in E site tRNA release.
CC       {ECO:0000256|HAMAP-Rule:MF_01318}.
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01318}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01318}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000256|ARBA:ARBA00010531, ECO:0000256|HAMAP-Rule:MF_01318,
CC       ECO:0000256|RuleBase:RU000659}.
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:SCC95836.1}.
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DR   EMBL; FMBP01000011; SCC95836.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238DWJ5; -.
DR   OrthoDB; 9803740at2; -.
DR   Proteomes; UP000250096; Chromosome thix.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.30.190.20; -; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR   InterPro; IPR005878; Ribosom_uL1_bac-type.
DR   InterPro; IPR002143; Ribosomal_uL1.
DR   InterPro; IPR023674; Ribosomal_uL1-like.
DR   InterPro; IPR028364; Ribosomal_uL1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_uL1_CS.
DR   NCBIfam; TIGR01169; rplA_bact; 1.
DR   PANTHER; PTHR36427:SF3; 39S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR36427; 54S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; Ribosomal protein L1; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000250096};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_01318};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01318};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_01318}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01318}.
SQ   SEQUENCE   234 AA;  24288 MW;  A812BF06994F16EC CRC64;
     MAKKLPKRYA ALRAKVEANK LYSVDDALNL IKECAVAKFD ESIDVAVALG IDARKSDQVV
     RGSVVLPAGT GKVKRVAVFA QGAKAEEAKA AGADIVGFED LAEQVKAGNL NFDVVIASPD
     AMRIVGALGQ ILGPRGLMPN PKVGTVTPDV AGAVKNAKAG QVQFRADKAG IVHSTIGRAS
     FQPDALKSNL QALVEALNKS RPQTAKGVYL RKVAVSSTMG VGLRVDAASI MATA
//
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