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RL7_ALIF1
ID   RL7_ALIF1               Reviewed;         122 AA.
AC   Q5E236;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN   Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=VF_2415;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC       interact with GTP-bound translation factors. Is thus essential for
CC       accurate translation. {ECO:0000255|HAMAP-Rule:MF_00368}.
CC   -!- SUBUNIT: Homodimer. Part of the ribosomal stalk of the 50S ribosomal
CC       subunit. Forms a multimeric L10(L12)X complex, where L10 forms an
CC       elongated spine to which 2 to 4 L12 dimers bind in a sequential
CC       fashion. Binds GTP-bound translation factors. {ECO:0000255|HAMAP-
CC       Rule:MF_00368}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00368}.
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DR   EMBL; CP000020; AAW86910.1; -; Genomic_DNA.
DR   RefSeq; WP_005421323.1; NC_006840.2.
DR   RefSeq; YP_205798.1; NC_006840.2.
DR   AlphaFoldDB; Q5E236; -.
DR   SMR; Q5E236; -.
DR   STRING; 312309.VF_2415; -.
DR   EnsemblBacteria; AAW86910; AAW86910; VF_2415.
DR   GeneID; 64243755; -.
DR   KEGG; vfi:VF_2415; -.
DR   PATRIC; fig|312309.11.peg.2448; -.
DR   eggNOG; COG0222; Bacteria.
DR   HOGENOM; CLU_086499_3_2_6; -.
DR   OMA; LEDKWGV; -.
DR   OrthoDB; 1822695at2; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00387; Ribosomal_L7_L12; 1.
DR   Gene3D; 1.20.5.710; -; 1.
DR   Gene3D; 3.30.1390.10; -; 1.
DR   HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR   InterPro; IPR000206; Ribosomal_L7/12.
DR   InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR   InterPro; IPR013823; Ribosomal_L7/L12_C.
DR   InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR   InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR   PANTHER; PTHR45987; PTHR45987; 1.
DR   Pfam; PF00542; Ribosomal_L12; 1.
DR   Pfam; PF16320; Ribosomal_L12_N; 1.
DR   SUPFAM; SSF48300; SSF48300; 1.
DR   SUPFAM; SSF54736; SSF54736; 1.
DR   TIGRFAMs; TIGR00855; L12; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..122
FT                   /note="50S ribosomal protein L7/L12"
FT                   /id="PRO_0000243525"
SQ   SEQUENCE   122 AA;  12254 MW;  E2B913C62941917C CRC64;
     MSITNEQILD AVAEMSVMQV VELIEAMEEK FGVTAAAAVV AGGAAGGDAA EEQSEFDVIL
     TSAGANKVAV IKAVRGATGL GLKEAKGLVD SAPAPLKEGV DKAEAEALKA QLEEAGASVE
     VK
 
 
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