(data stored in SCRATCH zone)

SWISSPROT: D6ZAA1_SEGRD

ID   D6ZAA1_SEGRD            Unreviewed;       161 AA.
AC   D6ZAA1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 45.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000256|HAMAP-Rule:MF_01331, ECO:0000256|RuleBase:RU004008};
GN   Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
GN   OrderedLocusNames=Srot_0154 {ECO:0000313|EMBL:ADG96643.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96643.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96643.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: The globular domain of the protein is located near the
CC       polypeptide exit tunnel on the outside of the subunit, while an
CC       extended beta-hairpin is found that lines the wall of the exit
CC       tunnel in the center of the 70S ribosome. {ECO:0000256|HAMAP-
CC       Rule:MF_01331}.
CC   -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding
CC       is stimulated by other ribosomal proteins, e.g., L4, L17, and L20.
CC       It is important during the early stages of 50S assembly. It makes
CC       multiple contacts with different domains of the 23S rRNA in the
CC       assembled 50S subunit and ribosome. {ECO:0000256|HAMAP-
CC       Rule:MF_01331, ECO:0000256|RuleBase:RU004008}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01331, ECO:0000256|RuleBase:RU004006}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22
CC       family. {ECO:0000256|HAMAP-Rule:MF_01331,
CC       ECO:0000256|RuleBase:RU004005}.
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DR   EMBL; CP001958; ADG96643.1; -; Genomic_DNA.
DR   STRING; 640132.Srot_0154; -.
DR   EnsemblBacteria; ADG96643; ADG96643; Srot_0154.
DR   KEGG; srt:Srot_0154; -.
DR   eggNOG; ENOG4105KAP; Bacteria.
DR   eggNOG; COG0091; LUCA.
DR   HOGENOM; HOG000205046; -.
DR   KO; K02890; -.
DR   OMA; PQGRAHR; -.
DR   Proteomes; UP000002247; Chromosome.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00336; Ribosomal_L22; 1.
DR   Gene3D; 3.90.470.10; -; 1.
DR   HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR   InterPro; IPR001063; Ribosomal_L22.
DR   InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR   InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR   InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR   PANTHER; PTHR13501; PTHR13501; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; SSF54843; 1.
DR   TIGRFAMs; TIGR01044; rplV_bact; 1.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZAA1.
DR   SWISS-2DPAGE; D6ZAA1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01331,
KW   ECO:0000256|RuleBase:RU004005};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01331,
KW   ECO:0000256|RuleBase:RU004005, ECO:0000313|EMBL:ADG96643.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01331,
KW   ECO:0000256|RuleBase:RU004006};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01331,
KW   ECO:0000256|RuleBase:RU004006}.
SQ   SEQUENCE   161 AA;  17403 MW;  2D87E904E903FAC6 CRC64;
     MSTVQDNPTA HASLKGARFS ATKARRVIDL IRGKRVDEAL AILRFAPQSA SEEVSKVLAS
     AVANAEHNLN LHRSTLVVSK AFADEGPTLK RYQPRAQGRS FRIRKRTAHI TIEVAAALAN
     ERPSRAKRVA GSKQGASKKT ESKKTESKKT AATATEKGGE E
//

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