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Database: UniProt
Entry: A0A1M5MUC9_9ACTN
LinkDB: A0A1M5MUC9_9ACTN
Original site: A0A1M5MUC9_9ACTN 
ID   A0A1M5MUC9_9ACTN        Unreviewed;       163 AA.
AC   A0A1M5MUC9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
GN   ORFNames=SAMN05444351_3303 {ECO:0000313|EMBL:SHG80954.1};
OS   Geodermatophilus nigrescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1070870 {ECO:0000313|EMBL:SHG80954.1, ECO:0000313|Proteomes:UP000184471};
RN   [1] {ECO:0000313|EMBL:SHG80954.1, ECO:0000313|Proteomes:UP000184471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45408 {ECO:0000313|EMBL:SHG80954.1,
RC   ECO:0000313|Proteomes:UP000184471};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 tunnel
CC       in the center of the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01331}.
CC   -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding is
CC       stimulated by other ribosomal proteins, e.g., L4, L17, and L20. It is
CC       important during the early stages of 50S assembly. It makes multiple
CC       contacts with different domains of the 23S rRNA in the assembled 50S
CC       subunit and ribosome. {ECO:0000256|HAMAP-Rule:MF_01331,
CC       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 family.
CC       {ECO:0000256|ARBA:ARBA00009451, ECO:0000256|HAMAP-Rule:MF_01331,
CC       ECO:0000256|RuleBase:RU004005}.
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DR   EMBL; FQVX01000003; SHG80954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5MUC9; -.
DR   STRING; 1070870.SAMN05444351_3303; -.
DR   OrthoDB; 9805969at2; -.
DR   Proteomes; UP000184471; Unassembled WGS sequence.
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; Ribosomal protein L22/L17; 1.
DR   HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR   InterPro; IPR001063; Ribosomal_uL22.
DR   InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type.
DR   InterPro; IPR047867; Ribosomal_uL22_bac/org-type.
DR   InterPro; IPR018260; Ribosomal_uL22_CS.
DR   InterPro; IPR036394; Ribosomal_uL22_sf.
DR   NCBIfam; TIGR01044; rplV_bact; 1.
DR   PANTHER; PTHR13501:SF10; 50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR13501; CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01331};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01331};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01331};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01331}.
FT   REGION          124..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   163 AA;  17599 MW;  F692E83A64CF1158 CRC64;
     MTSQLGEETQ VARATARFVR VAPMKARRVV DLVRYLPTDE ALALLRFAPQ AASEPVAKVV
     ASAVANAEHN LRLDPAALVV SAAYVDEGPT LKRIRPRAQG RAYRINKRTS HITVEVTEVG
     ASAELAGKSR TARRRTGQSG PATQQTGQQQ GTQQRSNTRG GTR
//
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