UniProt: Q6Y4P5

Database: UniProt
Entry: Q6Y4P5_ASTYP

LinkDB:  Q6Y4P5_ASTYP 
Original site:  Q6Y4P5_ASTYP

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Ontology (4)   
   GO (4)   
DNA sequence (19)   
   EMBL (19)   
Protein domain (7)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (31)   

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ID   Q6Y4P5_ASTYP            Unreviewed;       129 AA.
AC   Q6Y4P5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000313|EMBL:AAO74904.1};
GN   Synonyms=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
OS   Aster yellows phytoplasma.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX   NCBI_TaxID=35779 {ECO:0000313|EMBL:AAO74904.1};
RN   [1] {ECO:0000313|EMBL:AAO74904.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Btsv4M.f.6 {ECO:0000313|EMBL:AAO74904.1};
RA   Lee I.-M., Martini M., Bottner K.D., Black M.C., Troxclair N.;
RT   "Ecological aspects of phytoplasmas involved in an aster yellows epidemic
RT   in various crops in Texas.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAO74901.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BB {ECO:0000313|EMBL:AAO74910.1}, Btsv2C.a13
RC   {ECO:0000313|EMBL:AAO74916.1}, Btsv2C.a28a
RC   {ECO:0000313|EMBL:AAO74919.1}, Btsv2CarD1
RC   {ECO:0000313|EMBL:AAO74922.1}, Btsv2CarD4
RC   {ECO:0000313|EMBL:AAO74925.1}, Btsv2CarD5
RC   {ECO:0000313|EMBL:AAO74928.1}, Btsv4C.a.2
RC   {ECO:0000313|EMBL:AAO74901.1}, Btsv4C.a21
RC   {ECO:0000313|EMBL:AAO74931.1}, Btsv4CarD6
RC   {ECO:0000313|EMBL:AAO74934.1}, Btsv4S.i4
RC   {ECO:0000313|EMBL:AAO74937.1}, BtsvCarH4
RC   {ECO:0000313|EMBL:AAO74913.1}, Chry {ECO:0000313|EMBL:AAO74940.1},
RC   DillH2 {ECO:0000313|EMBL:AAO74943.1}, OnionD1
RC   {ECO:0000313|EMBL:AAO74907.1}, ParsD3 {ECO:0000313|EMBL:AAO74952.1},
RC   PLD1 {ECO:0000313|EMBL:AAO74958.1}, RgwdD1
RC   {ECO:0000313|EMBL:AAO74964.1}, and RgwdD2
RC   {ECO:0000313|EMBL:AAO74967.1};
RA   Lee I.-M., Martini M., Bottner K.D., Dane R.A., Black M.C., Troxclair N.;
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAO74901.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BB {ECO:0000313|EMBL:AAO74910.1}, Btsv2C.a13
RC   {ECO:0000313|EMBL:AAO74916.1}, Btsv2C.a28a
RC   {ECO:0000313|EMBL:AAO74919.1}, Btsv2CarD1
RC   {ECO:0000313|EMBL:AAO74922.1}, Btsv2CarD4
RC   {ECO:0000313|EMBL:AAO74925.1}, Btsv2CarD5
RC   {ECO:0000313|EMBL:AAO74928.1}, Btsv4C.a.2
RC   {ECO:0000313|EMBL:AAO74901.1}, Btsv4C.a21
RC   {ECO:0000313|EMBL:AAO74931.1}, Btsv4CarD6
RC   {ECO:0000313|EMBL:AAO74934.1}, Btsv4S.i4
RC   {ECO:0000313|EMBL:AAO74937.1}, BtsvCarH4
RC   {ECO:0000313|EMBL:AAO74913.1}, Chry {ECO:0000313|EMBL:AAO74940.1},
RC   DillH2 {ECO:0000313|EMBL:AAO74943.1}, OnionD1
RC   {ECO:0000313|EMBL:AAO74907.1}, ParsD3 {ECO:0000313|EMBL:AAO74952.1},
RC   PLD1 {ECO:0000313|EMBL:AAO74958.1}, RgwdD1
RC   {ECO:0000313|EMBL:AAO74964.1}, and RgwdD2
RC   {ECO:0000313|EMBL:AAO74967.1};
RX   PubMed=18944064;
RA   Lee I.M., Martini M., Bottner K.D., Dane R.A., Black M.C., Troxclair N.;
RT   "Ecological implications from a molecular analysis of phytoplasmas involved
RT   in an aster yellows epidemic in various crops in Texas.";
RL   Phytopathology 93:1368-1377(2003).
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|ARBA:ARBA00025084}.
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; AY183683; AAO74901.1; -; Genomic_DNA.
DR   EMBL; AY183684; AAO74904.1; -; Genomic_DNA.
DR   EMBL; AY183685; AAO74907.1; -; Genomic_DNA.
DR   EMBL; AY183686; AAO74910.1; -; Genomic_DNA.
DR   EMBL; AY183687; AAO74913.1; -; Genomic_DNA.
DR   EMBL; AY183688; AAO74916.1; -; Genomic_DNA.
DR   EMBL; AY183689; AAO74919.1; -; Genomic_DNA.
DR   EMBL; AY183690; AAO74922.1; -; Genomic_DNA.
DR   EMBL; AY183691; AAO74925.1; -; Genomic_DNA.
DR   EMBL; AY183692; AAO74928.1; -; Genomic_DNA.
DR   EMBL; AY183693; AAO74931.1; -; Genomic_DNA.
DR   EMBL; AY183694; AAO74934.1; -; Genomic_DNA.
DR   EMBL; AY183695; AAO74937.1; -; Genomic_DNA.
DR   EMBL; AY183696; AAO74940.1; -; Genomic_DNA.
DR   EMBL; AY183697; AAO74943.1; -; Genomic_DNA.
DR   EMBL; AY183700; AAO74952.1; -; Genomic_DNA.
DR   EMBL; AY183702; AAO74958.1; -; Genomic_DNA.
DR   EMBL; AY183704; AAO74964.1; -; Genomic_DNA.
DR   EMBL; AY183705; AAO74967.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6Y4P5; -.
DR   SMR; Q6Y4P5; -.
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}.
SQ   SEQUENCE   129 AA;  14289 MW;  19B8A3BD52ED36EA CRC64;
     METKNAKAIA RKVSIAPRKA RLVVDLIRGK NIAQAQAILT FTPKVAAPVI LKLLNSAVSN
     AVNNLKLNRE QLYVKEVFVN EGFRLKRMFP RAKGSGDMIK KRTSHITLVI TSSTNLQTSK
     EEEQSGSKN
//

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