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Database: UniProt
Entry: D7KQZ8_ARALL
LinkDB: D7KQZ8_ARALL
Original site: D7KQZ8_ARALL 
ID   D7KQZ8_ARALL            Unreviewed;       160 AA.
AC   D7KQZ8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Large ribosomal subunit protein uL22c {ECO:0000256|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000256|HAMAP-Rule:MF_01331,
GN   ECO:0000313|EMBL:BAW03025.1};
GN   ORFNames=ARALYDRAFT_315497 {ECO:0000313|EMBL:EFH63100.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:BAW03025.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|EMBL:EFH63100.1}
RP   NUCLEOTIDE SEQUENCE.
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ottilar R., Schmutz J., Salamov A., Cheng J.F., Lucas S., Pitluck S.,
RA   Gundlach H., Guo Y., Haberer G., Nasrallah J., Mayer K.F.X.,
RA   van de Peer Y., Weigel D., Grigoriev I.V.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFH63100.1}
RP   NUCLEOTIDE SEQUENCE.
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Bakker E., Bergelson J., Cheng J.Fang., Clark R.M., Fawcett J., Gaut B.,
RA   Grigoriev I., Gundlach H., Guo Y., Haberer G., Hollister J., Hu T.T.,
RA   Mayer K.F.X., Nasrallah J., Nordborg M., Otillar R., Pattyn P., Schmutz J.,
RA   Spannagl M., van de Peer Y., Wang X., Weigel D., Yang L.;
RT   "The basis of rapid genome size change in Arabidopsis.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
RN   [4] {ECO:0000313|EMBL:CUA65444.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26410304; DOI=10.1105/tpc.15.00482;
RA   Hohmann N., Wolf E.M., Lysak M.A., Koch M.A.;
RT   "A Time-Calibrated Road Map of Brassicaceae Species Radiation and
RT   Evolutionary History.";
RL   Plant Cell 27:2770-2784(2015).
RN   [5] {ECO:0000313|EMBL:CZF91271.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PIN {ECO:0000313|EMBL:CZF91271.1};
RA   Novikova P.Y., Hohmann N., Nizhynska V., Lanz C., Tsuchimatsu T., Muir G.,
RA   Guggisberg A., Paape T., Schmid K., Fedorenko O.M., Holm S., Saell T.,
RA   Schloetterer C., Marhold K., Widmer A., Sese J., Shimizu K.K., Weigel D.,
RA   Kraemer U., Koch M.A., Nordborg M.;
RT   "Sequencing of the genus Arabidopsis reveals a complex history of non-
RT   bifurcating speciation and abundant trans-specific polymorphism.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:BAW03025.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MN47 {ECO:0000313|EMBL:BAW03025.1};
RA   Kawabe A., Tsujino Y., Furihata H.Y., Yoshida T.;
RT   "CHloroplast genome of Arabidopsis lyrata ssp. lyrata.";
RL   Submitted (MAY-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|ARBA:ARBA00003478,
CC       ECO:0000256|HAMAP-Rule:MF_01331, ECO:0000256|RuleBase:RU004009}.
CC   -!- FUNCTION: This protein binds specifically to 23S rRNA.
CC       {ECO:0000256|ARBA:ARBA00003611, ECO:0000256|HAMAP-Rule:MF_01331,
CC       ECO:0000256|RuleBase:RU004009}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01331}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_01331, ECO:0000256|RuleBase:RU004009}.
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; LC154068; BAW03025.1; -; Genomic_DNA.
DR   EMBL; LN877383; CUA65444.1; -; Genomic_DNA.
DR   EMBL; LT161942; CZF91271.1; -; Genomic_DNA.
DR   EMBL; GL348714; EFH63100.1; -; Genomic_DNA.
DR   RefSeq; XP_002886841.1; XM_002886795.1.
DR   AlphaFoldDB; D7KQZ8; -.
DR   STRING; 81972.D7KQZ8; -.
DR   EnsemblPlants; fgenesh1_pm.C_scaffold_2000530; fgenesh1_pm.C_scaffold_2000530; fgenesh1_pm.C_scaffold_2000530.
DR   Gramene; fgenesh1_pm.C_scaffold_2000530; fgenesh1_pm.C_scaffold_2000530; fgenesh1_pm.C_scaffold_2000530.
DR   eggNOG; KOG1711; Eukaryota.
DR   HOGENOM; CLU_083987_3_1_1; -.
DR   OrthoDB; 313251at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   ExpressionAtlas; D7KQZ8; baseline.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   Chloroplast {ECO:0000313|EMBL:BAW03025.1};
KW   Plastid {ECO:0000313|EMBL:BAW03025.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
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   160 AA;  18600 MW;  DE4783CE003BF511 CRC64;
     MIKKRKKKSY TSVYALGQYI SMSAHKARRV IDQIRGRSYE EALMILELMP YRGCYPIFKL
     VYSAAANASH NKGFKETNLV ISKAEVNQGN TVKKLKPRAR GRSYPIKRST CHITIVLEDI
     SFYQQYEEYL MYLKKPGCSN ENRNLTCYDR YSSGGLWDKK
//
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