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Database: UniProt
Entry: A0A0E0CLG0_9ORYZ
LinkDB: A0A0E0CLG0_9ORYZ
Original site: A0A0E0CLG0_9ORYZ 
ID   A0A0E0CLG0_9ORYZ        Unreviewed;       682 AA.
AC   A0A0E0CLG0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=60S acidic ribosomal protein P2 {ECO:0008006|Google:ProtNLM};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI02G18930.1};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI02G18930.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI02G18930.1};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI02G18930.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- FUNCTION: Plays an important role in the elongation step of protein
CC       synthesis. {ECO:0000256|ARBA:ARBA00003362}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC       {ECO:0000256|ARBA:ARBA00011266}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000256|ARBA:ARBA00005436}.
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DR   AlphaFoldDB; A0A0E0CLG0; -.
DR   STRING; 40149.A0A0E0CLG0; -.
DR   EnsemblPlants; OMERI02G18930.1; OMERI02G18930.1; OMERI02G18930.
DR   Gramene; OMERI02G18930.1; OMERI02G18930.1; OMERI02G18930.
DR   Proteomes; UP000008021; Chromosome 2.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR   CDD; cd11072; CYP71-like; 1.
DR   CDD; cd05833; Ribosomal_P2; 1.
DR   Gene3D; 1.10.10.1410; -; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR038716; P1/P2_N_sf.
DR   InterPro; IPR027534; Ribosomal_P1/P2.
DR   InterPro; IPR044076; Ribosomal_P2.
DR   PANTHER; PTHR47956; CYTOCHROME P450 71B11-RELATED; 1.
DR   PANTHER; PTHR47956:SF13; ENT-ISOKAURENE C2/C3-HYDROXYLASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   Pfam; PF00428; Ribosomal_60s; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   REGION          647..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  74617 MW;  76AC19BF7DA13058 CRC64;
     MEDKTILLSL ALSMLFVILL SKLVSISKKP RLNLPPGPWT LPVIGSIHHL ASNPNTHRVL
     RALSEKHGPL MQLWLGEVPA VVASTPEAAR EILKSQDLRF ADRHVTSTVA TVSFGASDIF
     FSPYGERWRQ LRKLCTQELL TATRVRSFSR VREDEVARLV RELAASAGGA AVDLTERLGR
     LVNDVVMRCS VGGRCRYRDE FLDALHEAKN QLTWLTVADL FPSSRLARML GAAPRRGLAS
     RKRIERIIAD IVREHEGYMG GGGGEAAAAG KDCFLSVLLG LQKEGGTPIP ITNEIIVVLL
     FDMFSGGSET SATVMIWIMA ELIRWPRVMT KVQAEVRQAL QGKVTVTEDD IVGLNYLKMV
     IKETLRLHCP GPLLVPHRCR ETCKVMGYDV LKGTCVFVNV WALGRDPKYW EDPEEFKPER
     FENSDMDYKG NTFEYLPFGS GRRICPGINF GIANIELPLA SLLYHFDWKL PDEMASKDLD
     MQEAPGMVAA KLTSLCVCPI TRVAPLISAP GPYLLPNNIL EARPNPAHSE PEADLFLAIS
     LLSRDLAAVT FSPHTLRLPD PHRPPPSSKM KFISAYLLAT LAGNPNPSAE DLSTILESVG
     AEVDHGKMDL LLSQLAGKDI TEIIASGREK FASVPCGGGG IAVAAAAPAA GGGAAPQSEA
     KKEEKVEEKE ESDDDMGFSL FD
//
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