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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//