ID A0A062V9V0_9EURY Unreviewed; 335 AA.
AC A0A062V9V0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000256|HAMAP-Rule:MF_01325};
GN Name=rpl3 {ECO:0000256|HAMAP-Rule:MF_01325};
GN ORFNames=ANME2D_00374 {ECO:0000313|EMBL:KCZ73308.1};
OS Candidatus Methanoperedens nitroreducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1392998 {ECO:0000313|EMBL:KCZ73308.1, ECO:0000313|Proteomes:UP000027153};
RN [1] {ECO:0000313|EMBL:KCZ73308.1, ECO:0000313|Proteomes:UP000027153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANME-2d {ECO:0000313|EMBL:KCZ73308.1,
RC ECO:0000313|Proteomes:UP000027153};
RX PubMed=23892779; DOI=10.1038/nature12375;
RA Haroon M.F., Hu S., Shi Y., Imelfort M., Keller J., Hugenholtz P., Yuan Z.,
RA Tyson G.W.;
RT "Anaerobic oxidation of methane coupled to nitrate reduction in a novel
RT archaeal lineage.";
RL Nature 500:567-570(2013).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000256|HAMAP-Rule:MF_01325}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L24e. {ECO:0000256|HAMAP-Rule:MF_01325}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000256|ARBA:ARBA00006540, ECO:0000256|HAMAP-Rule:MF_01325}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KCZ73308.1}.
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DR EMBL; JMIY01000001; KCZ73308.1; -; Genomic_DNA.
DR RefSeq; WP_048088642.1; NZ_JMIY01000001.1.
DR AlphaFoldDB; A0A062V9V0; -.
DR PATRIC; fig|1392998.3.peg.734; -.
DR OrthoDB; 6121at2157; -.
DR Proteomes; UP000027153; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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 Gene3D; 3.30.1430.10; -; 1.
DR Gene3D; 4.10.960.10; Ribosomal protein L3, domain 3; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_01325_A; Ribosomal_L3_A; 1.
DR InterPro; IPR045077; L3_arc_euk.
DR InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR InterPro; IPR000597; Ribosomal_uL3.
DR InterPro; IPR019928; Ribosomal_uL3_arc.
DR InterPro; IPR019926; Ribosomal_uL3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR03626; L3_arch; 1.
DR PANTHER; PTHR11363:SF5; 60S RIBOSOMAL PROTEIN L3; 1.
DR PANTHER; PTHR11363; 60S RIBOSOMAL PROTEIN L3-RELATED; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000027153};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01325};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01325}.
SQ SEQUENCE 335 AA; 37152 MW; D78E55797CD0D78E CRC64;
MSHPHRPRRG SIAYSPRVRA RSEIPRVRAW PMKKEPKLLG FAGYKAGMTH IIMIDDVPNS
LTAGMEVSIP VTILEAPPMR AAGIRIYDST AYGAHTIAEA WTTELDKELN RTITVPKKND
LSAALARIDQ LINDGVAKDL RIIMYTLPDK VTGIPKKKPE IMENNIGGTD LKARFEYAKT
LLGKTINISD VFNNGDTIDV LAITTGKGTQ GPVKRWGIQL QKSKHSRAGS VRQIGTLGPW
HPSHVSWRVP QLGQTGYHQR TEFNKRIMQI GKDGKTVTPE GGFLNYGIVR NDYVVIKGSV
PGPVKRLVRI RPAIRSKRQL PAPEITYLST ESKQG
//