ID A0A062V7N2_9EURY Unreviewed; 250 AA.
AC A0A062V7N2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000256|HAMAP-Rule:MF_01328};
GN Name=rpl4 {ECO:0000256|HAMAP-Rule:MF_01328};
GN ORFNames=ANME2D_00373 {ECO:0000313|EMBL:KCZ73307.1};
OS Candidatus Methanoperedens nitroreducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1392998 {ECO:0000313|EMBL:KCZ73307.1, ECO:0000313|Proteomes:UP000027153};
RN [1] {ECO:0000313|EMBL:KCZ73307.1, ECO:0000313|Proteomes:UP000027153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANME-2d {ECO:0000313|EMBL:KCZ73307.1,
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: Forms part of the polypeptide exit tunnel.
CC {ECO:0000256|HAMAP-Rule:MF_01328}.
CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC initially binds near the 5'-end of the 23S rRNA. It is important during
CC the early stages of 50S assembly. It makes multiple contacts with
CC different domains of the 23S rRNA in the assembled 50S subunit and
CC ribosome. {ECO:0000256|HAMAP-Rule:MF_01328}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01328}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000256|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}.
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:KCZ73307.1}.
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DR EMBL; JMIY01000001; KCZ73307.1; -; Genomic_DNA.
DR RefSeq; WP_048088640.1; NZ_JMIY01000001.1.
DR AlphaFoldDB; A0A062V7N2; -.
DR PATRIC; fig|1392998.3.peg.733; -.
DR OrthoDB; 10737at2157; -.
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; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_A; Ribosomal_L4_A; 1.
DR InterPro; IPR002136; Ribosomal_uL4.
DR InterPro; IPR023574; Ribosomal_uL4_dom_sf.
DR InterPro; IPR013000; Ribosomal_uL4_euk/arc_CS.
DR InterPro; IPR045240; Ribosomal_uL4_euk/arch.
DR InterPro; IPR019970; Ribosomall_uL4-arc.
DR NCBIfam; TIGR03672; rpl4p_arch; 1.
DR PANTHER; PTHR19431; 60S RIBOSOMAL PROTEIN L4; 1.
DR PANTHER; PTHR19431:SF0; 60S RIBOSOMAL PROTEIN L4; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; Ribosomal protein L4; 1.
DR PROSITE; PS00939; RIBOSOMAL_L1E; 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_01328};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01328}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}.
FT REGION 80..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 250 AA; 27609 MW; 37EA127DC2FA998E CRC64;
MEVNIIDLSG NTTKKIASRL FDEPLRPDLI KKAVLAAQAN RQQPYGPHTY AGMRTSAEGW
GPGRGVSRVA RLRNSRRAAR IPQAVKGRQA HPPKPETDRT EKINDRERKK AIRSAIAATG
NEQLVKERGH RFQAQLPLVA VDDLAAITKT KDVKSFMEAV LVWDDILRAK DKTIRAGKGK
RRGRKYKRAK SILIVTSEDK GIAKAARNLA GVDIVTSDQL NAELLAPGTY TGRLTIYTES
AIAKLEEAIQ
//
