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Database: UniProt
Entry: A0A151BFI1_9ARCH
LinkDB: A0A151BFI1_9ARCH
Original site: A0A151BFI1_9ARCH 
ID   A0A151BFI1_9ARCH        Unreviewed;       245 AA.
AC   A0A151BFI1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|ARBA:ARBA00035242, ECO:0000256|HAMAP-Rule:MF_01320};
GN   Name=rpl2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN   ORFNames=AYL30_003540 {ECO:0000313|EMBL:KYH38666.1};
OS   Candidatus Hecatellales archaeon B24.
OC   Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia;
OC   Candidatus Hecatellales.
OX   NCBI_TaxID=1779369 {ECO:0000313|EMBL:KYH38666.1, ECO:0000313|Proteomes:UP000075493};
RN   [1] {ECO:0000313|EMBL:KYH38666.1, ECO:0000313|Proteomes:UP000075493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B25 {ECO:0000313|EMBL:KYH38666.1};
RA   He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT   "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT   phylum Bathyarchaeota widespread in marine sediments.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC       association of the 30S and 50S subunits to form the 70S ribosome, for
CC       tRNA binding and peptide bond formation. It has been suggested to have
CC       peptidyltransferase activity; this is somewhat controversial. Makes
CC       several contacts with the 16S rRNA in the 70S ribosome.
CC       {ECO:0000256|HAMAP-Rule:MF_01320}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC       subunit in the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01320}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000256|ARBA:ARBA00005636, ECO:0000256|HAMAP-Rule:MF_01320}.
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:KYH38666.1}.
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DR   EMBL; LUCC01000015; KYH38666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BFI1; -.
DR   STRING; 1779369.AYL30_003540; -.
DR   PATRIC; fig|1779369.3.peg.395; -.
DR   Proteomes; UP000075493; Unassembled WGS sequence.
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   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1.
DR   HAMAP; MF_01320_A; Ribosomal_L2_A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR002171; Ribosomal_uL2.
DR   InterPro; IPR023672; Ribosomal_uL2_arc.
DR   InterPro; IPR022669; Ribosomal_uL2_C.
DR   InterPro; IPR014726; Ribosomal_uL2_dom3.
DR   InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691:SF16; 60S RIBOSOMAL PROTEIN L8; 1.
DR   PANTHER; PTHR13691; RIBOSOMAL PROTEIN L2; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01320};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01320}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01320};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01320}.
FT   DOMAIN          90..223
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   245 AA;  25887 MW;  2BF41D7A731B921F CRC64;
     MGKRIRAQRR GKGTPVFRAP THKRVSPARY PPPEVLKGKL KGVVRALIHD LGRGTPLALI
     ECDGGLAFYT VAAEGIHVGQ EIEIGPEAPL KLGNMVPVSV LPEGFTVCNV EKNPGDGGKF
     ARASGSYATV VAKTPAGVIL RLSSGKTTLV NSEALATVGI VAGFGRTEKP FMKAGEKYHL
     MRAKGRKWPV TRGVAMIAAA HPHGGGRHRH LGKPGTISRR APPGRKVGLI AAKQSGRSKR
     SRGGR
//
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