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Database: UniProt
Entry: A0A0T5ZC25_9ARCH
LinkDB: A0A0T5ZC25_9ARCH
Original site: A0A0T5ZC25_9ARCH 
ID   A0A0T5ZC25_9ARCH        Unreviewed;       243 AA.
AC   A0A0T5ZC25;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN   Name=rpl2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN   ORFNames=XU09_C0010G0013 {ECO:0000313|EMBL:KRT60400.1};
OS   Thaumarchaeota archaeon CSP1-1.
OC   Archaea; Nitrososphaerota.
OX   NCBI_TaxID=1640512 {ECO:0000313|EMBL:KRT60400.1, ECO:0000313|Proteomes:UP000051388};
RN   [1] {ECO:0000313|EMBL:KRT60400.1, ECO:0000313|Proteomes:UP000051388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-1 {ECO:0000313|EMBL:KRT60400.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) 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:KRT60400.1}.
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DR   EMBL; LDXL01000010; KRT60400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T5ZC25; -.
DR   STRING; 1640512.XU09_C0010G0013; -.
DR   PATRIC; fig|1640512.3.peg.1655; -.
DR   Proteomes; UP000051388; 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          89..222
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          202..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   243 AA;  25993 MW;  947E37D1F2B2354B CRC64;
     MGKRPLVRRR GRGGMQFRAT TTGKLAPAKY PNYNLTEKHL GDIIDLVHER GRDVPLAKVR
     FEDGSISFIP AVLGTKVGSK IQFGLEADIS DGNVISVQNI PDGTIVCNVE KHFGDGGSLI
     KSAGTNATVF SHGPDGVTIK LPSGKFSTIN PKNRAMIGTL AGGGVGDRPF MRAGVKWRRF
     RSKGQKYPIV RGVAQAAYVH PHGGGRHQHV GQSSTVSRNA PPGAKVGSIA ARKTGRARIK
     ERK
//
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