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Database: UniProt
Entry: V4YIN8_9ARCH
LinkDB: V4YIN8_9ARCH
Original site: V4YIN8_9ARCH 
ID   V4YIN8_9ARCH            Unreviewed;       240 AA.
AC   V4YIN8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=A07HR60_01918 {ECO:0000313|EMBL:ESS11202.1};
OS   uncultured archaeon A07HR60.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=1412874 {ECO:0000313|EMBL:ESS11202.1, ECO:0000313|Proteomes:UP000030679};
RN   [1] {ECO:0000313|Proteomes:UP000030679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24335829;
RA   Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA   Heidelberg K.B., Banfield J.F., Allen E.E.;
RT   "Seasonal fluctuations in ionic concentrations drive microbial succession
RT   in a hypersaline lake community.";
RL   ISME J. 0:0-0(2013).
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}.
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DR   EMBL; KI543232; ESS11202.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4YIN8; -.
DR   STRING; 1412874.A07HR60_01918; -.
DR   PATRIC; fig|1412874.3.peg.2202; -.
DR   Proteomes; UP000030679; 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; IPR022671; Ribosomal_uL2_CS.
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.
DR   PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030679};
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          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   240 AA;  25431 MW;  1932D1C755F11426 CRC64;
     MGRRIQGQRR GRGSSTFRAP SHRYKAELSH KETEDTDTIA GEIVDIEHDP ARSAPLADVE
     FEDGDRRLIL APEGVRVGEE IQLGVSAEIK PGNTLPLAEI PEGVPICNVE SQTGDGGKFA
     RASGVSARLV SHDSTVTVVE LPSGAIKQLS PQCRATIGVV AGGGRTEKPF VKAGNKHHKM
     RSRGSKYPTV RGVAMNAVDH PFGGGGRQHP GKPKSISRDA PPGRKVGDIA SKRTGRGGDE
//
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