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Database: UniProt
Entry: A0A101WVI8_9CREN
LinkDB: A0A101WVI8_9CREN
Original site: A0A101WVI8_9CREN 
ID   A0A101WVI8_9CREN        Unreviewed;       271 AA.
AC   A0A101WVI8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|ARBA:ARBA00035242, ECO:0000256|HAMAP-Rule:MF_01320};
GN   Name=rpl2p {ECO:0000313|EMBL:KUO80010.1};
GN   Synonyms=rpl2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN   ORFNames=AT718_06945 {ECO:0000313|EMBL:KUO80010.1};
OS   Vulcanisaeta sp. JCHS_4.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Vulcanisaeta.
OX   NCBI_TaxID=1714253 {ECO:0000313|EMBL:KUO80010.1, ECO:0000313|Proteomes:UP000054689};
RN   [1] {ECO:0000313|EMBL:KUO80010.1, ECO:0000313|Proteomes:UP000054689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA   Inskeep W.P.;
RT   "The distribution, diversity and function of predominant Thermoproteales in
RT   high-temperature environments of Yellowstone National Park.";
RL   Submitted (OCT-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:KUO80010.1}.
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DR   EMBL; LOCE01000078; KUO80010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101WVI8; -.
DR   STRING; 1714253.AT718_06945; -.
DR   Proteomes; UP000054689; 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          92..223
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          199..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   271 AA;  29466 MW;  AB6C1F3B57A6F374 CRC64;
     MGKRILVQRR GRGGSQFRSP SWIREGPVRY LSMSEAELNG VIRGIVKELL HVPGLNAPVA
     RIVLEDGREF LNYAAEGMYV GQVIEIGTAA RPTPGNILPL GKVPEGTMVY NVEKRLNDGG
     KFVRSGGTYA VVLAHKDGTT VVQLPSGKIM EVDSRSRVTI GIVAGGGRIE KPMLKAGAKY
     YRAKAKAWKY PTVRGKAMNP YAHPHGGGSH QKGETPVPRN APPGQKIGII APRCTGRRCP
     QIVPRSKRVW ASGYSKKTRL KNKRSNALPS E
//
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