GenomeNet

Database: UniProt
Entry: C4F9T7_9ACTN
LinkDB: C4F9T7_9ACTN
Original site: C4F9T7_9ACTN 
ID   C4F9T7_9ACTN            Unreviewed;       276 AA.
AC   C4F9T7;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   08-NOV-2023, entry version 57.
DE   RecName: Full=Large ribosomal subunit protein uL2 {ECO:0000256|HAMAP-Rule:MF_01320};
GN   Name=rplB {ECO:0000256|HAMAP-Rule:MF_01320,
GN   ECO:0000313|EMBL:EEP44465.1};
GN   ORFNames=COLINT_02821 {ECO:0000313|EMBL:EEP44465.1};
OS   Collinsella intestinalis DSM 13280.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=521003 {ECO:0000313|EMBL:EEP44465.1, ECO:0000313|Proteomes:UP000003295};
RN   [1] {ECO:0000313|EMBL:EEP44465.1, ECO:0000313|Proteomes:UP000003295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13280 {ECO:0000313|EMBL:EEP44465.1,
RC   ECO:0000313|Proteomes:UP000003295};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2009) 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:EEP44465.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABXH02000015; EEP44465.1; -; Genomic_DNA.
DR   RefSeq; WP_006723049.1; NZ_GG692710.1.
DR   AlphaFoldDB; C4F9T7; -.
DR   STRING; 521003.COLINT_02821; -.
DR   GeneID; 77465034; -.
DR   eggNOG; COG0090; Bacteria.
DR   HOGENOM; CLU_036235_2_1_11; -.
DR   Proteomes; UP000003295; 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:0016740; F:transferase activity; 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_B; Ribosomal_L2_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR002171; Ribosomal_uL2.
DR   InterPro; IPR005880; Ribosomal_uL2_bac/org-type.
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   NCBIfam; TIGR01171; rplB_bact; 1.
DR   PANTHER; PTHR13691:SF5; 39S RIBOSOMAL PROTEIN L2, MITOCHONDRIAL; 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   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          124..253
FT                   /note="Large ribosomal subunit protein uL2 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01382"
FT   REGION          221..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  30061 MW;  400D5C0B4A0FFFB8 CRC64;
     MAVKHLKPTS AGRRWQTIAD FSEITCTTPE KSLLEPLPVK AGRNNAGRIT MRHQGGRVKR
     QYRVIDFKRN KDGVPAKVAT IEYDPNRSAR IALLHYVDGE KRYILAPKGL KVGDTVISGA
     GADIKPGNAM PLSEIPVGTL IHAIEFQPGK GAAIARSAGT ACQLMGKEGK YAIIRMPSSE
     MRRVLVTCRA SIGEVGNSEH ANIVIGKAGR HRKMGVRPTV RGTVMNPVDH PHGGGEGRSH
     TSGRPSVSPW GTPSKGYRTR NKKKTSNDLI IRRRKK
//
DBGET integrated database retrieval system