ID A0A162R5H3_MUCCL Unreviewed; 308 AA.
AC A0A162R5H3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 26.
DE RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN ORFNames=MUCCIDRAFT_154944 {ECO:0000313|EMBL:OAD08520.1};
OS Mucor lusitanicus CBS 277.49.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD08520.1, ECO:0000313|Proteomes:UP000077051};
RN [1] {ECO:0000313|EMBL:OAD08520.1, ECO:0000313|Proteomes:UP000077051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD08520.1,
RC ECO:0000313|Proteomes:UP000077051};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. uL10 forms part of the P stalk that participates in recruiting
CC G proteins to the ribosome. {ECO:0000256|PIRNR:PIRNR039087}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000256|ARBA:ARBA00008889, ECO:0000256|PIRNR:PIRNR039087}.
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:OAD08520.1}.
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DR EMBL; AMYB01000001; OAD08520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162R5H3; -.
DR STRING; 747725.A0A162R5H3; -.
DR VEuPathDB; FungiDB:QYA_154944; -.
DR OrthoDB; 168365at2759; -.
DR Proteomes; UP000077051; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd05795; Ribosomal_P0_L10e; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR001859; Ribosomal_P1/P2_euk.
DR InterPro; IPR001790; Ribosomal_uL10.
DR InterPro; IPR040637; Ribosomal_uL10-like_insert.
DR InterPro; IPR043164; Ribosomal_uL10-like_insert_sf.
DR InterPro; IPR043141; Ribosomal_uL10-like_sf.
DR InterPro; IPR030670; uL10_eukaryotes.
DR PANTHER; PTHR45699; 60S ACIDIC RIBOSOMAL PROTEIN P0; 1.
DR PANTHER; PTHR45699:SF3; 60S ACIDIC RIBOSOMAL PROTEIN P0; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR PIRSF; PIRSF039087; L10E; 1.
DR PRINTS; PR00456; RIBOSOMALP2.
DR SUPFAM; SSF160369; Ribosomal protein L10-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077051};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|PIRNR:PIRNR039087};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|PIRNR:PIRNR039087}.
FT DOMAIN 108..177
FT /note="Large ribosomal subunit protein uL10-like insertion"
FT /evidence="ECO:0000259|Pfam:PF17777"
FT REGION 285..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 32918 MW; 631077F004DB393E CRC64;
MSKRENKALY FQKLTNYLDT YQSIFIVNVD NVSSNQMHQI RFSLRGEAVV LMGKNTMVRR
ALKGMIAERP ELEKLLNFVK GNIGFVFTNG DLKDIREKIV SNRVAAPARA GAVAPADVIV
PGGNTGMEPG KTSFFQALGI PTKIARGTIE IVSDVKLVQS GSKVGPSEAV LLNMLNISPF
TYGMGVVQVY DAGSLFSADV LDVEESQLVA NLLAAIREIA SISLAVGYPT LASVPHSVIN
GYKNLLAVSV ASDYTFPGSE QIKEYIANPD AFAVAAPVAA ETSSAPAAEA AAEESEEEDD
DMGFGLFD
//
