ID F2PTP8_TRIEC Unreviewed; 311 AA.
AC F2PTP8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=60S acidic ribosomal protein P0 {ECO:0000256|PIRNR:PIRNR039087};
GN ORFNames=TEQG_04422 {ECO:0000313|EMBL:EGE05266.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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 ---------------------------------------------------------------------------
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; DS995738; EGE05266.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PTP8; -.
DR VEuPathDB; FungiDB:TEQG_04422; -.
DR eggNOG; KOG0815; Eukaryota.
DR HOGENOM; CLU_053173_1_1_1; -.
DR Proteomes; UP000009169; 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:0042254; P:ribosome biogenesis; 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; 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 SUPFAM; SSF160369; Ribosomal protein L10-like; 1.
PE 3: Inferred from homology;
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 109..178
FT /note="Large ribosomal subunit protein uL10-like insertion"
FT /evidence="ECO:0000259|Pfam:PF17777"
FT REGION 271..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 34030 MW; 91A24310381EE78B CRC64;
MGGKSEAKAA YFDKLKSLLD EYRSIFIVNV DNVSSQQMHE IRLALRGEGV VLMGKNTMVR
RALKGFISDN PEYERLLPFV KGNVGFIFTN GDLKEIREKI ISNRVAAPAR AGAIAPVDVY
IPAGNTGMEP GKTSFFQALG VPTKIARGTI EITTELRLVE AKTKVGPSEA TLLNMLNISP
FTYGMTVAQI YDAGQTFDSS VLDIEEDHLL SVFQSAVNNI ACVSLAANFP TMPSVIHSLI
NTYKKCVAIG IETEYSWESI EELKDRIANP DAYVSTGPAV TETKEDKPKE EAKVEEEEEE
SDEGGFGDLF G
//
