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Database: UniProt
Entry: R9TK54_TRYRA
LinkDB: R9TK54_TRYRA
Original site: R9TK54_TRYRA 
ID   R9TK54_TRYRA            Unreviewed;       128 AA.
AC   R9TK54;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000256|ARBA:ARBA00035298};
OS   Trypanosoma rangeli.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX   NCBI_TaxID=5698 {ECO:0000313|EMBL:AGN32898.1};
RN   [1] {ECO:0000313|EMBL:AGN32898.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Stoco P.H., Wagner G., Gerber A., Zaha A., Monteiro K.M., Thompson C.,
RA   Bartholomeu D.C., Bahia D., Loreto E., Prestes E.B., De Moraes M.H.,
RA   Lueckemeyer D.D., Lima F.M., Vallejo G.A., Silveira Filho J.F., Tyler K.M.,
RA   Almeida L.G., Steindel M., Ortiz M.F.D.E., Siervo M.A., Cunha O.L.D.E.,
RA   Neto R., Rodrigues-Luiz G., Teixeira S.M., Silva R., Murta S.M.,
RA   Sincero T.C., Mendes T.A., Urmenyi T.P., Da Rocha W.D., Vasconcellos A.T.,
RA   Grisard E.C.;
RT   "Unveiling the Trypanosoma rangeli genome, the neglected and avirulent
RT   trypanosome of mammals.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the 60S subunit of the ribosome.
CC       {ECO:0000256|ARBA:ARBA00002241}.
CC   -!- FUNCTION: Exists either covalently attached to another protein, or free
CC       (unanchored). When covalently bound, it is conjugated to target
CC       proteins via an isopeptide bond either as a monomer (monoubiquitin), a
CC       polymer linked via different Lys residues of the ubiquitin
CC       (polyubiquitin chains) or a linear polymer linked via the initiator Met
CC       of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains,
CC       when attached to a target protein, have different functions depending
CC       on the Lys residue of the ubiquitin that is linked: Lys-48-linked is
CC       involved in protein degradation via the proteasome. Linear polymer
CC       chains formed via attachment by the initiator Met lead to cell
CC       signaling. Ubiquitin is usually conjugated to Lys residues of target
CC       proteins, however, in rare cases, conjugation to Cys or Ser residues
CC       has been observed. When polyubiquitin is free (unanchored-
CC       polyubiquitin), it also has distinct roles, such as in activation of
CC       protein kinases, and in signaling. {ECO:0000256|ARBA:ARBA00029384}.
CC   -!- SUBUNIT: Part of the 60S ribosomal subunit.
CC       {ECO:0000256|ARBA:ARBA00035124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eL40 family. {ECO:0000256|ARBA:ARBA00010570}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC       {ECO:0000256|ARBA:ARBA00008373}.
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DR   EMBL; KC544836; AGN32898.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9TK54; -.
DR   VEuPathDB; TriTrypDB:TRSC58_06589; -.
DR   VEuPathDB; TriTrypDB:TRSC58_07107; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006412; P:translation; IEA:InterPro.
DR   CDD; cd01803; Ubl_ubiquitin; 1.
DR   Gene3D; 4.10.1060.50; -; 1.
DR   InterPro; IPR001975; Ribosomal_eL40_dom.
DR   InterPro; IPR038587; Ribosomal_eL40_sf.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR10666:SF437; POLYUBIQUITIN-B; 1.
DR   PANTHER; PTHR10666; UBIQUITIN; 1.
DR   Pfam; PF01020; Ribosomal_L40e; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01377; Ribosomal_L40e; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
SQ   SEQUENCE   128 AA;  14640 MW;  6CF17F6F62A7B6B6 CRC64;
     MQIFVKTLTG KTIALEVEAS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EEGRTLADYN
     IQKESTLHLV LRLRGGVMEP TLVALAKKYN WEKKVCRRCY ARLPVRATNC RKKACGHCSN
     LRMKKKLR
//
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