ID RL40_TRYCR Reviewed; 128 AA.
AC P14795; P08565;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 08-NOV-2023, entry version 71.
DE RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000305};
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=Large ribosomal subunit protein eL40 {ECO:0000305};
DE AltName: Full=60S ribosomal protein L40;
DE AltName: Full=CEP52;
DE Flags: Precursor;
GN Name=FUS1;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=CL;
RX PubMed=2841110; DOI=10.1002/j.1460-2075.1988.tb02921.x;
RA Swindle J., Ajioka J., Eisen H., Sanwal B., Jacquemot C., Browder Z.,
RA Buck G.;
RT "The genomic organization and transcription of the ubiquitin genes of
RT Trypanosoma cruzi.";
RL EMBO J. 7:1121-1127(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2457589; DOI=10.1016/s0021-9258(18)37809-8;
RA Kirchhoff L.V., Kim K.S., Engman D.M., Donelson J.E.;
RT "Ubiquitin genes in trypanosomatidae.";
RL J. Biol. Chem. 263:12698-12704(1988).
CC -!- FUNCTION: [Ubiquitin]: Exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is conjugated
CC to target proteins via an isopeptide bond either as a monomer
CC (monoubiquitin), a polymer linked via different Lys residues of the
CC ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC initiator Met of the ubiquitin (linear polyubiquitin chains).
CC Polyubiquitin chains, when attached to a target protein, have different
CC functions depending on the Lys residue of the ubiquitin that is linked:
CC Lys-48-linked is involved in protein degradation via the proteasome.
CC Linear polymer chains formed via attachment by the initiator Met lead
CC to cell signaling. Ubiquitin is usually conjugated to Lys residues of
CC target proteins, however, in rare cases, conjugation to Cys or Ser
CC residues 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 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Large ribosomal subunit protein eL40]: Component of the 60S
CC subunit of the ribosome. {ECO:0000250}.
CC -!- SUBUNIT: [Large ribosomal subunit protein eL40]: Part of the 60S
CC ribosomal subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquitin is synthesized as a polyubiquitin precursor
CC with 5 or 6 exact head to tail repeats. Some ubiquitin genes contain a
CC single copy of ubiquitin fused to a ribosomal protein.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eL40 family. {ECO:0000305}.
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DR EMBL; X07451; CAA30333.1; -; Genomic_DNA.
DR EMBL; X07452; CAA30335.1; -; mRNA.
DR AlphaFoldDB; P14795; -.
DR SMR; P14795; -.
DR VEuPathDB; TriTrypDB:BCY84_04472; -.
DR VEuPathDB; TriTrypDB:C3747_16g221; -.
DR VEuPathDB; TriTrypDB:C4B63_138g31; -.
DR VEuPathDB; TriTrypDB:ECC02_012811; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0110010; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0110090; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM07171; -.
DR VEuPathDB; TriTrypDB:TcG_06155; -.
DR VEuPathDB; TriTrypDB:TcYC6_0037180; -.
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; 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 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114829"
FT CHAIN 77..128
FT /note="Large ribosomal subunit protein eL40"
FT /id="PRO_0000138772"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 128 AA; 14658 MW; A5CA0F709902E544 CRC64;
MQIFVKTLTG KTIALEVESS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGVMEP TLEALAKKYN WEKKVCRRCY ARLPVRASNC RKKACGHCSN
LRMKKKLR
//
