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Database: UniProt
Entry: A0A0D8XKS6_DICVI
LinkDB: A0A0D8XKS6_DICVI
Original site: A0A0D8XKS6_DICVI 
ID   A0A0D8XKS6_DICVI        Unreviewed;       128 AA.
AC   A0A0D8XKS6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000256|ARBA:ARBA00035298};
GN   ORFNames=DICVIV_08744 {ECO:0000313|EMBL:KJH45203.1};
OS   Dictyocaulus viviparus (Bovine lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX   NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH45203.1, ECO:0000313|Proteomes:UP000053766};
RN   [1] {ECO:0000313|EMBL:KJH45203.1, ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH45203.1,
RC   ECO:0000313|Proteomes:UP000053766};
RA   Mitreva M.;
RT   "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX   PubMed=26856411; DOI=10.1038/srep20316;
RA   McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA   Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA   Sternberg P.W., Gasser R.B., Mitreva M.;
RT   "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT   lungworm biology and support future intervention.";
RL   Sci. Rep. 6:20316-20316(2016).
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   -!- 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; KN716420; KJH45203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D8XKS6; -.
DR   STRING; 29172.A0A0D8XKS6; -.
DR   Proteomes; UP000053766; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR10666:SF515; 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   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053766};
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;  14664 MW;  0190B972777F017B CRC64;
     MQIFVKTLTG KTITLEVEAS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGIIEP SLRQLAQKYN CDKQICRKCY ARLPPRASNC RKKKCGHSND
     LRIKKKLK
//
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