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Database: UniProt
Entry: A0A093XDE0_9PEZI
LinkDB: A0A093XDE0_9PEZI
Original site: A0A093XDE0_9PEZI 
ID   A0A093XDE0_9PEZI        Unreviewed;       757 AA.
AC   A0A093XDE0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   18-JUN-2025, entry version 44.
DE   RecName: Full=Ubiquitin-like domain-containing protein {ECO:0000259|PROSITE:PS50053};
GN   ORFNames=V490_06322 {ECO:0000313|EMBL:KFX90695.1};
OS   Pseudogymnoascus sp. VKM F-3557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Thelebolales; Thelebolaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX90695.1, ECO:0000313|Proteomes:UP000029320};
RN   [1] {ECO:0000313|EMBL:KFX90695.1, ECO:0000313|Proteomes:UP000029320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX90695.1,
RC   ECO:0000313|Proteomes:UP000029320};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the 60S subunit of the ribosome.
CC       {ECO:0000256|ARBA:ARBA00002241}.
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. eL40 is essential for translation of a subset of cellular
CC       transcripts, including stress response transcripts, such as DDR2.
CC       {ECO:0000256|ARBA:ARBA00045962}.
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: Belongs to the eIF-5A family.
CC       {ECO:0000256|ARBA:ARBA00006016}.
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}.
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:KFX90695.1}.
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DR   EMBL; JPJS01001847; KFX90695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093XDE0; -.
DR   STRING; 1437433.A0A093XDE0; -.
DR   HOGENOM; CLU_016553_0_1_1; -.
DR   OrthoDB; 1082at34379; -.
DR   Proteomes; UP000029320; Unassembled WGS sequence.
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:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0045901; P:positive regulation of translational elongation; IEA:InterPro.
DR   GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR   CDD; cd01803; Ubl_ubiquitin; 1.
DR   FunFam; 2.30.30.30:FF:000007; Eukaryotic translation initiation factor 5A; 1.
DR   FunFam; 3.10.20.90:FF:000014; Ubiquitin-60S ribosomal L40 fusion; 1.
DR   FunFam; 4.10.1060.50:FF:000001; ubiquitin-60S ribosomal protein L40; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 4.10.1060.50; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR   InterPro; IPR001884; IF5A-like.
DR   InterPro; IPR048670; IF5A-like_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR001975; Ribosomal_eL40_dom.
DR   InterPro; IPR038587; Ribosomal_eL40_sf.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   InterPro; IPR048538; Rrn7_cyclin_C.
DR   InterPro; IPR048540; Rrn7_cyclin_N.
DR   InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
DR   InterPro; IPR020189; Transl_elong_IF5A_C.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   NCBIfam; TIGR00037; eIF_5A; 1.
DR   PANTHER; PTHR11673; TRANSLATION INITIATION FACTOR 5A FAMILY MEMBER; 1.
DR   Pfam; PF01287; eIF-5a; 1.
DR   Pfam; PF21485; IF5A-like_N; 1.
DR   Pfam; PF01020; Ribosomal_L40e; 1.
DR   Pfam; PF20645; Rrn7_cyclin_C; 1.
DR   Pfam; PF20644; Rrn7_cyclin_N; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01376; eIF-5a; 1.
DR   SMART; SM01377; Ribosomal_L40e; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR   PROSITE; PS00302; IF5A_HYPUSINE; 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   Elongation factor {ECO:0000256|ARBA:ARBA00022768};
KW   Hypusine {ECO:0000256|ARBA:ARBA00023071};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029320};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          630..705
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   REGION          254..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..279
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  85375 MW;  CF8852377E5B7B83 CRC64;
     MASADQQDYS IDSADAGASL TYPMQCSALR KGGHVLIKQR PCKIIDMSTS KTGKHGHAKV
     HLVAEDIFTG KKLEDLSPST HNMDVPNVTR KEYALLGVDD GFLNLYDEAT GQTKDDIKVP
     EPIGGDDKRA EMLKRLADIT DDDDKEGVVI IISAMNENAC IEVKEEGFTQ VAADEDDFNT
     EGRKTRKRRK EVAETGIVYD GIEAIKLYAQ CWQVVLRKQA MWLISSRGMP PELETVIRDL
     WAVRIRSIRG VGEDERDVRD GSGFSSTSEG ETEGEDDGIG IEMSRRHRKI AREKGLPKLI
     ESLALCYMAM LLLRLPVSVG DLQKWAEQHE IPYFRVIQDI PADMRSHLPP KYYSALETRS
     SLRRGRLQQC IGELMLNFTT NFNILFPPLN TPLLIFRFVK ELCLPLEIYG SCFQLAEALG
     IRFQYPKILS RHKLSEYPEL QVAALVVIST KLLQPFDKMI RSPESLKDPS ALRVDWDEWS
     GMVTEGGDST VGQEAKVSEA DVFNMSGDML DRYLDWYYRT WSGGRDSKVS QQILDLFPIE
     DSPNLHDNYQ EIATPMSEHL GRVQSRLKVQ KPVSANDEQY VATINRPGAC YTRWQRDGDL
     SANEKVFVAK TAENAGTTVD ILIRTTIAIM QIFVKTLTGK TITLEVESSD TIDNVKSKIQ
     DKEGIPPDQQ RLIFAGKQLE DGRTLSDYNI QKESTLHLVL RLRGGIIEPS LKALASKFNC
     DKMICRKCYA RLPPRATNCR KKKCGHTNQL RPKKKLK
//
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