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Database: UniProt
Entry: G7E7L5_MIXOS
LinkDB: G7E7L5_MIXOS
Original site: G7E7L5_MIXOS 
ID   G7E7L5_MIXOS            Unreviewed;      1118 AA.
AC   G7E7L5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=U-box domain-containing protein {ECO:0000259|PROSITE:PS51698};
GN   Name=Mo05513 {ECO:0000313|EMBL:GAA98825.1};
GN   ORFNames=E5Q_05513 {ECO:0000313|EMBL:GAA98825.1};
OS   Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC   Mixiales; Mixiaceae; Mixia.
OX   NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA98825.1, ECO:0000313|Proteomes:UP000009131};
RN   [1] {ECO:0000313|Proteomes:UP000009131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC   {ECO:0000313|Proteomes:UP000009131};
RX   PubMed=21478649; DOI=10.2323/jgam.57.63;
RA   Nishida H., Nagatsuka Y., Sugiyama J.;
RT   "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL   J. Gen. Appl. Microbiol. 57:63-67(2011).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
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:GAA98825.1}.
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DR   EMBL; BABT02000165; GAA98825.1; -; Genomic_DNA.
DR   RefSeq; XP_014566998.1; XM_014711512.1.
DR   AlphaFoldDB; G7E7L5; -.
DR   STRING; 764103.G7E7L5; -.
DR   GeneID; 26268993; -.
DR   eggNOG; KOG2042; Eukaryota.
DR   HOGENOM; CLU_003224_2_1_1; -.
DR   InParanoid; G7E7L5; -.
DR   OMA; FKMLPEY; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009131; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13931:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 1.
DR   PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009131}.
FT   DOMAIN          1036..1110
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          24..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1118 AA;  125680 MW;  09A7695CD8FDBB50 CRC64;
     MADAQSDADK IRLKRIERLA ALAAKAPSDD AAPSSSPTSQ NGASKPADPA GTLKRIRPDS
     QASVRTPAGS AKPTDAPVAS TSKLATSEPA IVQRPSESTT VSFPEPFDSW QSAALARILN
     VTLDIATAEK SNWEIVYLKQ LRTELIEEDS RQRDPALYVV APSEQMTDGD SENGNAERAI
     LARLALDPTD MSDDPEEITV LAGMSQISPF EYLVGAWQRS NEERAKIANG VRGKVFDPTE
     TSKRLHVLER IRQLLISYIG LDLQETSIFV QPDGQDVGDI ELFNLMLNKH QSLRLTPGQL
     TVLLGELAKR FEDDGLEDLI GAVARRLSLN MFQNRKVYSL GNMDAPGAWQ QSFAALRLLT
     SNKTIASTFA SLPQFDPDAE PRFMQMTSLL GPFDQISVFP DDAPEVANEF FNNEEAADLE
     DNETHDGQSG SLRRMLASVQ SELFSVYNDL IRSSPKAREN VLNHWAHIAN QNAKRSAIQQ
     DKMRIASDGV MINLQTVLTQ FAEPFMDASY SKMDKIDIEY YLKCRRLDIR EETKINATQQ
     EADDYYALAD GQPAPGANFI SDIFFLSAAY LHLGLMSALS QHKRSIKDYG RFKDHLAELR
     EAAESHRSNA PLYARYQAAI EKLRHQMRGI SASQCQLHSP AFLNSQATFC NFMTVWLVRA
     MDPQHKHPQT AITLPLPTEP PISFKMLPEY LVDDVTEFFT YVSRYRPDVM SQLRLDDLVT
     FIIVVLSTPY VKNPFLKSKF VEILFYNTRR QTRRDGHDGV LGPIINTHPL ALSNLMGALI
     HTYVEIESTG SHTQFYDKFN TRFYISLIFR VVWHNAEHRE ALKREAGDTK RFVRFCNLLL
     NDTTFLLDES LGKFSLIKEL DKLMADSAAW SALTEEERKA KSKEKADYEG QAQSYLQLVY
     ESVGLLRVFT EETTAPFVRG EIVDRLAAML DNNLDVLAGP RCKDLKIANA DKIKFRPREL
     LADILQVIMN LSRRVEFATA VARDGRSYSR ELYYRAAGIA VRAALKTEQE MDELRKFVDQ
     VEQIAADDRD DEAGEDVPEE FMDPLTYTIM RDPVLIPKSN NILDRTSISQ HLLSEATDPF
     TRQPLTIEEC VPAVDLKSRI DAFLQAKRDA RALGHATT
//
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