ID   A0A164V0I9_9AGAM        Unreviewed;      1094 AA.
AC   A0A164V0I9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=U-box domain-containing protein {ECO:0000259|PROSITE:PS51698};
GN   ORFNames=SISNIDRAFT_474241 {ECO:0000313|EMBL:KZS93704.1};
OS   Sistotremastrum niveocremeum HHB9708.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX   NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS93704.1, ECO:0000313|Proteomes:UP000076722};
RN   [1] {ECO:0000313|EMBL:KZS93704.1, ECO:0000313|Proteomes:UP000076722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB9708 {ECO:0000313|EMBL:KZS93704.1,
RC   ECO:0000313|Proteomes:UP000076722};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR   EMBL; KV419406; KZS93704.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164V0I9; -.
DR   STRING; 1314777.A0A164V0I9; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000076722; 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   CDD; cd16657; RING-Ubox_UBE4A; 1.
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:UP000076722}.
FT   DOMAIN          997..1071
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..69
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1094 AA;  123761 MW;  398F91E51117B139 CRC64;
     MSEQPTPQEE ADRIRLKRLA KLGGSASSSP APSNPTANAS TSSTPHPPLQ APVQKPAPRP
     QPVQPVPTPV STPTKKANVV QAPVALTNRA AWEEGLVETV FLVTIDREKG VRMGYKLLWL
     KSLKEDLESE RAEVHLSAQI VDSVLISRLE VDPKTPSADP SYQPFLDHIS PKTTVFEYLF
     GCWRRLVLAR RSLPKKYRAE DVSAVQPTLD KLRDLIISYI GLNMQDPTMF PQPEGTTGGS
     LELYESLLSL NSSSHPFAST STQAGLVNID EFPLFLTDLQ RRFQTADEDV LDEILGPVVR
     LLTFSSWLAR PEGLASGDNG WRSIVTGLEA LMSNKGIAKM VTKLEEWCPE NASASSFERS
     SLLGPLIRLG VFQREWPTIS KTYFSEPEKR TRADVDASNT SLRATLHNLQ TSLFQLFNSI
     VRASPESRES VLEYFSKVIS LNVKRRGLQV DFATVASDGF MVNLQAVLLQ FAEPFIDSKF
     SKLDRIDPKF FGRSSRISMA EETRVNATSD EASRWAEEVQ SESQGPANFI TEIFYLTATI
     NHYGLMRTIQ SAQDLHKAID ERQNVIDRYE GDPTWREQPM KRIKDEMQLI HEEMFAYQVQ
     LLDPEFSARQ LAFNGFLSTW LINLVDPSKN HPTITIELPL PQEIPTVFKM IPEFFIEDIA
     DYALYLMRLK PDAIEKPARV EILNLCFTFL SSTWYIKNPF LKTRLVQVMF YGTLGYGRER
     EGILTELLNS HPLSLKHLMS ILTGFYIEVE STGSHTQFYD KFSARDIAYI LKAVWNNPAH
     RDALKRESLN LDKFVRFINL MMNDVTFLLD ESVSKLTEIH NIEIEMAAPD WEGKPLRHKQ
     ERIQTLSSIG QQATSWSALG KSTVDLLKKF THETKTPFMT PEIVDRLAAM LNYNLDALVG
     PKCQDLKVKD MDKYQFNPRQ LLSDILQVYI NLSGEGTFVQ AIAGEGRSYK KELFERAAGI
     AKKRGLKTDM EIEQLRLFVV KVEETRATLQ AEDDLGEIPD EYLDPLMYTV MRDPVILPSS
     RTVIDRSTIK AHLLSDTTDP FNRVPLKLED VVPDHELKAK IEGFLAERRR KGGALDVAPE
     DVMQIDENAD AMHM
//