ID W2S6U5_9EURO Unreviewed; 528 AA.
AC W2S6U5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=UEV domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1541_02823 {ECO:0000313|EMBL:ETN43664.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN43664.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN43664.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN43664.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000256|ARBA:ARBA00009594}.
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DR EMBL; KB822718; ETN43664.1; -; Genomic_DNA.
DR RefSeq; XP_008715400.1; XM_008717178.1.
DR AlphaFoldDB; W2S6U5; -.
DR STRING; 1220924.W2S6U5; -.
DR GeneID; 19970162; -.
DR VEuPathDB; FungiDB:HMPREF1541_02823; -.
DR eggNOG; KOG2391; Eukaryota.
DR HOGENOM; CLU_017548_2_1_1; -.
DR InParanoid; W2S6U5; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0072666; P:establishment of protein localization to vacuole; IEA:UniProt.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:UniProt.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR Gene3D; 6.10.140.820; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR017916; SB_dom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR008883; UEV_N.
DR PANTHER; PTHR23306:SF3; TUMOR SUPPRESSOR PROTEIN 101; 1.
DR PANTHER; PTHR23306; TUMOR SUSCEPTIBILITY GENE 101 PROTEIN-RELATED; 1.
DR Pfam; PF05743; UEV; 1.
DR Pfam; PF09454; Vps23_core; 1.
DR SUPFAM; SSF140111; Endosomal sorting complex assembly domain; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51312; SB; 1.
DR PROSITE; PS51322; UEV; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 9..155
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 461..528
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 149..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..335
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 58729 MW; C24FED753CE2221C CRC64;
MAQVPQSTLR YLYYDVLKVQ PYRDPNRTYS DLVSTLQKYP AIAVKGTKEY VYDNGRPELL
LHLGGVLPVS FRGTLYHFPI LIWIPYAYPY DAPMIYVDPK DDIVVNPGQH VAPDGRVYHS
YLAHWRDTWE RSNVVDFLSI LSDVFAKEPP VRARSGRPPA RQQQQQQQHQ PPPPPRPPLP
HEAQSPAPAS PRPQDAPPPP PPKEPAGAYG SASSPAQPKP SRYDAPLPLP SQTRSPRPTS
MYQQSPQAMP QSRPQSQYMP QRASSLRQSH PPQNWQQQSQ PQQQPPYPPN QQTQPNNYQT
SSPPHQQPPL GPYPPQHQIT PQQPLPQPKQ PPPDLLDSPF DLALPSSTPA NLPAPPIPRN
PEKDALLSHL SASITTNLHN LISQNQSQIA PLQSQHSAIQ QSQHQLQSEL SQLQTLHAAL
TSNITDLQSS LAKADHTISD AQSRSGKGDI PPVDGMLITP HVVSTQLYNV VAEERGIEAA
ILALQDAFTR GRVGSEVWGR KTRELARDGF RRRWVARKVG RGMGLDGA
//