ID W9XA66_9EURO Unreviewed; 598 AA.
AC W9XA66;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=UEV domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O3_10286 {ECO:0000313|EMBL:EXJ77128.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ77128.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ77128.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ77128.1,
RC ECO:0000313|Proteomes:UP000019478};
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 Capronia epimyces CBS 606.96.";
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}.
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:EXJ77128.1}.
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DR EMBL; AMGY01000011; EXJ77128.1; -; Genomic_DNA.
DR RefSeq; XP_007738566.1; XM_007740376.1.
DR AlphaFoldDB; W9XA66; -.
DR STRING; 1182542.W9XA66; -.
DR GeneID; 19174366; -.
DR eggNOG; KOG2391; Eukaryota.
DR HOGENOM; CLU_017548_2_1_1; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000019478; 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:UP000019478};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..152
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 526..594
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 147..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 66024 MW; 4509C730D77A9DFE CRC64;
MAGVPQKTLG WLYNVLKREY HDPNRTYSDL AHVLARNPGL APRTDVYTFE NGTAALLVHF
QGTVPVDFRG SPYRIPISLW IPHAYPYEPP ICYVTPTEEM VIRPGQHVGG DGKIYHPYLA
HWRETWARCN VVDFLSILAD IFGREPPVMS RTSQDQQRPV QPTPPPVPPL PREIQHQQHP
PHPNMPVLSS PVQTGGPTPP PPPPPPKQPA QGIPNPSPTS PGSAYQRPGR YDAPPPVSQQ
PYGNGNLSGM NYLPQRSSSL RQSIPPPRRQ PQPYDRQAQQ QMPSLYQPGR PGEAQQYPPN
QPNQPPQVPG PSRSLGQGYE QGWPQGQTSL ERPVSQHYPP GQAPAPPRQP QNARPYPFPA
PHVQTQAQPP YQHQQQQQQH PQPVKPPPPP TPDLLDSPFD IALPTATGPG ASQTSNIPAP
PIPRNPEKDA LLTHLSHQIT QSLHSQIEQS GAALGPLSSQ HVAMQSTLQT LTAELNNLQS
LHSTLSSNIS LLSTSLSKSD GVIASARKRA QQNDIPLVDE MLVPPTVVAR QLYDAACEER
GIEAAILALQ EAFVRGRVAG DVWARRTRDL AREEFKRRWI ERKVATGMGL DLTVYSQE
//
