ID A0A1G4MFQ7_LACFM Unreviewed; 447 AA.
AC A0A1G4MFQ7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=LAFE_0F09648g1_1 {ECO:0000313|EMBL:SCW02581.1};
GN ORFNames=LAFE_0F09648G {ECO:0000313|EMBL:SCW02581.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW02581.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) 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; LT598490; SCW02581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MFQ7; -.
DR STRING; 4955.A0A1G4MFQ7; -.
DR OMA; GTVYKFP; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000190831; Chromosome f.
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, ECO:0000256|SAM:Coils};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 9..161
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 383..447
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 149..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 327..365
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 219..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 49717 MW; 1817C949C46D7D8C CRC64;
MESIELPPAV VNWLFKVLQP TYFDARTTFH DVACTLSTYK QLRPRTRVFT DIYGRSQLLL
CLYGKIGTEY PLPILIWIPT EYPIVAPLVY LDFESLQSPP VDLAGIVDSN GSLNLPTLSQ
WNSEHCNLLQ LVADLDNLRS DYFAIPTPLS NPSSPPIPSK EISVTPEIPE LPSKPPKPPI
KEPASLHANV DRLASEINNV SITGQSPALP PRPNFSLPST PQPLSNIPTG GASVSSNDIS
LSRTSPCVPA ADSKLANAVS VSQQFQQPDL MDLGTETSED PVHVKKIQEL QNTLNKMAHS
DQDTIQESLG SRVLSIKVAA DQFETIYRHE SASLDNLEQQ IEEGKKLLTK EVEETDKELK
RAREYIQNYG PPVDMSTILT TDREGLNQLY SLLAKDHAIT DTIHTLNEML GTDDVDFDVF
LKKVRSLARE QFLTRFHINK ILSTVNK
//
