ID A0A1E3NP18_9ASCO Unreviewed; 401 AA.
AC A0A1E3NP18;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=UEV domain-containing protein {ECO:0000259|PROSITE:PS51322};
GN ORFNames=PICMEDRAFT_119935 {ECO:0000313|EMBL:ODQ47817.1};
OS Pichia membranifaciens NRRL Y-2026.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ47817.1, ECO:0000313|Proteomes:UP000094455};
RN [1] {ECO:0000313|EMBL:ODQ47817.1, ECO:0000313|Proteomes:UP000094455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ47817.1,
RC ECO:0000313|Proteomes:UP000094455};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000256|ARBA:ARBA00009594}.
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DR EMBL; KV454002; ODQ47817.1; -; Genomic_DNA.
DR RefSeq; XP_019018930.1; XM_019159863.1.
DR AlphaFoldDB; A0A1E3NP18; -.
DR STRING; 763406.A0A1E3NP18; -.
DR GeneID; 30176550; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000094455; 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-KW.
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; 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; 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:UP000094455};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 3..175
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT REGION 167..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43973 MW; 5B3DA2C58750929E CRC64;
MQAVLNWLYA AVQPLYANPI LTYQDVSLVL SVFQDVRIRT EVANGALLLK LYTVQDAADT
ADAAAGLRLL AAASPPLGVQ VYLPRDYPQS PPVVLLAPAD SKSHTLAAST YLTQAGTFTH
PLLDAWTYTH ANSRSNDGVP PRENRLLVLF YTLHRLIAEH PSIWVQRIPS LPPKPSRTLP
AAPTRAPAPT TPAESPAVTS RVPPPLPPPP SSSSEKTTAT ASPASSSTAL PPQLPPNPIR
QALIRNASER LNAELLTLLN GSSQYSPLPP ISTVLENQRK LVASYDTFNR TAKSIEGIST
SLGTNTPVVE LKSAEASALI EKVRNYVDSD YNHEENLLLP LDSRSKQLHD LCFREASQMD
SLHFLELLFN TQKISFTDYV ENVRKVSRER AKVLIWINKF N
//
