ID A0A1Q5QBH5_9EURO Unreviewed; 584 AA.
AC A0A1Q5QBH5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=UEV domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=UA08_01686 {ECO:0000313|EMBL:OKL63266.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL63266.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL63266.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL63266.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) 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:OKL63266.1}.
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DR EMBL; LFMY01000002; OKL63266.1; -; Genomic_DNA.
DR RefSeq; XP_020123387.1; XM_020261377.1.
DR AlphaFoldDB; A0A1Q5QBH5; -.
DR STRING; 1441469.A0A1Q5QBH5; -.
DR GeneID; 31001441; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000214365; 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:UP000214365};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 14..159
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 508..576
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 153..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 63467 MW; 91C9391E2752AB73 CRC64;
MAAVPQSTLT WLWNVLAKNH YDPKQTYRDP NRTYHDVARA LAQYPSFGPR TDVYTSENGT
PSLLLHLAGT LPVSFRGAVY NIPIDTWVPT AYPLEAPIVY VSPTPDMLVR SGQHVTLEGR
VYHHYLAHWH EAWDRSSIVE LFAILREVFA KEPPVKHRPP RATPPTQPGA PPPLPPLPPE
ISASPQPIEL PAIDNRQAPP RPPQLPPKPG QAPPVHSPPP ASRGSGPAVP PLPPKAQIPQ
RQDYIYSHNG SPPANAATAQ PYRSSSMRTT QIPQQLPTTP TTPNYQREPY IHSPSPVPLQ
SINTAQHMQS PRQFSGQSFQ QQQQYPPYTA VPKQSSQYHQ PSYQNTPQKT ATASRNPGTP
DLLTSPFDVE LPSIAPAGPP PPVPPNPEKD ALLHTISRTL TETLQGNVSQ SASAAISLQS
QSQALASAMI TLQSEISTLN NYQAAIQSNI NILQQSLHRA DAVIADAKAR ASRKPSSAHN
TPPPDQTGAV SVADGGLPPI DEVLVAPTVV GKQLYDLVAD ERGIQQAIYA LQAALVKGVI
GADTWSRHTR SLAREAFIKR ALIRKIAQGM GLDLGEAHEL KTDV
//
