ID Q0CS33_ASPTN Unreviewed; 592 AA.
AC Q0CS33;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=UEV domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATEG_03501 {ECO:0000313|EMBL:EAU36775.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU36775.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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; CH476597; EAU36775.1; -; Genomic_DNA.
DR RefSeq; XP_001212679.1; XM_001212679.1.
DR AlphaFoldDB; Q0CS33; -.
DR STRING; 341663.Q0CS33; -.
DR EnsemblFungi; EAU36775; EAU36775; ATEG_03501.
DR GeneID; 4317662; -.
DR VEuPathDB; FungiDB:ATEG_03501; -.
DR eggNOG; KOG2391; Eukaryota.
DR HOGENOM; CLU_017548_2_1_1; -.
DR OMA; GTVYKFP; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000007963; 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:UP000007963};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 14..159
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 525..592
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 159..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 64376 MW; 95593EA508946CD1 CRC64;
MAAVPQRTLN WLYSVLIRDH YDPRQTYQDP NRTYSDVANV LAQYPSLSPR TEVYTYENGF
SALLLQLSGT VPVSFRGTIY KFPITLWVPN TYPRDPPLVY VTPTQDMAVR VGQHVTLEGR
VYHHYLAHWT EAWERSSLVD LLLILREVFA KEPPVKYKQH QALPVQPPQP RHVPTPPPLP
PLPPELGVST SRSPTVQNAP SPQTASPVPP APPPKPGQMV AAEPRQATQV IHQGPPSSMP
PLPPKEQVPR PQSFHPHAGF TSPANRASQY LPGQTDAAPG PSIQHHFPQQ QQHHSMGQAI
SLHPQGQAPF RADGGISTSP TPQTLQGPPQ QPPYVSGQQP LPHPAYQQPN GRFPQSPLPP
SHPSPHYGAP PPVPTTQPAP RPKPEQVDLL TSPFEVELPS IAPTGPAPPI PPNPEKDALL
HAVSKTLAQT LQTNIAQSES AAHSLQSQSH SLHAAIATLQ GEISSLKDFN ATLQSNTSIL
QQSLHRADGV IADAQSRIAS SNPQASTDPV ASGLPSVDEI LVAPTVVGKQ LYDLVAEERG
IQQAIYALQA ALVKGVIGVE TWSRHTRGLA REAFLKRALI RKIGRGMGLE EY
//
