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Database: UniProt
Entry: A0A2V1AYX7_9ASCO
LinkDB: A0A2V1AYX7_9ASCO
Original site: A0A2V1AYX7_9ASCO 
ID   A0A2V1AYX7_9ASCO        Unreviewed;       524 AA.
AC   A0A2V1AYX7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=UEV domain-containing protein {ECO:0000259|PROSITE:PS51322};
GN   ORFNames=CXQ85_003011 {ECO:0000313|EMBL:PVH23277.1};
OS   [Candida] haemuloni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH23277.1, ECO:0000313|Proteomes:UP000244309};
RN   [1] {ECO:0000313|EMBL:PVH23277.1, ECO:0000313|Proteomes:UP000244309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B11899 {ECO:0000313|EMBL:PVH23277.1,
RC   ECO:0000313|Proteomes:UP000244309};
RA   Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA   Litvintseva A.P.;
RT   "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT   Patient with Chronic Leg Ulcers in Israel.";
RL   Submitted (DEC-2017) 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:PVH23277.1}.
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DR   EMBL; PKFO01000010; PVH23277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1AYX7; -.
DR   STRING; 45357.A0A2V1AYX7; -.
DR   EnsemblFungi; CXQ85_003011-t46_1; CXQ85_003011-t46_1-p1; CXQ85_003011.
DR   VEuPathDB; FungiDB:CXQ85_003011; -.
DR   OrthoDB; 37962at2759; -.
DR   Proteomes; UP000244309; 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; 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; 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:UP000244309};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          7..167
FT                   /note="UEV"
FT                   /evidence="ECO:0000259|PROSITE:PS51322"
FT   REGION          159..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          370..432
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        166..187
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..223
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..275
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  58161 MW;  1ACC3B63B90991F5 CRC64;
     MAKISSKVAN WLYSVLQPQY LHKEIAYSHL YHFLSAYLPE GFKIRTAVYT SVSGHSQLLI
     NLYGNLDCGT CLVPLNIWIP LNYPFQDENI PSHEPNGVPE VFVVPEHGLV IRPNNNVDSQ
     GRFYHPFIAS WHQNYTPTSS TKQFSLLSLM GCLKATFEQT PPLDTRPSPS AAPSGPPAPP
     KVLPNQTGPQ LPPKRAYNEP EQAKSPTPVA QTPEPPRRET TGPPLPQKPI SRQATQDTSI
     PEKYRMPLPL PGENVPTPPP AQQPVSPPSF QHPISPPSFQ RPFGSPQYER PVHAPVQATG
     PAYIEDDSDI YEPHRPQSVK PSAIAEVEDL MDKVTVNETK NDKPILQELS AKVNAFLESE
     ESVFQAMPFV EEQKAKVNAL HSQLSNHLKQ AQANDENLQK HVSYLSGQIE AVKRLNGELQ
     QLDQINAQSK DEISTGTAPG QSIKLDDLIT PDSILVNQLY ETVADIKAHK DTIDLVGGNF
     KGEKEVINDE NMDTCIKSVR GLARELFWLE VTKSEIGKSM GLRM
//
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