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Database: UniProt
Entry: A0A081CGY5_PSEA2
LinkDB: A0A081CGY5_PSEA2
Original site: A0A081CGY5_PSEA2 
ID   A0A081CGY5_PSEA2        Unreviewed;       662 AA.
AC   A0A081CGY5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Related to Tumor susceptibility gene 101 protein {ECO:0000313|EMBL:SPO45564.1};
GN   ORFNames=PAN0_010d4153 {ECO:0000313|EMBL:GAK65931.1}, PSANT_03250
GN   {ECO:0000313|EMBL:SPO45564.1};
OS   Pseudozyma antarctica (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK65931.1, ECO:0000313|Proteomes:UP000053758};
RN   [1] {ECO:0000313|Proteomes:UP000053758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA   Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA   Morita T.;
RT   "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT   JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT   Lipids.";
RL   Genome Announc. 2:e00878-e00814(2014).
RN   [2] {ECO:0000313|EMBL:GAK65931.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK65931.1};
RA   Morita T., Saika A., Koike H.;
RT   "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT   as a producer of lipase B which used in a wide range of industrial
RT   applications.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SPO45564.1, ECO:0000313|Proteomes:UP000325008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC   {ECO:0000313|EMBL:SPO45564.1};
RA   Guldener U.;
RL   Submitted (MAR-2018) 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; DF830077; GAK65931.1; -; Genomic_DNA.
DR   EMBL; OOIQ01000006; SPO45564.1; -; Genomic_DNA.
DR   RefSeq; XP_014656093.1; XM_014800607.1.
DR   AlphaFoldDB; A0A081CGY5; -.
DR   GeneID; 26304980; -.
DR   HOGENOM; CLU_017548_2_0_1; -.
DR   OrthoDB; 37962at2759; -.
DR   Proteomes; UP000053758; Unassembled WGS sequence.
DR   Proteomes; UP000325008; 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:UP000053758};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          4..149
FT                   /note="UEV"
FT                   /evidence="ECO:0000259|PROSITE:PS51322"
FT   DOMAIN          597..662
FT                   /note="SB"
FT                   /evidence="ECO:0000259|PROSITE:PS51312"
FT   REGION          144..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..218
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..421
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   662 AA;  70848 MW;  DD7BD7F5D6C0883B CRC64;
     MDHAVVQRWL RSVLGPYNDR DRVYADVDRA LIAVSSLSPK TEVFTFNDGR TQLLLTLEGT
     VPVEFRTTTY NIPVAYWIPR DYPREPPMAF VAPTPDMAIR KGPNVDPSGQ IGGNYIARWR
     SKPEACNLLD LIHDCQHMFG REPPVYAKPK PTPVYATAAS SQQRSQPSTP QQGSSANPLA
     QPPGPSLPAS PRSPQVVGSP SLEARQRPPP PPPGPGSAHH DHPQGSSTPQ RPPKPSSSMG
     FDRSGFHSPR SSSSHFDPHQ SPAPLPALQI QSPHTFGHPP GAGSDVNRRA SGGAYGPGAH
     QAPFGAPSPQ AHFAPADRTQ TRIESSHSPV SPSHRPAYAD GRPYAYGHQS TPQQHPPTRA
     QTYPYPTQEP HPSHTQYGNE AAQAGGRQPA YSGAPGAQSY AQPGLPPANG GGPPPVPGPH
     PYASGSVSQA PNPAAVAVAD RNGVPARPTA APRPKSVNLL DDEDSALGIS DTRGQANGFA
     SAGGPTSAGS SAPPPPRPIN PELLALHERV YSKIDQRLVT LSSTLQASNQ RLEVLSSDLD
     RGLPAIEDEM SRLKAVRDVC KITGDRLQGS VDEITESVRS IHARDDPDPD SMVLATSIVG
     NQLVDLVAED NAIEDTLYHL GRALNAERID LDRFLKQTRM LAREQFMKRA LAHKISEGMG
     WS
//
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