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Database: UniProt
Entry: A0A1B9IDS8_9TREE
LinkDB: A0A1B9IDS8_9TREE
Original site: A0A1B9IDS8_9TREE 
ID   A0A1B9IDS8_9TREE        Unreviewed;       556 AA.
AC   A0A1B9IDS8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=ESCRT-I complex subunit TSG101 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=I206_01008 {ECO:0000313|EMBL:OCF53702.1};
OS   Kwoniella pini CBS 10737.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296096 {ECO:0000313|EMBL:OCF53702.1, ECO:0000313|Proteomes:UP000094020};
RN   [1] {ECO:0000313|EMBL:OCF53702.1, ECO:0000313|Proteomes:UP000094020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10737 {ECO:0000313|EMBL:OCF53702.1,
RC   ECO:0000313|Proteomes:UP000094020};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus pinus CBS10737.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000094020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10737 {ECO:0000313|Proteomes:UP000094020};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) 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; KI894007; OCF53702.1; -; Genomic_DNA.
DR   RefSeq; XP_019014921.1; XM_019152783.1.
DR   AlphaFoldDB; A0A1B9IDS8; -.
DR   STRING; 1296096.A0A1B9IDS8; -.
DR   GeneID; 30169377; -.
DR   OrthoDB; 37962at2759; -.
DR   Proteomes; UP000094020; 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; IPR000608; UBQ-conjugat_E2.
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; PS50127; UBC_2; 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:UP000094020};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          5..150
FT                   /note="UEV"
FT                   /evidence="ECO:0000259|PROSITE:PS51322"
FT   DOMAIN          19..178
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   DOMAIN          488..556
FT                   /note="SB"
FT                   /evidence="ECO:0000259|PROSITE:PS51312"
FT   REGION          145..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  62133 MW;  9B2E2F3B47C3055F CRC64;
     MSNLDLTREW LGNVTRPYQA KERVINETMK ILSEKRTLSV KTDAFTFDSG QTALLLLLHG
     TLPISYRGST YHIPINVWIP HDYPKSPPIL FVVPTKEMAI RKSKEVDPSG RVNENAVEYW
     WRSWPTQDLE TILKHLTSVF STVPPVYARP SESSSSSAQS SRSPISSPVQ PRIQSQAIGQ
     APQPPPPPAR PGYVPAKQTQ ESLPQYRPAP TPPPHTFTQQ GSHSRQSSAT YPGTPPQHPA
     SPQLTDRPDR IPQSQPQSPI SPSGIPRIPQ RPFIPQTQTQ PQVSFQPPRP DPISHQLGYP
     PHMNGQSPVH QQQLPQQYQQ QQVPQQYPPQ PIIPPHPSSQ LYPPQQIISQ SSHTMAAPRQ
     PIPDLLGSPE SSSLSLSSET APPIPPSKPP PPSLQHLHSI LLPHLQASLP PLIHHLQSTR
     IHLLERKEDL ESGEPAIKDE MSRLEAVKKV CDSTGKKLGD VVKSGEERIN ELEGKGEISV
     DELVCGISIV HNQLIDLVAE DNAIEDTIYH MTRALDAERV DLDRYLKSIR SLAREQYMKR
     ALIERILHGM GQTQRW
//
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