ID   A0A0L6VLQ3_9BASI        Unreviewed;       390 AA.
AC   A0A0L6VLQ3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=UEV domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VP01_145g3 {ECO:0000313|EMBL:KNZ61045.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ61045.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ61045.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ61045.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-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:KNZ61045.1}.
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DR   EMBL; LAVV01005110; KNZ61045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6VLQ3; -.
DR   STRING; 27349.A0A0L6VLQ3; -.
DR   VEuPathDB; FungiDB:VP01_145g3; -.
DR   OrthoDB; 37962at2759; -.
DR   Proteomes; UP000037035; 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:UP000037035};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..144
FT                   /note="UEV"
FT                   /evidence="ECO:0000259|PROSITE:PS51322"
FT   DOMAIN          310..382
FT                   /note="SB"
FT                   /evidence="ECO:0000259|PROSITE:PS51312"
FT   REGION          137..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..175
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..214
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  44579 MW;  AC1687417F02EFEB CRC64;
     MLKWLTQALL PYPHKELALN HIQVALHQFT TLSPKTESFT FDDGRTTLLL ALSGTIPVVY
     RALRYNLPIA IWFPFNYPFE PPIIYLTPTN DMIIKTSNNV DPNGKCLVNY LNLWQSKPEA
     CSLIQLLQSL QDIFSNDPPL YSKPKQQAPP YSSSPPPPPP PPPTEKYPPP LPPKLETSES
     STQQPNQNLL DDDPPDLTER NNLIPPPPRP PNPELLSLRQ TLHHKLQNEI YRLKTSLHKE
     QQQLDILETD LLKGEPAIRD EIARLDAVNL VCLNVADRYR LLIDQLDKRF NDLTLHRRIV
     DVDELVCSTT VLYNQLWELG INDKVIQDIL YHLSKALNNS MDGSKIDLDK FLKRVRVLGH
     EQFLIRANIN HISRLLGFQL SSSTTTRITG
//