ID A0A1V8S9B4_9PEZI Unreviewed; 568 AA.
AC A0A1V8S9B4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=UEV domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A48_18242 {ECO:0000313|EMBL:OQN95643.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN95643.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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:OQN95643.1}.
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DR EMBL; NAJO01000083; OQN95643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8S9B4; -.
DR STRING; 1507870.A0A1V8S9B4; -.
DR InParanoid; A0A1V8S9B4; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000192596; 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:UP000192596};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..151
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 501..568
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 147..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 61725 MW; A1EBCF8876C846A1 CRC64;
MAQVPEKVLS WLYSVLHEYQ DPQRAYSDIA HTLASFPSLS PRTEVYTYET GGSALLTTVT
GTLPVNFRGT LYRFPVKLWI PLSYPQEAPI VYVTPGKEML VRPGQHVGVD GRVYHPYLRD
WSVMWDRASV VDFLGYLQQA FAREPPVISK AQQQQYRRAS PPRGQQPPRS QGAGPPVLPP
KQLPGAAPPV EMPAASTPPP RPPKPGKGPV YAPTVSSRDV QRDGPPLPPL PGQALPAVQH
QRAQYAGPNG HPTHAQRPYD QWQSNGQPPP APYAQQAQPQ MYRPQRNESP VSPVEAPHGY
GGPRARHPSQ AAQPVYDSRY GPGQPGPSRQ PGSAMSPPQT HPQPPGPRHQ GQYPQSQPSG
PQYGQQYPPQ PKPPQAPQDL LSDPFDIPIL TSGPAAPAPP IPPNPEREHL HHAISNSLVS
QAQDAVSRNL AAISPLQAQH SALLAAHANL QAELTALSHL DQNLASNESI LYKSIADCDA
RITASKKKPL PPIDEVLVAP NLVSQQLWTL CAEEAAAREA MECLQRALDK GRIGAGEFVR
LMRGLGRERF GKTVLARKCA RGLGLEAG
//