ID A0A436ZS07_9PEZI Unreviewed; 593 AA.
AC A0A436ZS07;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=UEV domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DFL_009517 {ECO:0000313|EMBL:RVD81665.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD81665.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD81665.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD81665.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) 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:RVD81665.1}.
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DR EMBL; SAEB01000012; RVD81665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A436ZS07; -.
DR STRING; 97331.A0A436ZS07; -.
DR VEuPathDB; FungiDB:DFL_009517; -.
DR Proteomes; UP000283090; 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:UP000283090};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..152
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 528..593
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 145..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 65685 MW; 80333978AD2FC6A8 CRC64;
MAELAPELLR WLSTVLAPKY HSANRAYTDT ATLLHHHRSL SPKTEVYTYD DGRSDLLLCI
HGTLPVAFRG ATYNIPLNIW VPHQYPDTPP TVMVVPGKNM GIRPTNHVDT NGRCYHPYLA
YWSQNPDKST LVDLCGQLKD VFGKEPPLYS KQPSPQPQPQ PIRSTATPPP RPPLPQEIEA
RRARPHPATQ PAEQAAPPPP PPPKAEPQHQ SAAAYSYTTT PHLFTPQNQP TPQPVASPPP
QNNNNQDRPA LPRKLPHEEP RPAYPIPGPS YQQTQPPPPP PVPPIPSPVR NSATGPPGPR
SPPPPPHSPY HRQHHIGSPP PPPVHPQHGW HPQPPPPQAH GPSGQYDPLN RFPIAVQPTN
QQQQRPISIH GYPPQQLPSA GPSNLNPSAA KLPQRSQSQR KPFNILDADD GAGTLPVPTS
KTAVPPPLPP NPEKDRLINE IARILQQKAE AASVKTVASL EQTASQAEAM AKTEAYMERE
RMELIRINDV CEKDQRILNE RIGMADELIR EVRDREAPNI DAVVVAPTVV HNQLYELVTD
DMAIEDTIYV LGKALDKERI TLDVFLKHTR ALAREQFTKR ALVKKISRQI GMT
//
