ID A0A165H873_9APHY Unreviewed; 625 AA.
AC A0A165H873;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=UEV-domain-containing protein {ECO:0000313|EMBL:KZT11380.1};
GN ORFNames=LAESUDRAFT_720609 {ECO:0000313|EMBL:KZT11380.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT11380.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT11380.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT11380.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000256|ARBA:ARBA00009594}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV427607; KZT11380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165H873; -.
DR STRING; 1314785.A0A165H873; -.
DR InParanoid; A0A165H873; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000076871; 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:UP000076871};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..151
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 545..613
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 148..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 68058 MW; 76605E7F322AC511 CRC64;
MGSTETLTQK WLRQNIQSYA NRDTVFAHVD AVLLRHPTIR PKTDVYTYDD GRTQLLLCLH
GLLPISFRGA SYNIPIAVWL TREYPRQPPI AYVVPTSDML VRASADVDVS GRCHIEYLYN
WDKKCEGCSL VELIEAMQDI FSRVPPVYAK PTRPSSSQSA PRPHVLGHDY SARPPPPLPG
TSSATTPQPA SPSNQNEERP PLPAKPGTSA TPYDRAPSVP PQRPRHNSRD RSPVVFGNTD
LEMRPPPPLP PHPPIAPGIS SYSSSPIPPI YTPRSSSASI ETATIALPSS SNLPRAPATP
VRAANHHLPM RVPHAAYLSG PSSSSPPPVP PVPHSILSQP FLGPERQAYS PPVSPAESTR
LSAPQPLLPP PFVSSPPFAD SHPLRRQIQH AAPPPTSIPP PAFSAPLPLP LPAPSNPPPD
LLDADDAAVL EAAVSPPSSP TAPPRPPNPE LLRLHAQVHA KMQSELASLS HVMALDAERL
RAHQADLLAG EPAIRDEMAR LEAVRDVCLT VADRMRAVVD AGTQNVAELR RKGDPEVDEL
VCSTTIVHNQ LINLVAEDNA IEDTIYHLHR ALNTGRIDLE RFIRTARVLA EEQFTKRALI
EKIQAGLPQD DSDAVWSVPP GWHYQ
//
