ID Q7S4R9_NEUCR Unreviewed; 580 AA.
AC Q7S4R9;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=ESCRT-I component {ECO:0000313|EMBL:EAA30492.1};
GN ORFNames=NCU05753 {ECO:0000313|EMBL:EAA30492.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA30492.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA30492.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000256|ARBA:ARBA00009594}.
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DR EMBL; CM002242; EAA30492.1; -; Genomic_DNA.
DR RefSeq; XP_959728.1; XM_954635.2.
DR AlphaFoldDB; Q7S4R9; -.
DR STRING; 367110.Q7S4R9; -.
DR PaxDb; 5141-EFNCRP00000005762; -.
DR EnsemblFungi; EAA30492; EAA30492; NCU05753.
DR GeneID; 3875890; -.
DR KEGG; ncr:NCU05753; -.
DR VEuPathDB; FungiDB:NCU05753; -.
DR HOGENOM; CLU_017548_2_1_1; -.
DR InParanoid; Q7S4R9; -.
DR OMA; GTVYKFP; -.
DR OrthoDB; 37962at2759; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0000813; C:ESCRT I complex; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
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 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:UP000001805};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..151
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 514..580
FT /note="SB"
FT /evidence="ECO:0000259|PROSITE:PS51312"
FT REGION 146..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..385
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 62812 MW; F4313B136DC2CB7A CRC64;
MVVQQHILNW LYSVLTSEYH DVNRTYNDVA QVLSHYPSLS PRTDVHTFPN GASALLVHLS
GTLPVVFRGT TYRFPISVWI PHAYPREAPL VYVTPTEHIM VRPGQHVDPQ GQVYHPYLAG
WSTYWDKSTI LDFLAILRDV FAKEPPVIAR PPPQGQVRSP PPQQQQQPQP PQAPGVPTPP
PVPPLPQELA ARSPVPVPLP AQQDGARPPP PPPKPGAPAA AAPIPQHQPS PAPSYAAAPP
VPPHPPHPGR PTSQHGGPGA STTQSPRPGP SRYDAPPPLP PHPTAQQQQQ QQPPQPPHGA
PYQSPPPVPA ALPHNQAPPQ PPFSQMDPRR MSTLQQHTPQ HYASPPNWQQ QQYPPQASPP
PHQQHQFPPQ PQPKPPPPPD LLDDDTPASP PSSTPGAGAN ATTTTASPDA PPPPPPNPEK
DALLRQLAST LYTHRQHARA QNDSSLAGLQ AQRTAMDQAA TTLQAEYAQL SQLSALLTSN
TDILQESLRK ADAVIENSKT LKEPDIDELL VAPTVVGNQL YELVAEERAL ADAIFMLGRA
VERGRIAPGT HAKMVRGLAR EWYLKKALVK KIGDGMGLSQ
//
