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Database: UniProt
Entry: B6H2Y6_PENRW
LinkDB: B6H2Y6_PENRW
Original site: B6H2Y6_PENRW 
ID   B6H2Y6_PENRW            Unreviewed;       587 AA.
AC   B6H2Y6;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Pc13g15730 protein {ECO:0000313|EMBL:CAP92642.1};
GN   ORFNames=Pc13g15730 {ECO:0000313|EMBL:CAP92642.1}, PCH_Pc13g15730
GN   {ECO:0000313|EMBL:CAP92642.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92642.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92642.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC       subfamily. {ECO:0000256|ARBA:ARBA00009594}.
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DR   EMBL; AM920428; CAP92642.1; -; Genomic_DNA.
DR   RefSeq; XP_002559968.1; XM_002559922.1.
DR   AlphaFoldDB; B6H2Y6; -.
DR   STRING; 500485.B6H2Y6; -.
DR   GeneID; 8315138; -.
DR   KEGG; pcs:Pc13g15730; -.
DR   VEuPathDB; FungiDB:PCH_Pc13g15730; -.
DR   eggNOG; KOG2391; Eukaryota.
DR   HOGENOM; CLU_017548_2_1_1; -.
DR   OMA; YMNFPQP; -.
DR   OrthoDB; 37962at2759; -.
DR   BioCyc; PCHR:PC13G15730-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
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:0006886; P:intracellular protein transport; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00644}; Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PROSITE-
KW   ProRule:PRU00644}.
FT   DOMAIN          13..158
FT                   /note="UEV"
FT                   /evidence="ECO:0000259|PROSITE:PS51322"
FT   DOMAIN          518..586
FT                   /note="SB"
FT                   /evidence="ECO:0000259|PROSITE:PS51312"
FT   REGION          155..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..182
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..211
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..236
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..370
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  63037 MW;  1F6F9EC7442E1CC1 CRC64;
     MAVPQRTLNW LYSVLSKDHY DPQQTYRDPN RTYHDVANAL AQYPSLSPRT DVYTYETGFS
     ALLLHLVGTL PVTFRGTTYR FPIALWIPNT YPREPPIAYV TPTQDMAVRV GQHVTLEGQV
     YHHYLAHWAE AWDRSTIADL LSILQDIFAK EPPVRYRQQV PHPPPEAAQT PPPLPPLPPG
     VGSARQAQPL SPPTAQSQIP PPPPPKPSAA GEPLQQQPHP VDEYRSPPPL PPLPPKEQDS
     RRTYISTQSA SPGIHSYQHY APPGQTGGPI SSPRPLSQPP NQQAAGQPMP PQSAQGQAPY
     YRNNGAAVHH GTGSGIASQA PPQINPAGGH LPPQPQLPHQ PHQQLSGPPY PQHSPYPSNY
     PRPPPAAPAK AETPDLLTSP FEVELPSIAP TGPAPPIPPN PEKDALLNAV SRTLAEALRA
     NAAQSDTAAQ SLVSQSRSLH AAMATLQGEL SALNTLHTTL QSNTTVLQES IHRADATIAD
     AQARSTSISA SSAPSTSTPS GDTPSGLPPI DDVLVAPTVV GKQLYDLVAE EQGIQQALYA
     LQAALVRGVI GVDSWSRHTR SLAREALLKR ALIRKIGRGM GLDESVG
//
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