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
//