ID G7XV05_ASPKW Unreviewed; 664 AA.
AC G7XV05;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Ubiquitin C-terminal hydrolase {ECO:0000313|EMBL:GAA90714.1};
GN ORFNames=AKAW_08828 {ECO:0000313|EMBL:GAA90714.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA90714.1};
RN [1] {ECO:0000313|EMBL:GAA90714.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA90714.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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DR EMBL; DF126475; GAA90714.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XV05; -.
DR STRING; 1033177.G7XV05; -.
DR VEuPathDB; FungiDB:AKAW_08828; -.
DR eggNOG; KOG1867; Eukaryota.
DR InParanoid; G7XV05; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02662; Peptidase_C19F; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006:SF936; C-TERMINAL HYDROLASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:GAA90714.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..592
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 254..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 73113 MW; 9790690915CDF199 CRC64;
MNARREGINF LTPNPFNVQR SNYETILQQL QGNPSLVASI LVTLITLYFT IGYWGPASLS
VARIAWNILV HLTPSRLIAA LDSQTRKSDT TDENPLSMTF EAKSEAMQRI LGLDDTSSSS
LFPRAPAFSS FGTSLLSSKN NVPPGLGNWD NSCYQNSIIQ GLASLQSLEK FLDQNVEQLG
EKALMSTHQA LKDIIERLNS ADSNGQRLWT PADLKSMSSW QQQDAQEYFS KIVDQLDLEV
QQATRRHTRN LGLKMAGPQE HVIGSGSSQE LQENSGAESR STGNQVFRNP LEGLLAQRVG
CIQCGWTEGL SLIPFNCLTV PLGPKFEYDL RECLHHYMHL EPIEGVECAK CTLLRVQSQL
LNLLKQISDD EETPSATPES PKISDALRSS AQERLQAVEQ ALGEEDFAEK TLSQKCHIPG
KNRVSTTKSR QAVIARPPQC LVIHINRSMF DETTGMLRKN YAAVKFPNAL NLNPWCLGGV
SKNGEPNFEA WETNPSVSML SHAGRGATAG GHYQLRAVIT HYGRHENGHY ICYRKYPSDS
FPAHVPDAII EADGDKERDE RWYRLSDEDV QMVSEASVMS QGGAFMLFYE AVDDYSPEAA
EDVDSGLAEE EGSAPSSCTP SETMSTTSAA TGDSTSDVSQ ATSVSTALNV EPRSEKSLLM
SDVD
//
