ID A0A317VTA4_ASPEC Unreviewed; 665 AA.
AC A0A317VTA4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:PWY77553.1};
GN ORFNames=BO83DRAFT_219997 {ECO:0000313|EMBL:PWY77553.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY77553.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY77553.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY77553.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY77553.1}.
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DR EMBL; MSFU01000007; PWY77553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VTA4; -.
DR VEuPathDB; FungiDB:BO83DRAFT_219997; -.
DR OrthoDB; 1749511at2759; -.
DR Proteomes; UP000246171; 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 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 600..665
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 611..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 665 AA; 73272 MW; 52AA7F821DCB0E81 CRC64;
MNARREGINF LTPNPFNVQR SNYETVLQQL QGNPSLVASI LVTLITLYFT ISYWGPASLS
VARIAWNILV HLTPSRLIAA LDSQTRKSDT TDENPLSMTF EAKSEAMQRI LGLDDTSFSS
LFPRAPAFSS FGTSLLSSKN NVPPGLGNWD NSCYQNSIIQ GLASLQSLEK FLDQNVEQLG
EKALMSTHQA LKDIIERLNS ADSNGQRLWT PADLKSMSSW QQQDAQEYFS KIVDQLDLEV
QQATRRHTRN LGLKMAGPQE HVIGSGSSQE LQENSGAESR STGNQVFRNP LEGLLAQRVG
CIQCGWTEGL SLIPFNCLTV PLGPKFEYDI RECLHHYMHL EPIEGVECAK CTLLRVQSQL
LNLLKQISDD EETPSATPES PKISDALRSS AQERLQAVEQ ALGEEDFAEK TLSQKCHIPG
KNRVSTTKSR QAVVARPPQC LVIHINRSMF DETTGMLRKN YAAVKFPNTL NLNPWCLGGV
SKNGEPNLEA WETNPSVSML SHAGRGATAG GHYQLRAVIT HYGRHENGHY ICYRKYPTDS
FPAHVPDAII EADGDKERDE RWYRLSDEDV QMVSEASVMS QGGAFMLFYE AVDDYSPEAA
EDVDSGLAEE EGSAPSSSCT PSETMSTTSA ATGDSTSDVS QATSVSTALN VEPRSEKSLL
MSDVD
//