ID A0A317X6X3_9EURO Unreviewed; 1273 AA.
AC A0A317X6X3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=BO94DRAFT_609542 {ECO:0000313|EMBL:PWY94374.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY94374.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY94374.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY94374.1,
RC ECO:0000313|Proteomes:UP000246702};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
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:PWY94374.1}.
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DR EMBL; MSFK01000004; PWY94374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317X6X3; -.
DR STRING; 1450535.A0A317X6X3; -.
DR OrthoDB; 1423057at2759; -.
DR Proteomes; UP000246702; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02666; Peptidase_C19J; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR025305; UCH_repeat_domain.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR Pfam; PF13446; RPT; 3.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PWY94374.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702}.
FT DOMAIN 618..1191
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 142088 MW; 253DA3550BB03E1D CRC64;
MSSPPRSGKT APRLVQDLHD YDPAHPPGSG RNLLSDVPPA FPDYYTGPPE LISPSACRHT
YVTKPNQSFL PQPEKRSSSG NPIKVSAICS QCRYHLQVVV TSTPGIGSQS LPGHIHHLVY
KSGRQVGGAS AEEVTPKGQT AETFHYDCSY LTCPVVVSVR VVSPVLHPDW VQLLTDPELL
RERADEAIAA HPERLEGIAR PQPINVLENL RAYISNAFLT SQQGKSISAI NKRFMTCFGV
EGKPCKDLLE FLGFAVKNEG FWDPPRPNPW AENPYQDQLK IFLDDVLHEL SALIEQRPVL
EKKGHQLEYS HRPARDDLLY ALEAQDYQKA LGIEEFQMPP APYYEDLGVV EDMSSQSIVE
AFNRQVAVDP ARMPAYLKCL KEIGGLRAGP EHNTIDQAVQ VAYADGKYTD DDVADAYKYF
GLTHDDPRLT EDSIIGTFHA YLSSTTQEIE SRRQLWRIGD SRRSERIKSA AEDMATVEQA
QVYLGVSDGT SDDFIMAMYT AKVNDTPSSR DLARRAVELI AEARKSDALR HFVKTGEMTS
GEMDIGDAYR LLQIPDRTVD EAAIMAAYTI CVDEAPAQAD TYNQALRIIA KDKNSPLLSS
MISGDDTKPD RDMSEWPVGL QNIGNTCYLN SLLQFYFSVR PYREMVLDFE NFKMDLSDES
LSRKQVGSRK VSQKEVERSQ KFLRELRTLF SDMITSSSSY VIPGQELARL TLISPSNEAA
IRRRSTISAY RPAGALGEIN GMPVLGPLGP PQLIPEKETE KPTATESEAS KQSTTSDVDS
EATLVSDGVK HDVKTSQFDD KENEPPGDSE MKDVQDEPNG SAAQVSSSDT TSIDQPEPSS
RPPPVPPRPT PQVDAQKQLI EDVEIGAQQD VTEVINNVLF QSQCAIRPIA HSPDGEQIDQ
VKDLFYGRTR SYIASEKGIR SKEEWWADIK IDVASGPRDI YAAIDGAFDV QKVNVENSVA
EQYGAISKLP PVLQIQVQRV QFDPATKRSF KSTHHLGLKE TIYLDRYMDT QQPEFLDRRQ
QSWQLKSSLR ELEARRAELL RQSESDGMDT AGLLNSAKEI LDDLICMKNE PEFAGEAIDI
DPRTAAELDQ LSQIAKADLI YVEDQIKETE AMISSQFADY KHLAYRLYAV FVHHGSVSFG
HYYIYIFDFE RKVWRKYNDN YVTEVDNLDE IFQDDGQQNP PTPYFLVYVN DALKDRLVNP
VCREIIETSS ANTTGDISMN PPAYDEIWGE NSEPGTGADH PMKEATGDVD AVTTGLLGGW
QGNTGADIEN VEW
//
