ID A0A2I2GRW7_9EURO Unreviewed; 1107 AA.
AC A0A2I2GRW7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=P170DRAFT_452930 {ECO:0000313|EMBL:PLB55615.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB55615.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB55615.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB55615.1,
RC ECO:0000313|Proteomes:UP000234275};
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:PLB55615.1}.
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DR EMBL; MSFO01000001; PLB55615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GRW7; -.
DR STRING; 1392250.A0A2I2GRW7; -.
DR VEuPathDB; FungiDB:P170DRAFT_452930; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PLB55615.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT DOMAIN 419..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 739..1104
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 124385 MW; A0288D394DD966B2 CRC64;
MSSNAAALPS PPEFAPWDKT PRPHSIGGLY SGGQGRPAGA LQNGPSAPHG ARSPRFPSIK
DLQDEAAALD VNESSSLDDL LSRAQEAIQQ ARSFADNDQP DTAYVQYLRA SEITVNIIPH
HADYRVTISQ RPGWYKQFAN LMMAVRTKQG TMDDIKRQIL EDNFINNVQP SSTPKHSSPR
PVSEILPAGT FRSSSPRGRR NDSGDNSVRM PSPTEFQRSL DTKMNRFSSP PEDALAQRFA
KLRASPPTTN GLDSVINGQN GAISMPLQEN TDNNSSRPSS YIPPRSQQSS VLSSPSRRPL
GPRSMGAPHG APTLPPKLPL NTSLPRAPDP TYSPIWSVPS QPPSNPPRTS TESSRPVNPR
YSQFTNSPRG SPSRNGLDDN PYRSRTPNGI HQVKEARSST ADIPHAPTIS AQHLLDYLRR
YNILLIDVRS RDQYDEGHIF AKSVICIEPV ALNENVSADD LEERLVVSPE HEQSLFERRN
EFDMVVYYDQ NTGSVSYLAG SPVGTTAPHL RALHDTLYEF NPYKALKDGR PPALLLGGLD
AWIDLLGQQS LATSTTAIAM GSIQARHKPG RPLGRKPTIA SANSSLEVRK RRLREYKPLN
PEELTEWMEK SKNEEIDTST YVGEGELTEE PEGEVQEEQP PSPFVHTYED FLRRFPEPHT
VQESMVAPHA RKPVPTAPNY AAPVPVAPSR PPPAVPRPSY SGVSDGRQIQ PTLERQNSAT
KTALYTANSV LNRIKLPRTG LTNFGVTCYM NSTIQCLSAT LMLSKFFIDD RFRFYVQKNW
KGSQGVMPSL FANLVRSLWK NDVEVIMPTS FRNFCGRLNQ EWAIDRQQDA KEFFDFVVDC
LHEDLNINWQ RTPLRPLTFS EEVQRERMPV PKVSRIEWDR YCHREESFIS SLFAGQHASR
LRCTTCQRTS TTYEAFYSIS VEIPPSGTGD VYQCLRSYCQ EELLSGDEVW KCPYCKCERV
ATKQIIITRA PQILVVHFKR FSASKTHSAR KIHTPIDFPL HGLRMDDFVF AWSSQVPPSD
PKATGRPEMI SATVPPFTYD AYGVLRHIGS SMGSGHYISL VRDAQRQCWR RFDDHRVTDF
NPRDLQYKDR LQNEQAYIVF YERVPAK
//
