ID A0A1Y1YQX2_9PLEO Unreviewed; 864 AA.
AC A0A1Y1YQX2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=BCR34DRAFT_627955 {ECO:0000313|EMBL:ORY00441.1};
OS Clohesyomyces aquaticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY00441.1, ECO:0000313|Proteomes:UP000193144};
RN [1] {ECO:0000313|EMBL:ORY00441.1, ECO:0000313|Proteomes:UP000193144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY00441.1,
RC ECO:0000313|Proteomes:UP000193144};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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:ORY00441.1}.
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DR EMBL; MCFA01000183; ORY00441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YQX2; -.
DR STRING; 1231657.A0A1Y1YQX2; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000193144; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000193144};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 407..782
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 94424 MW; DF44FE0E6A00D0E8 CRC64;
MPPHAHSPVP HNPYAQYHHH PQHYGAPHAS PYQQQWYPYP QPQHQYQMPP RQYQPQPQPQ
PHGSPVVVSS HLHMGAPMPL VNRQLGQTPP IAHSRTPPAP RNMTPQPAPS TPSVTSQTHV
SSPTPPTNMT TPTPPPRTPS RPVFSAPPLP PQPTHRMPYY PQLPWLSVPD VDFPPRASQK
KKRRKTPVAS TDEGLAFPTR EVTLEDEQVT KEEAEVEKTP TEVPEDAHVD ESQASTVAAA
SEIETPSTSN PPSEADSTHP TTPSSAMPPP AARPATSGHT RTATIPAVPL IPIKPVKPAS
VTSTTQKSVT SKGEPKKAEA ASSSTTEPSA SAEETPKASP PPKPAPPKSW AELLRSKAAA
PAVQAPVVPN GVVTTNGASA PKSNSLADVL TSFAVDSEKK ISFLEPRGLV NTGNLCYMNS
ILQVLVFCVP FYDFLDQVAK RAAHNFKSET PLVDAMIMFM RDFKVIDSHG SIETLRMRLK
GTELEQYGDP LTPEYVYDVI KRLPRFDNMK RGQQEDAEEF LGFLLAGLHD ECAHVIKSGL
STNGASSVTS PNSDRSGSVD GGWLEVGPKQ KSSVTQSSGA IEVETPVTKI FGGKIRSEYR
KPGEKPSVTL EPYQPLQLDI HSPGINNITD ALKGLTHLET LDGTTHGARA STKQMFIETL
PPVLILHLKR FHYSASGAQK IWKKIGYPLE LEIPKEVFPL HKRGGFAARG GLPRYRLTAV
VYHHGKNASG GHYTVDLRRQ EGREWIRMDD TIIRRIRAED VAEGGAEEDP KVLAAALEQH
KRDSSRSRNF FEQVGMDGDE EKTEEGGWSQ VNGVDKKDAG AKKWTGVVNG TATPSTTGKR
TPLPKESVRD NKVAYILFYQ KIEA
//
