ID A0A0C3DIT5_9AGAM Unreviewed; 1162 AA.
AC A0A0C3DIT5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=SCLCIDRAFT_133507 {ECO:0000313|EMBL:KIM55976.1};
OS Scleroderma citrinum Foug A.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Sclerodermataceae;
OC Scleroderma.
OX NCBI_TaxID=1036808 {ECO:0000313|EMBL:KIM55976.1, ECO:0000313|Proteomes:UP000053989};
RN [1] {ECO:0000313|EMBL:KIM55976.1, ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|EMBL:KIM55976.1,
RC ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KN822124; KIM55976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3DIT5; -.
DR STRING; 1036808.A0A0C3DIT5; -.
DR HOGENOM; CLU_005922_2_1_1; -.
DR InParanoid; A0A0C3DIT5; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000053989; 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; 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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF95; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4-RELATED; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 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 Reference proteome {ECO:0000313|Proteomes:UP000053989}.
FT DOMAIN 415..534
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 802..1160
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 206..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1162 AA; 126510 MW; 7C79774ACA1E2F5B CRC64;
MPVVAVLPPS LPGRGVGSLY SENSVVFPSG IPGVNHIPNS TMQNGSIAPT ERLSILDIKE
KAKEDALRHG KGISAISLLK AARNQSQLAQ TNEDQGDLKG ALSALLKAGS LAAMVMNSSE
FVGESRQGKH GVLYKEFVNF QKYDGNNLKQ RVEAIESKLA DLEKSAATEP ILDATNKRVG
NSIADRVRSL NDAGLVVGTA AKRLSRDLTG TPSTPPKSPE LVRTHRLSTS IPSHPQPLHF
PISISATASS SAGSSPHAVV PASSFGPPSP ISSESSSPRL PHPSIAEFSQ TFPSIDQLNE
LDPLRFPTVP QGHPTNSESL LPGVDDVELP RLKSFPSLSI DPGPRPSSTP ITITMNSLMS
RPASPAITSK PSINNFASSS LSSKPSPQGE KPVLPNTNSV TPKQLFEYLH TPNLNVLLVD
IRTRAEFETE HIKNGAVVCL EPSVLTRASV SAQSIEDSFS VAPREEFVLF QNREKFDLVV
LYDASSETYD PAGPLCAFAR VVYENAFSKM LRRPPVLLLG GLQAWKKDIE ESDIVCGVPS
EQRRSPISTG ETRLSNTSGS VLLSTSTMRD PSRLVLPLNQ PSPNGASPSD RISPESHVPD
LPTSHSGYVF SVCSFLDVNN DKVSNGPVSI SPKIPILRPL SSAVPPPESS PYMSRVVPQS
LFNNANAPSG SISYPTFSSQ NLPGSSKRLS ISSSSSPYTT VSVPPQASIN PSRRRSEYMD
GPQSPVSVLT TRPVIDYPDL LSTLRPPPPA ASNSYERQDT RPRLVHATSL SMSPPTKLAP
KPPTIPNDYV VTYWSDVQIN TAGLKNLGNT CYMNATIQCL RATVPFAGFF TDGRWKSAVN
VLNPLGTKGS LAQAFKNILY EMSHSEMPHL NPLGFRKSIC HHASQFGGSD QHDSQEFLTF
LLDGLHEDLN RVITKPSNQA STPEREAELE KLPQQVASAQ EWEQYKMRND SLIVDYFQGQ
FRNRMECLTC HHTSTTYNSF MYLSLPIASV RSPSKISLQS CLDAFVREEV MEKAEAWHCP
KCKQLRKATK KLTLSRLPPV LLIHLKRFSV KGPFTDKIET FVDFPLKGLD LTNYMPPPLP
PGVLPTVNGT TPDDSRVQIP PYKYDLYGVT NHFGSLSNGH YTAFIASGGG WLYCDDSRIT
PTLATEVVGR PAYVLYYKRV KN
//
