ID A0A2A9NH20_9AGAR Unreviewed; 1140 AA.
AC A0A2A9NH20;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=AMATHDRAFT_4113 {ECO:0000313|EMBL:PFH50295.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH50295.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH50295.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH50295.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ302007; PFH50295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9NH20; -.
DR STRING; 703135.A0A2A9NH20; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000242287; 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 CDD; cd00158; RHOD; 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 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:UP000242287}.
FT DOMAIN 369..492
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 791..1140
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 132..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 124832 MW; 38FA19499C320286 CRC64;
MPGVTITPSS PNAGSFGPSS SALYLGMSVA EIKAKAKEAV SKDARGVSAM TLIKTARSQI
VMAQDYESRG ELKSALSAYI KAASLATMTL ESSEYFSERG KSGMVRKELN DFMEKHANVL
NARANAIEEM LKTSEKQSQE DTHDPKGPIT KTGGSIQDRL RALESHGMDI TAKSSKRSFR
DSLNQQPTSP VLAKRFSNPP SNIAVLSALS PPASISTASS QHTVVSPSSL GPPSPSSSPS
SSPLMSNLDI SGFSRAFPTI DELNGDLNFS LPSVPTGTSI GSVKSSPRHA PVDEPPPAIP
TIGEFAVPFE RPSSTPITPL TTNFVSRPTS PSKNTAPIKS SGLSASMLSK SPIPVSNSAT
AKELLNYIRD YNVLLIDVRN RDEFEQEHIK ADAIVCIEPT VLLRENVTEQ MLEDAMVIAP
KQEQSLFMNR DKFDLVAVYD NNSTTFGAPT GPLQVLVRAI KEQAFKKMLK RMPMMLMGGI
AAWKHEFGDS EVVKGYSSLS SLQSPKPTQS LNSETLVNGN TSTPMFTPSS PSHNGFMING
NVPHSPLLAA STSSSSSITQ SQIPPRSPFV SHPQPGDHRT QFSVDYAYGH NRSPAEFSYP
SSPFPNDARN GLARRPAISR PSSNSVSYTR STLDSLVNGH ASINGATPVS PITYPSVSRR
ISPAMSGSNS TSPIPPQIYH GIASPTIASP PQASINASHI SRRRGDFVDQ SQEALSNLND
HRPPIDYPEI PGPQIPRPPP AAALSGLERQ DKRAQHMPHP APQPHSAGPK PPRIPSDYPV
TFWFDMQVGT SGLKNLGNTC YMNAPIQCLS ATVPFARFFT EGRWKHAINF CNPLGYKGKL
TDAFAKLVQE MWHADFPYLT PIEFRKNICQ LKSEFIGNDQ HDSQEFLSFL LDGIHEDLNR
VIYKPPVIQS PEQEAELERL PPQIASEQEW QAWKTRNDSL IVDFFQGQFR SRLECLTCRK
TSTTYNVFSI LQLPVPHAKT GKIPIQRCLD AFFNEEILEK DDSWDCPQCK AKRRATKKLS
LARLPPILLI QLKRFEANGR FSDKIDTFVD YPTKSLDLTN YMPPPLPPGV DKKQLNGGAP
MSPDDPRTQL PPYRYELYAV TNHYGNLSSG HYTAFIASRG GWMYCDDSSV KPVDPKQVVV
//
