ID A0A1J8RC13_9AGAM Unreviewed; 1043 AA.
AC A0A1J8RC13;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=AZE42_00435 {ECO:0000313|EMBL:OJA19306.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA19306.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA19306.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA19306.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-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:OJA19306.1}.
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DR EMBL; LVVM01001096; OJA19306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8RC13; -.
DR STRING; 180088.A0A1J8RC13; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000183567; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000183567};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 4..31
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 32..59
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 60..90
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 91..115
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 482..782
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 427..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 114674 MW; 81D246C0C3E5E99F CRC64;
MSTWSCSSCS KIFSRKGDLT RHQLLHTGIK PHKCEVCDRE FAQYSGLKTH RNTHTKAKPY
TCGIGTCTKA FSDPSSCTRH RKETHRREGA YKCLLPECGT RIKRRSAYAA HMKKHGIDIR
TLDLDAITSS ANKSNSQETD FHFLPPYVPD APYCPPSKMG TEPTLLNCAA PAPTPMSNYQ
MQLPQYGGNS GVTDGMYAYG WPSVLGTGRS IPSLVPAPSM SPFPPSYIDN YLDNVFDNGY
LQSDVMFSRL PPAYSSVSPS LPPLLDGFMD SLGSRMRSLS SSPASSSSSA LDDPLDFAFL
GQDVPHQYLL ISQGPTRLGV SGVSPFLQSI LLNHCSAGHR WLHLRSFIRV RSRAGSFSST
KRNMLASPLY PTSSFAPQLA SDDHSQFRPA RDIEAFNSLL PPPIEFVEGS SSGTLAVAEG
KYEPINATPK ASKNNVHEHT RTPSTPLTSP SKQLISSSAK RGSLFTGVLD FSWPWPGHNI
GNGLHNTGNT CFLNSALQCL LHTPPLVNVL MAHSKSDPCR VRGGFCMSCN LRQVMLDSHQ
KKHPSTPFFI VSKLHLIAKH MRKGRQEDSH EFLRYAIDAL QKSCLAGYPP KIDPKLAETS
WVHKIFGGRL RSRVTCKECH YNSDTFDSML DVSLDIYGTN SVRDAFRKFV AVDCLKGSDK
YKCEKCKKPV VAEKRFTIHD APAVLTIHLK RFSPLGRKIG HFVHYDEHIT LKPFMSEGQF
GPTYSLYGVI CHAGGGPNSG HYYAMVRGVN GMWYEMNDDS VSLHRGIPMS LKNAYMLFYI
REKGQSLEAA ISRPSMTPRN IVAGMKKRKA LDSEDDGGDD LGVKTTRPFI GPLLPSPMGN
DAEVHKKPKT DDRDPQAESI KKKIEAASKV PGPSTALTSL SQYNDDDDDD SGSPLVTPVD
LKPPSSTTES VTAASSSPPC PPTSPPPRNS SAAASTSSIS SVQSNNTPSL GISPSTFYAS
SNKNDKKRKS PDYDDDEHTP QKHYARVPLH TPSSKHGHNR RKSSFGGGAV NPYGRLAGSN
TLSRSENWRP MQQYGRKRKK MLM
//
