ID A0A0D2ANQ7_9EURO Unreviewed; 1101 AA.
AC A0A0D2ANQ7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PV06_07099 {ECO:0000313|EMBL:KIW41551.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW41551.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW41551.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW41551.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
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 ---------------------------------------------------------------------------
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; KN847337; KIW41551.1; -; Genomic_DNA.
DR RefSeq; XP_016261767.1; XM_016408287.1.
DR AlphaFoldDB; A0A0D2ANQ7; -.
DR STRING; 215243.A0A0D2ANQ7; -.
DR GeneID; 27359173; -.
DR VEuPathDB; FungiDB:PV06_07099; -.
DR HOGENOM; CLU_005922_0_0_1; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000053342; 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; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 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; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT DOMAIN 418..550
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 741..1098
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 123560 MW; 55DCF27169253D64 CRC64;
MAAYASPSSF GSQATAPSAD SISTRSSWSD TRNTTPGSAS ERVFAHIKDI IHDATTGIEP
DGSLAHYLSE VETCIATAKS SVDFRRPDVA YKNYLRAYEI AVERIPTHKD YGIWDNNSSW
SSKYKAGLRR INELSNQMAQ VRGVIEENNR RHGTQQRSVS RKPVYSTGFG VPSTASSASS
GRTNGSEVWQ TDSRPSAELP DALRINRARP SSKPPKPESL QGRPLSEQPN DLSQRFARLR
GPGSSKEVGP ILTMPNPSDF QSAAGNAPRP QSYAPYATSK VNGASSHRLN GPRDMPGPGN
GPSLPPKVPL TTNMVMPKPP SPTYSPITTT SIASHANSSR LPTESGRPPH ERKQTYYNQS
QNSSTNSLHI QRTRDEILSP YRPTTPNGIN SAIVAKSSSS EIPHRPSIDA QTLLEYMKKY
NVLVVDIRER VLFDDGHIMS SSIICIEPIS LKEGVSAEEL EDRLVLAPDV EQTHFSRRNE
FDIVVYYDQD TSDISYLKGP PSMTRAPALR ALYDTLYEFN DTKPLKDGRP PALLAGGLDA
WVDFVGAQSL ARSKTAAMLG TIQRRRAVGP GRPIARQRLV SANSRYEVRN RRLRDHKFLD
ESEQEAWRQQ ALQEEVMPAE KTRAASDDED ATVDEELPPP SPFVPDYETF LRRFPSIRQQ
ESMIMPARRP LASHPAPYLP HAVAPVPQVP TRPPPAIPRP SYSGQADINA PQPALARVTS
ASRPPLYSSA TSIRAKRLPK TGLTNFGVTC YMNSTLQCLS ATIPLSAFFN DRMYEAYVQR
NWKGSNGIMP KLYANLVQAV WQGDNEVIKP STFRNFCGRM NREWVIDRQQ DAKEFFDFIV
DCLHEDLNVN WERTPLRPLT TAEEMQRERM EIARASPIEW KRYEHRDHSF LSSLFAGQHA
SRLRCLTCKR TSTTYEAFYS ISIEIPRSGT GHIYDCMNSY CREEKLSELW RCPYCKCERE
ATKQIILTRL PQFLVIHFKR FAASKHEKAK KIHTPIEFPL HGLSMDDFVI PRPPSVPDAE
GQIDMATTPP YSYDAYGVLR HLGNSGDGGH YISIVKDQGR GCWRKFDDER HVDLDPNKLS
ARDRLQNSEA YIVFYQRAQA R
//
