ID A0A0D1WCC2_9EURO Unreviewed; 1131 AA.
AC A0A0D1WCC2;
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=PV11_02017 {ECO:0000313|EMBL:KIV86405.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV86405.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV86405.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV86405.1,
RC ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
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; KN846951; KIV86405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1WCC2; -.
DR STRING; 1016849.A0A0D1WCC2; -.
DR HOGENOM; CLU_003532_2_1_1; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 65..194
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 220..546
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1131 AA; 130541 MW; B2148EC6448D7CD9 CRC64;
MDNLAGPDML IDGYDQYNEK ENEVVNISPD EGSEEPTDAL PRADDYEAMK RHVLVDLPDT
EPEAEIYNTW HIEKWRTLSR REHGPTFECG GHPWRVLFFP YGNQVDCASF YLEHGFEGDP
PADWYACVQF ALVLWNPNDP SLFRSHSATH RFNAKEGDWG FTRFVELRKA FHQPWEEGTR
HLIENDEANL TAYIRIIKDP TGVLWHNFEG YDSKKETGMV GLKNQGATCY LNSLIQSLYF
TDAFRKAVYQ IPTEQEANRS NSAWTLQRLF YKLQKDKFAV STNELTASFG WDTRQIFEQQ
DVQELSRILM ENLEKKMKGT PAERTLPELF VGKTKTYISC INVDFESSRI EEFWDLQLNV
RGNKNLHESF MDYIQVETLE GENKYDAGEP YKLQDAKKGV IFESFPPVLH LQLKRFEYDI
NRDAMMKVND RHEFPEEFNA SLYLSDEAKA STTEPWMYEL HGVLVHSGDF NAGHYYAFLK
PTKDGHFYKF DDDRVTRATM KEVLEENYGG EYANVANGGP GQRQPYMRGY STKRSMNAYM
LVYIRKSRAD QVLLGVNEND IPSHIERRIS EEQTELARKK KEREEAHLYM NVGLITEKTF
QAHHSFDLTN YELESSDPAA PQVHRLLRTT KVSEFAATVA EQEGLGPDQI RFWVMVGRQN
KTNRPDQPIR EVDISIEEAM NKYGSRGRPF YLWAEGVPRS EDGKVYFPDT TQGAGGNAPI
LVFLKYFDVK AQTLTGVGHV YVRKLDKVAE VAPQINKMMQ WDPSTSILLF EEIKFSMIEA
MKPKQTFQQS EIQDGDIICF QQNLPDLDSS TVTYTDARQY YDYLLNKIPV TFYPRPGTEG
EAFVLNLSKK MTYDQFSSKA GEHLKVDPTH IRFATISATN NKIKMWIKRG LNHNLNQILQ
SQFSSYGGYA THRPDALYYE VLETSLADYE TKKIMKVIWL SDGISKEEPL EVLVAKNGII
GDLISGIATK LKLDEEIARN IRILEVHGGK IHKELIEDFN VVGVNEFTTL YAERIPDEEL
NASDDDRFIY CYHFDKEANK PHGVPFKFML KPGEPLKETK ERISKRTGIK GKLLQQIKFA
LVSRALYAKP RYLEEDDIIV DLIQDGDEML GLDHVNKARN FWGRAEGMFI R
//
