ID A0A0D2AWV7_9EURO Unreviewed; 1130 AA.
AC A0A0D2AWV7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PV07_05556 {ECO:0000313|EMBL:KIW29767.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW29767.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW29767.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW29767.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
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; KN847042; KIW29767.1; -; Genomic_DNA.
DR RefSeq; XP_016249983.1; XM_016392464.1.
DR AlphaFoldDB; A0A0D2AWV7; -.
DR STRING; 569365.A0A0D2AWV7; -.
DR GeneID; 27344750; -.
DR VEuPathDB; FungiDB:PV07_05556; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000054466; 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 K02C4.3-RELATED; 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:UP000054466};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 64..193
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 219..545
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1130 AA; 130567 MW; F7FCDFB9D880CA2F CRC64;
MDHLAGPDML IDGYDQYPPD NEVVNISPDD ASEEPSEALP RADDFETMKR HVLVDLPDVE
VEAEAYHTWH IEKWRTLSRR EHGPIFECGG HPWRVLFFPY GNQVDCASFY LEHGFESDPP
PDWYACVQFA LVLWNPNDPT LYRTHTATHR FNAKEGDWGF TRFVELRKAF HQPWEDGSRH
LVENDEAKLT AYVRIIKDPT GVLWHNFEGY DSKKETGMVG LKNQGATCYL NSLLQSLYFT
NLFRKAVYQI PTEQEANRSN SAWTLQRLFY RLQKDRFAVS TNELTASFGW DTRQIFEQQD
VQELSRILME VLEKKMKDTP AERTLPELFV GKTKTYISCI NVDFESSRIE EFWDIQLNVR
GNKNLHESFM DYIQVETLEG ENKYDAGEPY KLQDARKGVI FESFPPVLHL QLKRFEYDIN
RDAMMKVNDR HEFPEEFDAS LYLSDEAKAA STEPWIYQLH GVLVHSGDFN AGHYYAFLKP
TKDGHFYKFD DDRVTRSTMK EVLEENFGGE YANVANGGLG QRQPYMRGYS TKRSMNAYML
VYIRKSRLDE VLLDVSESDI PAHIETKIAE EQAELARKKK EREEAHLYMN VGVITEKSFQ
AHHGFDLTSY ELEQSDPASA QVYRVLRTTK ISEFAATIAE ELGLESDQIR FWVMVGRQNK
TNRPDQPIRD VEITMEEAMT KYGSRGRPFY LWAENGTKGD DGKIQWPDPA QAVGGNIPIL
VFLKYFDVKA QALTGVGHVY VKKLDKVQEI APQINRIMNW DPTTPILLFE EIKFSMIEAM
KPKQTFQQSE IQDGDIICFQ QNLPDLDLST ATYTDARQYY DYLLNRIPVS FYPKPGTEGE
AFVLSLSKKM TYDQFSAKVG EHLKIDPTHI RFATISATNN KIKMWIKRGM NHNLQQILQS
QFSSYGGYAT HRGDALYYEV LETSLADYET KKIMKVIWLS DGISKEEPLE ILVAKNGIIG
DLVAGIAKKL NLDEQTARNI RVLEVHGGKI HKELIEDFNV VGVNEFTTLY AEKIPDEEQN
ASEDDRFIYC YHFDKEANKP HGVPFKFMLK PGEPLKETKE RISKRTGIKG KLLQQIKFAL
VSRTLYAKPR YIEDEDIIVD LIQDGDEMLG LDHVNKARNF WGRAEGMFIR
//