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Database: UniProt
Entry: A0A0D2AWV7_9EURO
LinkDB: A0A0D2AWV7_9EURO
Original site: A0A0D2AWV7_9EURO 
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
//
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