ID A0A0D2CF81_9EURO Unreviewed; 1117 AA.
AC A0A0D2CF81;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:KIW29768.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW29768.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW29768.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW29768.1,
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; KIW29768.1; -; Genomic_DNA.
DR RefSeq; XP_016249984.1; XM_016392465.1.
DR AlphaFoldDB; A0A0D2CF81; -.
DR GeneID; 27344750; -.
DR VEuPathDB; FungiDB:PV07_05556; -.
DR HOGENOM; CLU_003532_2_1_1; -.
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 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:UP000054466};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 51..180
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 206..532
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1117 AA; 129177 MW; E9094D66CCCBC435 CRC64;
MDHYPPDNEV VNISPDDASE EPSEALPRAD DFETMKRHVL VDLPDVEVEA EAYHTWHIEK
WRTLSRREHG PIFECGGHPW RVLFFPYGNQ VDCASFYLEH GFESDPPPDW YACVQFALVL
WNPNDPTLYR THTATHRFNA KEGDWGFTRF VELRKAFHQP WEDGSRHLVE NDEAKLTAYV
RIIKDPTGVL WHNFEGYDSK KETGMVGLKN QGATCYLNSL LQSLYFTNLF RKAVYQIPTE
QEANRSNSAW TLQRLFYRLQ KDRFAVSTNE LTASFGWDTR QIFEQQDVQE LSRILMEVLE
KKMKDTPAER TLPELFVGKT KTYISCINVD FESSRIEEFW DIQLNVRGNK NLHESFMDYI
QVETLEGENK YDAGEPYKLQ DARKGVIFES FPPVLHLQLK RFEYDINRDA MMKVNDRHEF
PEEFDASLYL SDEAKAASTE PWIYQLHGVL VHSGDFNAGH YYAFLKPTKD GHFYKFDDDR
VTRSTMKEVL EENFGGEYAN VANGGLGQRQ PYMRGYSTKR SMNAYMLVYI RKSRLDEVLL
DVSESDIPAH IETKIAEEQA ELARKKKERE EAHLYMNVGV ITEKSFQAHH GFDLTSYELE
QSDPASAQVY RVLRTTKISE FAATIAEELG LESDQIRFWV MVGRQNKTNR PDQPIRDVEI
TMEEAMTKYG SRGRPFYLWA ENGTKGDDGK IQWPDPAQAV GGNIPILVFL KYFDVKAQAL
TGVGHVYVKK LDKVQEIAPQ INRIMNWDPT TPILLFEEIK FSMIEAMKPK QTFQQSEIQD
GDIICFQQNL PDLDLSTATY TDARQYYDYL LNRIPVSFYP KPGTEGEAFV LSLSKKMTYD
QFSAKVGEHL KIDPTHIRFA TISATNNKIK MWIKRGMNHN LQQILQSQFS SYGGYATHRG
DALYYEVLET SLADYETKKI MKVIWLSDGI SKEEPLEILV AKNGIIGDLV AGIAKKLNLD
EQTARNIRVL EVHGGKIHKE LIEDFNVVGV NEFTTLYAEK IPDEEQNASE DDRFIYCYHF
DKEANKPHGV PFKFMLKPGE PLKETKERIS KRTGIKGKLL QQIKFALVSR TLYAKPRYIE
DEDIIVDLIQ DGDEMLGLDH VNKARNFWGR AEGMFIR
//
