ID W7HR54_9PEZI Unreviewed; 791 AA.
AC W7HR54;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
GN ORFNames=DRE_04199 {ECO:0000313|EMBL:EWC46476.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46476.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC46476.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC46476.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) 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 ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308,
CC ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KI966417; EWC46476.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HR54; -.
DR HOGENOM; CLU_009884_1_0_1; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02658; Peptidase_C19B; 1.
DR CDD; cd14385; UBA1_spUBP14_like; 1.
DR CDD; cd14386; UBA2_UBP5; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Protease {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 152..260
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 302..791
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 578..630
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 652..692
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 693..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 742
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 197..200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
SQ SEQUENCE 791 AA; 87071 MW; 1D66C6FAD9607971 CRC64;
MASCTHITQL SLRPPTVSQP VYREDCTICF DSIDDPDGLD VCLSCFNGGC AGDRMHGGLH
AAQQDHPLAL NIRRTKKPKV ERDEPPQKVT KLAIAAETED DIYDTKAMVR CHTCDVDDVE
QTGNLPEVVD GILKAMTAAR ATEVQAWTLE LEHCEHVSFL VQDDKAGKEI DLTKCADCDL
KENLWMCLQC GNLGCGRGHF GGVGGNGHGV AHYSSTKHAA SVKLGSVSPE GTADIYCYIC
DDERLDPHLT EHLHHWGIKI AERQKTEKSL VEMQIEQNLH WEFRMTGEDG KELKPLFGPG
LTGLKNLGNS CYLASILQCL FSLDGFRSRY GNIEDVPMAN RPAEDLDTQL KKVGDGLLSG
RYSKPDEPKK LNEDDNAYVQ YQRGITPAML KALVGKGHEE FSTMRQQDAF ELLLHLFKLV
SRSPHPEPLK DPVSDFRFAV EQRLQCLGCK KVRYRTDEQD NITVPVPARQ LKDVVMTDAD
QKKDEYEPVT LKECLDIFTG AETIDYACKA CGSKEGAIKK TGFKTFPKVL AVNARRFAII
NWVPTKLDIP VVVDTAPFPL DPYLSAGLLD TEELLPEDTD ESGSQPSFTA NADAMAMLGG
MGFPSGRCEK ALYHTGNADA EAAMNWLFQH MEDPDIDEPL QLPSGSSSSA TTADPESVMM
LASMGFTEAQ ARKALKETGG DVERAVEWVF SHPDDAGDEE GAAPTGGGEA KKSVLPGSSE
TPANFQLASI VCHKGTSIHA GHYVAFIRKL VDHGDGTPRE TWVLFNDEKV VDGADVEEMK
KFAYVYFFER L
//
