ID A0A091E427_FUKDA Unreviewed; 873 AA.
AC A0A091E427;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=H920_08818 {ECO:0000313|EMBL:KFO29831.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO29831.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO29831.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO29831.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KN122563; KFO29831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091E427; -.
DR STRING; 885580.ENSFDAP00000009468; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02658; Peptidase_C19B; 1.
DR CDD; cd14384; UBA1_UBP13; 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; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; 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 PIRSF; PIRSF016308; UBP; 3.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 2.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFO29831.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR016308-3}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR016308-3};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 84..192
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 233..619
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 601..642
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 676..716
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 873 AA; 96361 MW; 739AA773D9B73B4C CRC64;
MRVIGCGGSS SSTVLHLDTD ENLNSDDYEY EDEAKLVIFP DHYEIALPNI EELPALVTIA
CDAVLSSKSP YRKQDPDTWE NELPVSKYAN NLTQLDNGVR IPPSGWKCAR CDLRENLWLN
LTDGSILCGK WFFDSSGGNG HALEHYRDVG YPLAVKLGTI TPDGADVYSF QEEEPVLDPH
LSKHLAHFGI DMLHMHGTEN GLRDNDIKPR VSEWEVIQES GTKLKPMYGP GYTGLRNLGN
SCYLSSVMQA IFSIPEFQRA YVGNLPRIFD YSPLDPTQDF NTQMTKLGHG LLSGQYSKPP
VKSELIEQVM KEEHKPQQNG ISPRMFKAFV SKSHPEFSSN RQQDAQEFFL HLVNLVERNR
IGSENPSDVF RFLVEERIQC CQTRKVRYTE RVDYLMQLPV AMEAATNKDE LIAYELTRRE
AEANRRPLPE LVRARIPFSA CLQAFSEPEN VDDFWSSALQ AKSAGVKLKS QEGTTSVLKA
LDLVGPCRPD VMAFPKMILN GSHLGKAFVF GVFIHSANTQ RESPPRCCPG AAGTRGFASR
RGPGAVPDAS GDPHFSCDVS IDMPDLLDIN HLRARGLQPG EEELPDISPP IVIPDDSKAA
DIDESSVMQL AEMGFPLEAC RKAVYFTGNM GAEVAFNWII VHMEEPDFAE PLTMPGYGGT
ASAGASVFGA SGLDNQPPEE IVAIITSMGF QRNQAVQALR ATNNNLERAL DWIFSHPEFE
EDSDFVIEME NNANANIISE AKPEGPRVKD GSGKHLQIFL VQLAAMMLPS STLGGTGDPT
PGAENNNLER ALDWIFSHPE FEEDSDFVIE MENNANANII SEAKPEGPRV KDGSGNSSLF
HLCITSSAPP APAAQMLDSA SVLSCHRLLS HCR
//
