ID A0A091DKX2_FUKDA Unreviewed; 1125 AA.
AC A0A091DKX2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE Flags: Fragment;
GN ORFNames=H920_07558 {ECO:0000313|EMBL:KFO31123.1};
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:KFO31123.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO31123.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO31123.1};
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};
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DR EMBL; KN122326; KFO31123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DKX2; -.
DR STRING; 885580.ENSFDAP00000008003; -.
DR MEROPS; C19.054; -.
DR eggNOG; KOG1863; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02665; Peptidase_C19I; 1.
DR CDD; cd14355; UBA_UBP28; 1.
DR CDD; cd20487; USP28_C; 1.
DR Gene3D; 6.10.250.1720; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF678; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 28; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFO31123.1};
KW 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}.
FT DOMAIN 143..635
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 683..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 386..413
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 689..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO31123.1"
SQ SEQUENCE 1125 AA; 128244 MW; EB9E25C2C92463BA CRC64;
SCQMLLNQLR EITGIQDPSF LHEALKASNG DITQAVSLLT DERVKEPGQD TVATEPSEVE
GSAANKEVLA KVIDLTHDNK DDLQAAIALS LLESPKVQAD GRDLNRMHEA TSAETKRSKR
KRYEVWGENP NPSDWRRVDG WPVGLKNVGN TCWFSAVIQS LFQLPEFRRL VLSYSLPQNI
LENCRSHTEK RNIVFMQELQ YLFALMMGSN RKFVDPSAAL DLLKGAFRSS EEQQQDVSEF
THKLLDWLED AFQLAVNVNN PRNKSENPMV QLFYGTFLTE GIREGKPFCN NETFGQYPLQ
VNGYRNLDEC LEGAMVEGDI ELLPSDHSMK YGQERWFTKL PPVLTFELSR FEFNQSLGQP
EKIHNKLEFP QIIYMDRYMY RSKELIRNKR ECIRKLKEEV QVLQQKLERY VKYGSGPARF
PLPDMLKYVI EFASTKPVSE SSLSQNDTHV TLPISSVHCQ VSDLTSKKST RPESSSEDVD
CIFSTCEDHL HKSEVMNRPL TSPRSPLGMP AHPAPRTVTP EEMIFVKTCL QRWRSEIEQD
IQDLKDCIAS TTETIEQMYC DPLLRQVPYH LHAVLVHEGQ ANAGHYWAYI YNQPRQIWLK
YNDISVTESS WEELERDSYG GLRNVSAYCL MYINDKLPHF NAETAPNESD QMIGELEALS
VELKHYIQED NWRFEQEIEE WEEEQSCKIP QMEASSSSVS QEFSPSQEPA VASSHGVRCL
SSEHAVIVKE QTAQAIANTA HAYENSGVEA ALSELKEAEP KKPRPQETNP AEQSEQPPKP
NVAESAAQPN SEVSEVEIPS VGRILVRSDA DGYDEEVMLS PAMQGVILAI AKARQTFDRD
GSEAGLIKAF HEEYSRLYQL AEEIPTSHSD PRLQHVLVYF FQNEAPKRVI ERTLLEQFAD
KNLSYDERSI SIMKVARAKL KEIGPDDMNM EEYKKWHEDY SLFRKVSVYL LTGLELYQKG
KYQEALSYLV YAYQSNAALL MKGPRRGVKE SVIALYRRKC LLELNARAAS LFETNDDHSV
TEGINVMNEL IIPCIHLIIN NDISKDDLDA IEVMRNHWCS YLGQDIAENL QLCLGEFLPR
LLDPSAEIIV LKEPPTIRPN SPYDLCSRFA AVMESIQGVS TVTVK
//
