ID A0A091DPU6_FUKDA Unreviewed; 1106 AA.
AC A0A091DPU6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7 {ECO:0000256|ARBA:ARBA00021393};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Ubiquitin thioesterase 7 {ECO:0000256|ARBA:ARBA00031508};
DE AltName: Full=Ubiquitin-specific-processing protease 7 {ECO:0000256|ARBA:ARBA00031500};
GN ORFNames=H920_13832 {ECO:0000313|EMBL:KFO24836.1};
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:KFO24836.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO24836.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO24836.1};
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; KN123497; KFO24836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DPU6; -.
DR STRING; 885580.ENSFDAP00000007233; -.
DR MEROPS; C19.016; -.
DR eggNOG; KOG1863; Eukaryota.
DR Proteomes; UP000028990; 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; cd03772; MATH_HAUSP; 1.
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; PF00917; MATH; 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, ECO:0000313|EMBL:KFO24836.1};
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 60..187
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 206..513
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1106 AA; 128737 MW; B5F311EBCAF7E7E7 CRC64;
MIRGLACVHC DKFKHVFSSG DTDDPPRITQ NPVINGNVAL SDGHSNVEED MEDDTSWRSE
ATFQFTVERF SRLSESVLSP PCFVRNLPWK IMVMPRFYPD RPHQKSVGFF LQCNAESDST
SWSCHAQAVL KIINYRDDEK SFSRRISHLF FHKENDWGFS NFMAWSEVTD PEKGFIDDDK
VTFEVFVQAD APHGVAWDSK KHTGYVGLKN QGATCYMNSL LQTLFFTNQL RKAVYMMPTE
GDDSSKSVPL ALQRVFYELQ HSDKPVGTKK LTKSFGWETL DSFMQHDVQE LCRVLLDNVE
NKMKGTCVEG TIPKLFRGKM VSYIQCKEVD YRSDRREDYY DIQLSIKGKK NIFESFVDYV
AVEQLDGDNK YDAGEHGLQE AEKGVKFLTL PPVLHLQLMR FMYDPQTDQN IKINDRFEFP
EQLPLDEFLQ KTDPKDPANY ILHAVLVHSG DNHGGHYVVY LNPKGDGKWC KFDDDVVSRC
TKEEAIEHNY GGHDDDLSVR HCTNAYMLVY IRESKLSEVL QAVTDHDIPQ QLVERLQEEK
RIEAQKRKER QEAHLYMQVQ IVAEDQFCGH QGNDMYDEEK VKYTVFKVLK NSSLAEFVQS
LSQTMGFPQD QIRLWPMQAR SNGTKRPAML DNEADGNKTM IELSDNENPW TIFLETVDPE
LAASGATLPK FDKDHDVMLF LKMYDPKTRS LNYCGHIYTP ISCKIRDLLP VMCDRAGFIQ
DTSLILYEEV KPNLTERIQD YDVSLDKALD ELMDGDIIVF QKDDPENDNS ELPTAKEYFR
DLYHRVDVIF CDKTIPNDPG FVVTLSNRMN YFQVAKTVAQ RLNTDPMLLQ FFKSQGYRDG
PGNPLRHNYE GTLRDLLQFF KPRQPKKLYY QQLKMKITDF ENRRSFKCIW LNSQFREEEI
TLYPDKHGCV RDLLEECKKA VELGEKASGK LRQVFLETDG RGRRLLEIVS YKIIAVHQED
ELLECLSPAT SRTFRIEEIP LDQVDIDKEN EMLITVAHFH KEVFGTFGIP FLLRIHQGEH
FREVMKRIQS LLDIQEKEFE KFKFAIVMMG RHQYINEDEY EVNLKDFEPQ PGNMSHPRPW
LGLDHFNKAP KRSRYTYLEK AIKIHN
//
