ID A0A0N5AEX3_9BILA Unreviewed; 1154 AA.
AC A0A0N5AEX3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 32.
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};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000280001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000280001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0N5AEX3; -.
DR STRING; 451379.A0A0N5AEX3; -.
DR WBParaSite; SMUV_0000280001-mRNA-1; SMUV_0000280001-mRNA-1; SMUV_0000280001.
DR Proteomes; UP000046393; Unplaced.
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; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 79..214
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 233..542
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 132176 MW; B46DDABB3316E94D CRC64;
MTNDIVSGER GKHLKNSDTD EEFETVHNLD DDPEKENIRS RQLHVRGHEE QMDTTDYTGL
SGGQSPLSDE GEKDPYKPEA TLHLDIPRFS EFARSREPYQ VLSKPVYVRG LPWRILAMPR
EQTKIDRRPQ GRAFGFFLQC NGEAEAISWS CSASATLIVL AQKPGFENYT RRISHTFYQK
ENDWGYSQFL SCETLLSPEN GYIKDDTIKL EVTVNADAPH GVQWDSKKHA GHIGLKNQGA
TCYMNSILQT FFFTNQLRKA VYQMPTENDD PETSVALAMQ RVFYELQKSD KPVGTKKLTK
SFGWDSVESF HQHDVQELCR VLLDNLENKM ADTKVKNTIP SLFEGKMQSF VRCKKVDFES
NRIESFYDLQ LNIKGKANVL ESFDDYTATE TLDGDNKYDA GEYGLQPAEK GVKFISFPPV
LHLQLMRFQY DAAQDANVKI NDRFEFPPLL NLDSYVEDGG VKESNEYMLH AVLVHSGDFH
GGHYVVFINT NMTGTPRWCK FDDDVVSRAS VRDAIDSNYG GDDPEMPGKS FTNAYMLVYV
RKSRLNEVLC TVTEDDIPRH LKIRFEEEKT ADAKKKKEKL EAHLFTEVTV IFEEQMFGYD
GFDLFDQKVI DSSKVLRVEK KLTSRQLYDL FSAEFNLKEG SFRIWVVNDN AVRDEKTNVL
SLTRLRPSTL LKKDKDKLCT VESQLDNDRN IVFVEVAFKS TGSSGLLPYS ESHDMMFFLK
YYDVTEKRTF FCGHLMINCK SAIRGYLPQI LEKACLPAGT LLNFYEEIAP ERLRPLSADE
AVSQDNGLAE IADGAILVFE RADIRSEENN AQVYYNTKFN AMLVEAVQNP DGFGTPLTEK
FEPILGEISQ MWNMEQVMEW IANEINCPSD RILLWKASQY NDKPHSNYVN DHEMAVYTVK
DLLGLSGPHR HDPRRQKRYR IYFTKMPVSV TELDSRYKMK LQCMDEKMQI SEITVFPEKT
GTVQSILKEA EREFHFSENG TRVLRLVYVG MVSHSLRVYQ VLPKEMPVSD VYAKIGSASY
GARVEEVPHD ELTIKSTEVL LSVGHFDKEP SRMFGVPFLI KVSNGETLEA VSERIRKKLD
VSEKDFEKYK FAIVQNNRVT KFLEPGHVVN LNELSHARIT VPLIGTPWLG LDHLNKSRGT
RGSYITEKAI VIHN
//
