ID A0A0R3RWD6_9BILA Unreviewed; 1073 AA.
AC A0A0R3RWD6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000647001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000647001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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}.
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DR AlphaFoldDB; A0A0R3RWD6; -.
DR STRING; 1147741.A0A0R3RWD6; -.
DR WBParaSite; EEL_0000647001-mRNA-1; EEL_0000647001-mRNA-1; EEL_0000647001.
DR Proteomes; UP000050640; 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 1..134
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 153..469
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1073 AA; 123729 MW; 2E72582C5912AD24 CRC64;
MDIDHFSDFS RGSSETHQKL SEPIFVRGLP WRILAMPREQ NRFQSERRSA GRAFGFFLQC
NGEAEAISWS CTASAILTVL SQKSGVENHV RRINHTFYQK ENDWGYSQFL PCETLLNPES
GYIKDDTIKL EVLVMADAPH GVQWDSKKHA GFIGLKNQGA TCYMNSILQT FFFTNQLRKA
VYQMPTENDD PETSVALAMQ RVFYELQNSD KPVGTKKLTK SFGWDSVESF HQHDVQELCR
VLLDNLENKM SGTKVKNTIP SLFEGKMKSY VRCKNVCFES NRVESFYDLQ LNIKGKANGM
FFRWSFLESF SDYTAAEILD GDNKYDAGEF GLQPAVKGVK FISFPPILHL QLMRFQYDAL
QDANVKINDR FEFPALLNLN AFIEDGDKKE PQDFLLHAVL VHSGDFHGGH YVVFINTNLG
GPPKWCKFDD DVVSRASVRD AIEANYGGDD PDLPGKSFTN AYMLVYIKKN SINDVLCPVT
EEDIPRHLRL RFEEEKSADA KKKKEKLEAH LFTELIVVLE EHMYNYSGFD LFDPKVLDEA
RRLKVEKKMT IDQLYALFAE EFHLSENNFR LWQVHENTIR DERNNALSLN RLRPSTLLKR
DSERPHSNRV DMVLEGDRNI IFLETAQDSG TSANGLPPYN ESNDMMFFLK YYDADEKMTF
FCGHIMINYK SMIRNYLPQI LQKAHLPPGT ELKFYEEIAP ERMRPLCIDD MISQDHALVD
LVDGALLVFE RTDKSTTENN AHLYYTTKYN AMQIEALQNP EGFGTPLNEQ FDPILGEISQ
TWTMGQLMQW IASGIGCSAD HILLWKVSQY NEKPTNNHLN EHELRVYSVK DLLGLTGPHR
HDPRRQKRYR VYYTKMPISV SDLERRYKMR VQMMDEKMQI TETTVFPEKT GTVQSILDEA
QREFRFSAKG TKLLRLVYVG QASHCLRAYH VFTNDTLASE IYTKIGNTSY AVRVEEIPED
EVTIRSGEHL LPVGHFDKVS SVFPCRYRFI RSSYSDSELF ENEPVFLQYK FAIIVNNRVS
KYLDKDNVVN LNELSHTHIT GYASAPWLGL DHMNKSRGTR GSHTTEKAIV IHN
//
