ID   A0A0N4TV17_BRUPA        Unreviewed;      1250 AA.
AC   A0A0N4TV17;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 31.
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=BPAG_LOCUS12628 {ECO:0000313|EMBL:VDN93814.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001266601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0001266601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN93814.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UZAD01013308; VDN93814.1; -; Genomic_DNA.
DR   STRING; 6280.A0A0N4TV17; -.
DR   WBParaSite; BPAG_0001266601-mRNA-1; BPAG_0001266601-mRNA-1; BPAG_0001266601.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          156..294
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          313..629
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   1250 AA;  143338 MW;  0EB30FC168D8E503 CRC64;
     MPTHKLFRSV RILKRNSPLQ AGGCRGRRVS VCVAFETVLL GVAVGGKRVF WICVFIKRAH
     YKWHCNTIAS EMTNDLGSGQ RGREMKNSDT DDDVDNGVPF AEEHENKENA RGRVNFLKAS
     AQHNNQEDAM DTAYVNEGRS SPLPGDCEED DPYKPEGVLR MDIDHFSDFA RGSSETHQKL
     SEPIFVRGLP WRILAMPREQ NRFQSERRSA GRAFGFFLQC NGEAEAISWS CTASAILTVL
     SQKPGVENHV RRINHTFYQK ENDWGYSQFL PCETLLNPES GYIKDDTIKL EVLVMADAPH
     GVQWDSKKHA GFIGLKNQGA TCYMNSILQT FFFTNQLRKA VYQMPTENDD PETSVALAMQ
     RVFYELQNSD KPVGTKKLTK SFGWDSVESF HQHDVQELCR VLLDNLENKM SGTKVKNTIP
     SLFEGKMKSY VRCKNVCFES NRVESFYDLQ LNIKGKANVL ESFSDYTAAE ILDGDNKYDA
     GEFGLQPAVK GVKFISFPPI LHLQLMRFQY DALQDANVKI NDRFEFPALL NLNAFIEEGD
     KKEPQDFLLH AVLVHSGDFH GGHYVVFINT NLGGPPKDMG THFQWCKFDD DVVSRASVRD
     AIEANYGGDD PDLPGKSFTN AYMLVYIKKS CINDVLCPVA EEDIPRHLRL RFEEEKSADA
     KKKKEKLEAH LFTELIVILE EHMYSYSGFD LFDPKILDEA RRLKVEKKMS IDQLYTLFAE
     EFHLSENNFR LWQVHENTIR DERNNALSLN RLRPSTLLKR DGERPHSSRV DMALEGDRNI
     VFLETAQDSG NSLNGLPPYN ESNDMMFFLK YYDADEKMTF FCGHIMINYK SMIRNYLPQI
     LQKARLPPGT ELKFYEEIAP DRMRPLCIDD MISQDHALVD LVDGTLLVFE RTDKSTTENN
     AHLYYTTKYN AMQVEALQNP EGFGTPLNEQ FEPILGEISQ TWTMGQLMQW IASGIECSAD
     HILLWKVSQY NEKPTNNHLN EHELRVYSVK DLLGLTSPHK HDPRRQKRYR VYYTKMPISV
     SDLERRYKMR VQMMDEKMQI TETTVFPEKT GTVQSILDEA QREFRFSPNG TKLLRLVYVG
     QASHCLRAYH VFTNDTLASE IYTKIGNTSY AVSLPSHSVR VEEIPEDEVT VRPGEHLLPV
     GHFDKDPTRM FGIPFFIKVT NGETLESVSE RIRKKLDVTV KEFEKYKFAI IVNNRVSKYL
     DKDNVVNLNE LSHTHITGYA SAPWLGLDHM NKSRGTRGSH TTEKAIVIHN
//