ID   A0A3B4APJ7_9GOBI        Unreviewed;      1056 AA.
AC   A0A3B4APJ7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
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   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000018286.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000018286.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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; A0A3B4APJ7; -.
DR   STRING; 409849.ENSPMGP00000018286; -.
DR   Ensembl; ENSPMGT00000019507.1; ENSPMGP00000018286.1; ENSPMGG00000014943.1.
DR   Proteomes; UP000261520; Unplaced.
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; 2.
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; 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          68..195
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          203..492
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1056 AA;  123473 MW;  628E934E4F0BD3E7 CRC64;
     MNHHHHTQQQ KAGEQQLSEP EDMEMEAGDT DEPPRIPANP VINGNVAMAD GHNNTEEDME
     DDTSWRSEAT FRFVVERFSR LSESVLSPSC FVRNLPWKIM VMPRFYPDRP HQKSVGFFLQ
     CNAESDSTSW SCHAQAMLKI VHYKDDEKSF SRRISHLFFH KENDWGFSNF MSWSDVTDPE
     RGFIEDDKVT FEVYVQADAP HGVAYLGLQE THSFNSDMIS LLYCRNVPLA LQRVFYELQH
     SDKPVGTKKL TKSFGWETLD SFMQHDVQEL CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV
     SYIQCKHVDY RSERIEDYYD IQLSIKGKKN IFESFKDYVA TEQLDGDNKY DAGEHGLQEA
     EKGVKFLTFP PILHLQLMRF MYDPQTDQNI KINDRFEFPD QLPLDEFLQK PDSKDPANYI
     LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK FDDDVVSRCT KEEAIEHNYG GHDDDLSVRH
     CTNAYMLVYI RESKLSEVLQ PMTDVDIPQQ LVERLQEEKR VEAQKRKERQ EAHLYMQVQM
     VTEDQFCGHQ GNDMYDEEKV KYTVFKVLKS STLQEFVQNL SQTMGFPQDQ MRLWPMQARS
     NGTKRPAMLD YEADCNKSMI DLSDNENPWT IFLETVDPEM AASGATLPKF DKDHDVMLFL
     KMYDPKTRSL SYCGHIYTPI SCKIIIPFTL LLKPNLTERI QDYDVSLDKA LDELMDGDII
     VFQKDDPEND SSELPTAKDY FRDLYHRVDV IFCDKTIHND PGFVVTLSNR MNYFQVAKTV
     AQRLNTDPML LQFFKSQGYR DGPGNPLRHN YEGTLRDLLQ FFKPRQPKKL YYQQLKMKIT
     DFENRRSFKC IWLNSQFREE EITLYPDKHG CVRDLLEECK KAVELSEKGS EKLRLLEIVS
     YKIIGVHQED ELLECLSPAA SRTFRIEEIP LDQVDLDKDT EMLIPVAHFH KEVFGTFGIP
     FLLKIRQGEP FREVMRRIQT MLDIQEKEFE KFKFAIVMMG RHQYITEDEY EVNLKDFEPQ
     PGNMSHPRPW LGLDHFNKAP KRGRYTYLEK AIKIHN
//