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Database: UniProt
Entry: A0A3B4B8A3_9GOBI
LinkDB: A0A3B4B8A3_9GOBI
Original site: A0A3B4B8A3_9GOBI 
ID   A0A3B4B8A3_9GOBI        Unreviewed;      1210 AA.
AC   A0A3B4B8A3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
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:ENSPMGP00000025728.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000025728.1}
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};
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DR   AlphaFoldDB; A0A3B4B8A3; -.
DR   Ensembl; ENSPMGT00000027401.1; ENSPMGP00000025728.1; ENSPMGG00000020748.1.
DR   Proteomes; UP000261520; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028135; Ub_USP-typ.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
FT   DOMAIN          39..248
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          397..1173
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          99..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1210 AA;  135611 MW;  87104499C8ACEF49 CRC64;
     LGHLTLEDYQ IWSVKSALAN EFLNLLFQVC HIVLGLRPAT PEEEGQIIRG WLERESRHGL
     QQGQNWFLIS MQWWQQWKDY VKYEQKGIVV EQPSVLSSLR STAPPVCPEA DSRGAWSPQS
     SVSPSEERSP DTLSSASEAT ETTVGPLPSS ASESCFARPH HASENPQCFS APNGHLPQLC
     PQRPAAIDNQ PLVNMDPIKA PTLTMEGGRL KRSLQLVPGR DFEIVPEPVW RALYHWYGAN
     LSLPRPVILE SRTKIPELEL FPRYLLFLRQ QPATRSPQSN IWVNLGNVPS PNAPLKRALA
     YSGCFSRMGT IKDIHLYLSQ RLRIKEEDMR LWLYNSENYL TLLDDEDHTL ESLKIHDEQQ
     LVIEVRNKDM SWPEEMSFIA NSSKMDRHKV PTEKGATGLS NLGNTCFMNS SIQCVSNTKP
     LTDYFISGTH LYELNRYNGT QKNVAPLKLR WTIAKYAPRF NGFQQQDSQE LLAFLLDGLH
     EDLNRVHEKP YVELKDSDGR PDWEVASEAW ENHLRRNRSI VVDLFHGQLK SQVKCKTCGH
     ISARFDPFNF LSLPLPMDSS MHLEITVIKL DGSTPVRFGL RLNMDEKYTG LKKQLSELCS
     LKPEQILLAE VHSSNIKNFP LDNQKVRMSV NGFLCAFEIP VPGSPTSLSS PTLTDITPIA
     NGSALNGHLI PNGGPSSVPP SSPETPLVNG VANGHLTPLQ DSPFIGYIIA MHRKMMRSEL
     YFLSSQKNRP SLFGMPLIVP CTVHTSKKDL YDAVWVQVSR LASPLPPQES SNHAQDCDDS
     MGYQYPFTLR VVGKGGNSCA WCPWYRFCRG CTIDCTEERA SVGNAYIAVD WDPTALHLRY
     QTSQERIVEE HSSVEQSRRA QAEPISLDSC LRAFTSEEEL PPILVLTTTV YCYYYCYCYC
     YYKTHGIVHL KRFQFVNGRW IKSQKIVKFP REKFDPGAFL APRDRGQHCP YSRSESDDLL
     RVGEDNLSSI SAPAGFNNLH KASPCSSRKS APSLSRNSSP SGSPKTGVRR PGRLRLPQLG
     SKHRLCSSSK ENIHTETCAE GNHAGEGEEP QADGPDQTGP GLCGSAEVLA SESSVGTDAS
     HCDVVLMNGN GLNSDCSTES SLDQDLTRDL GLEAIYNLYA ISCHSGIMGG GHYVTYAKNP
     NGKWYCYNDS SCKEVHSGEM DTDSAYILFY EQQGVDYSQF LPQIDGKKMA DTSSMDEDFE
     SDYKKYCVLQ
//
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