ID A0A3Q0G4E0_ALLSI Unreviewed; 295 AA.
AC A0A3Q0G4E0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=USP15 {ECO:0000313|RefSeq:XP_025054561.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025054561.1};
RN [1] {ECO:0000313|RefSeq:XP_025054561.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_025054561.1; XM_025198776.1.
DR AlphaFoldDB; A0A3Q0G4E0; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; IPR028135; Ub_USP-typ.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR018200; USP_CS.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|RefSeq:XP_025054561.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT DOMAIN 1..103
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 201..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 295 AA; 34135 MW; 4D0288FAC7A47BE2 CRC64;
MTKTFLEVME RNATWYLVDS RWFKQWKKYV GFDSWDKYQM GDQNVYPGPI DNSGLLKDGD
SQSLKEHLID ELDYILLPTE GWNKLVSWYT LMEGQEPIAR KVVEQGMFVK HCKVEVYLTE
LKLCENGNMN NVVTRRFSKA DTIDTIEKEI RKIFNIPSEK ETRLWNKYMS NTFEPLNKPD
STIQDAGLYQ GQILVIEQKN EDGTWPRGPS TPKSPGASNF STLPKISPSL SNNYNNINNR
NVKNSNYCLP SYTAYKNYDY SEPGRHNEQP GLCGLSNLGN TCFMNSAIQK TRKWN
//
