ID   A0A1S3LR25_SALSA        Unreviewed;      1230 AA.
AC   A0A1S3LR25;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=LOC106567933 {ECO:0000313|RefSeq:XP_013993316.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013993316.1};
RN   [1] {ECO:0000313|RefSeq:XP_013993316.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013993316.1};
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_013993316.1; XM_014137841.1.
DR   AlphaFoldDB; A0A1S3LR25; -.
DR   GeneID; 106567933; -.
DR   OrthoDB; 1423057at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa13.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02665; Peptidase_C19I; 1.
DR   CDD; cd14354; UBA_UBP25; 1.
DR   CDD; cd20486; USP25_C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00726; UIM; 3.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|RefSeq:XP_013993316.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          215..706
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          459..486
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        773..788
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..891
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1230 AA;  139950 MW;  70581C516DB115B2 CRC64;
     MTVEQNVLQQ HSQKAEQATD GTQTAELGTD MQGQTGRDRE SQHQQTLLNQ LREVTGTTDV
     QLLQQALQVS NGDLAEAVAF LTEKNAKVPQ QDEAAYYQTT QVGNDRYISV GSQADTSEYL
     PHPALPGAVP SQGVTNVIDL TGDDKDDLQR AIALSLEESS RAFRETGITD EEQAISRVLE
     ASIAENKASL KRTHTEVWSD SPNPHDRKRM ENCPVGLKNV GNTCWFSAVI QSLFNLLEFQ
     RLVLHYSPPA RVQDLPRNQK EHRNLPFMQE LRNLFSLMVG SKRKYVDPSR AVEILKDAFK
     SSESQQDVSE FTHKLLDWLE DAFQMKAEED REGEKPKNPM VELFYGRFQA VGVLEGKKFE
     NTEMFGQYPL QVNGFKDLHE CLEAAMIEGE IESLHSSAEN SAKSGQEHWF TELPPVLTFE
     LSRFEFNQAL GRPEKIHNKL EFPSMLYMDR YMDRNREITR IKREEIRRLK EQLTLLQQRL
     ERYLSYGSGP KRFPLADVLQ YAMEFASSKP VCTSPLEDID TSAPPGGTTG QLLPALSTAE
     QGPSCTLPEG LAAAPTQAPS TQQRVPIHKP FTHSRLPPDL PMHPAPRHIT EEELRVLEGC
     LHRWRSEVEN DTHDLQGSIS RIHRTIELMY SDKSMMQVPF RLHAVLVHEG QANAGHYWAY
     IYDPHQQRWM KYNDISVTKS SWEELVRDSF GGYRNASAYC LMYINDKKPF LIEEEFDKET
     GQMLSGLDKL PSDLKAYVKE DNGLFDKEME EWDKLQARKA QQEKLALAAA AAATAETTTS
     HQPMSTEPSP PDSWGPQQDP EYMEQPSPTD DSKHLQEDTE RAISKAAAEQ QEERSPEGLL
     TASSGGSLSP PLPPKPQSDV QVNTETPLAP PSDPQPVDPS LTPPSDPDPP MEDEPLSQRT
     IEVAIPQVGT FVIESEEGGY DDEAMMTPNM QGIIMSIGKA RSVFEKLGPE AAFFKAIKVE
     YTRLLRFAQE DTAPENDYRL QHVIVYFIHN QAPKKILERT LLMQFADRNL SFDERCKSIM
     KVARAKLDLV KPEEVNMEEY EMWHQDYRNF RETTIFLMIG LELFQKKCFV EALMYLIYSY
     QYNRELLVKG LYRGHNDELI GHYRRECLLK LNENAARMFE SGEEPEVCNG LSIMNELVVP
     CIPLLLVHDT EKDLLAVEDM RNRWCSYLGQ EMEPNLQEKL TDFLPKLLDC STEIKSFHDP
     PKLPTYSTLE LVERYGRVMA SLCRVPADGR
//