ID A0A444UN06_ACIRT Unreviewed; 1252 AA.
AC A0A444UN06;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=EOD39_11750 {ECO:0000313|EMBL:RXM36518.1};
OS Acipenser ruthenus (Sterlet sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7906 {ECO:0000313|EMBL:RXM36518.1, ECO:0000313|Proteomes:UP000289886};
RN [1] {ECO:0000313|EMBL:RXM36518.1, ECO:0000313|Proteomes:UP000289886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WHYD16114868_AA {ECO:0000313|EMBL:RXM36518.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RXM36518.1};
RA Wei Q.;
RT "Draft Genome and Complete Hox-Cluster Characterization of the Sterlet
RT Sturgeon (Acipenser ruthenus).";
RL Submitted (JAN-2019) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXM36518.1}.
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DR EMBL; SCEB01214221; RXM36518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444UN06; -.
DR Proteomes; UP000289886; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0023051; P:regulation of signaling; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd09616; Peptidase_C12_UCH_L1_L3; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR031865; DUF4757.
DR InterPro; IPR029978; LMO-7.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR46767; LIM DOMAIN ONLY PROTEIN 7; 1.
DR PANTHER; PTHR46767:SF1; LIM DOMAIN ONLY PROTEIN 7; 1.
DR Pfam; PF15949; DUF4757; 2.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00140; UCH_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000289886};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 85..101
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|PROSITE:PS00140"
FT REGION 276..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 904..938
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 283..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1252 AA; 139583 MW; AA1A351422DD9837 CRC64;
MESQRWLPLE ANPDFLKQLG LLPTWQFGDV YGLDPDLLSM VPRPVCSVLL LFPVTEKYES
YRLEEEAKIK SQSQEVSSEV YFMKQTISNA CGTIGLIHAV ANNQDRLEFG PGSALKKFLS
ESRSLSPEKK AKFLEEDESI RVTHESSAQE GQTEDNINVF LKACGRLGLK EAQLFHPGDL
QDLSSRVTVK REETSRRLKN VLITIYWLGR KAQTDAVYNG PFLNLKAFEG LLGTALSKAL
EDCGSLKRSG RDSGYADSWY TDRGELLSLP ASHRRDDSLD SLDSVGSRSA SISSGATLKG
SSEGCGSDLS ESDSPFRMTE NKDSMSYRRI AVVEPKSSTQ FNQFLPSKSS QSGYVPAPLR
KKRVDRNEDN RRSWASPMFT ESDGSFSSGE ELGPGHTSQN GQTSRDYPLP ENQQAAYQYE
SGSDSEAEAR QPDVVLDDLA SRRFQMNRSV SPANYAKPLH MSDAGCPRSG PLWLGFSSAT
LDQEVGSTSS LRQCGGSKVE SGTPATGPFP LNDTCSYSEE EDDNSSPDVC KDDLYARKVG
VVLLPTANVP YDKYLPKYWT PEEDQHVQKI KVGSQRRPWY RKFQGFRKWQ SDSEEEDSDC
EGNPFSASSP VSEQRKLETT MHLGNLQRSE AAGPIPCEST SDVSRTRDQQ SPCTLDHDSN
DLELVEPPVS MPRVDAAAGR RIIKCERSSF LSPLNQQDGK DAQEGLLPDL ENDDMFTRRT
GSFHSNVDLM RYETKGRQSA ELPPEPDVKI VTQPRRGEPV VPDIERDDMV FRKVNFNSQK
KVRSPSGAPH VYHPVPIPEP WTLPANLQSK LLCQPNPPMP EEEEEEGEGR QYSIHPKTDD
MSARKLGKVH PPQAVLPSPF VPTSCSEQDL KKWEAIREGS RLRYKKRKMV ERSKSMSDVS
EEAVANRQIR FEELQKIKSQ LQEQDQQWQN DLTKWKNRRK SFTSDLVKKK EEREQIDQTV
GRRVKTFKEM QEERQDREQG IQSTELRAPS NRSLYASNEE VFTDEKPMSK TLRERSYTVE
VDTPYSSQNS EVTRSTPAYN PQKDDATITA TTSTSKAAQS NSSVSEAAGS QRTSQSPSEE
QSSVSLYAHN SMDTKPGVAR VSASLPRSYQ RPDSTRLTSI VAPRPFGTQS NRVSSLPRAV
AMDSAHSQYN GDLDSASQKT YSTSRYSQVM KMEDDGPSQS SSVLSSTEEG RTPSPKPAPS
AQPRDELTSS HVIESNPDHP SSSAKTQYVA STSTSTIKVP EAKVTTQVSS EK
//
