ID A0A0A0A234_CHAVO Unreviewed; 355 AA.
AC A0A0A0A234;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE Flags: Fragment;
GN ORFNames=N301_10532 {ECO:0000313|EMBL:KGL87992.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL87992.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL87992.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL87992.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL870348; KGL87992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0A234; -.
DR STRING; 50402.A0A0A0A234; -.
DR MEROPS; C86.001; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.40; -; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR InterPro; IPR033865; Ataxin-3.
DR InterPro; IPR006155; Josephin.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR14159; ATAXIN-3-RELATED; 1.
DR PANTHER; PTHR14159:SF0; ATAXIN-3-RELATED; 1.
DR Pfam; PF02099; Josephin; 1.
DR Pfam; PF16619; SUIM_assoc; 1.
DR Pfam; PF02809; UIM; 3.
DR PRINTS; PR01233; JOSEPHIN.
DR SMART; SM01246; Josephin; 1.
DR SMART; SM00726; UIM; 3.
DR PROSITE; PS50957; JOSEPHIN; 1.
DR PROSITE; PS50330; UIM; 3.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00331}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..172
FT /note="Josephin"
FT /evidence="ECO:0000259|PROSITE:PS50957"
FT REGION 253..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 6
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 6
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 111
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1,
FT ECO:0000256|PROSITE-ProRule:PRU00331"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL87992.1"
FT NON_TER 355
FT /evidence="ECO:0000313|EMBL:KGL87992.1"
SQ SEQUENCE 355 AA; 40673 MW; C6B02A83CBB47DEF CRC64;
QEGSLCAQHC LNNLLQGEYF SPVELSSIAQ QLDEEERMRM AEGGVSSEEY RTFLQQPSVN
MDDSGFFSIQ VISNALKVWG LELILFNSPE YQRLGIDPIN EKSFICNYKE HWFTVRKLGK
QWFNLNSLLM GPELISDTYL ALFLAQLQQE GYSIFVVKGD LPDCEADQLL QMIRVQQMQR
PKLIGEETAQ TRDQRLPRSD VDQAIEVNHP FDGTGMLDED EANFQRALAL SRQEIDMEDE
EADLRRAIQL SMQGSRRSQF SDSLPQNVPQ SPHTSQTDSL SSEELRRRRQ AYFEKQQQQL
QQQDRTPNLH DKPALSSSTP EADPGGDMSE EDMLQAAMNM SLESVRNHLN TEEEK
//
