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Database: UniProt
Entry: A0A093D1K5_TAUER
LinkDB: A0A093D1K5_TAUER
Original site: A0A093D1K5_TAUER 
ID   A0A093D1K5_TAUER        Unreviewed;       355 AA.
AC   A0A093D1K5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 33.
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=N340_04042 {ECO:0000313|EMBL:KFV18984.1};
OS   Tauraco erythrolophus (Red-crested turaco).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX   NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV18984.1, ECO:0000313|Proteomes:UP000053661};
RN   [1] {ECO:0000313|EMBL:KFV18984.1, ECO:0000313|Proteomes:UP000053661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV18984.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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; KL471341; KFV18984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093D1K5; -.
DR   Proteomes; UP000053661; 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:UP000053661};
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          184..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..323
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:KFV18984.1"
FT   NON_TER         355
FT                   /evidence="ECO:0000313|EMBL:KFV18984.1"
SQ   SEQUENCE   355 AA;  40664 MW;  B89E97FE964459F4 CRC64;
     QEGSLCAQHC LNNLLQGEYF SPVELSSIAQ QLDEEERMRM AEGGVSSEEY RTFLQQPSVN
     MDDSGFFSIQ VISNALKVWG LELILFNSPE YQRLGIDPIN EKSFICNYKE HWFTVRKLGK
     QWFNLNSLLM GPELISDTYL ALFLAQLQQE GYSIFVVKGD LPDCEADQLL QMIRVQQMQR
     PKLIGEETAQ PRDQRLPRSD ADQAIEVNHP FDGTGMLDED EENFQRALAL SRQEIDMEDE
     EADLRRAIQL SMQGSRRSEF LDSLPQNVPQ SPHTSQTDSL SSEELRQRRQ AYFEKQQQQL
     QQQDQTSDLH DKPTPSSSTL EADPGGDMSE EDMLQAAMNM SLESVRNHLS TEEEK
//
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