ID A0A091JDD1_EGRGA Unreviewed; 802 AA.
AC A0A091JDD1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE Flags: Fragment;
GN ORFNames=Z169_10934 {ECO:0000313|EMBL:KFP17715.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP17715.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP17715.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP17715.1};
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KK501770; KFP17715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JDD1; -.
DR STRING; 188379.A0A091JDD1; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR CDD; cd02667; Peptidase_C19K; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_03062; UBP16; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR030849; UBP16.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF12; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 16; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 3..123
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 174..801
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 126..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP17715.1"
FT NON_TER 802
FT /evidence="ECO:0000313|EMBL:KFP17715.1"
SQ SEQUENCE 802 AA; 91335 MW; 4E3E328EEF5D631D CRC64;
VEPVCKHIRK GLEQGHLKKA LLNVEWHVCQ DCKADNKTEE KSEEETDESP SIWLCLKCGH
RGCGRNSQEQ HALKHYTTPR SDPHCLVLSL DNWRLIFFFG GGGWAYSTSS RLGQTVDYVR
KQVCTDSPRT EKQQEKKEFE NKKVEKDSKN EQEKEVSLKE ENSHSNTNSE VTVKGLSNLG
NTCFFNAVMQ NLSQTPVLRE LLKEAKMPGA TVKIESTELS MEPQLIKLDQ PGPLTLAMYQ
FLTEMQETKK GVVTPKELFA QVCKKAIRFK GYQQQDSHEL LRYLLDGMRA EEIQQVSVGI
LKALTDSNKQ NEEELKKKIK EYEKKKGIQS FVDRIFGGEL TSTIMCEECR TVSLVHESFL
DLSLPVLDDQ KVKITNERNV KKTKEKESED EEDKNNDCYL KQRDEPSGTS KHLQKKAKKQ
AKKQAKSQRR QQKLQGKVLH LTDICATEQS EKDVEHNQES EAEIETPDMK QEEESSNDCE
GHCLTQKDLN IQGNSTEVHS MHENTGKPEH ECVENESLGD LPVEGLDSPT KFVNGLDNLS
LKDEDDENED EEELTTGFSE LHLGASAKSD NSILDDLQTV PVKTCEVSTE DPERAFCTLA
NREDLNPEEG SIYHCLYQFT RNEKLTETNK LLCDVCTQRH YGPKKNIKSE KKYVYTNAKK
QMLISFAPPI LTLHLKRFQQ AGFNLRKVNR HIKFPEVIDL APFCTAKCKN VAEGNTKVLY
SLYGVVEHSG TMRSGHYTAY AKMRSMNNHL SDLVLRGQSP QALDTEPVKG QWFHISDTHV
QAVSAAKVLS SQAYLLFYER LL
//
