ID H3BH21_LATCH Unreviewed; 395 AA.
AC H3BH21;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=OTUD3 {ECO:0000313|Ensembl:ENSLACP00000021192.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000021192.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000021192.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AFYH01015368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01015369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01015370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01015371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01015372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BH21; -.
DR STRING; 7897.ENSLACP00000021192; -.
DR Ensembl; ENSLACT00000021332.1; ENSLACP00000021192.1; ENSLACG00000018617.1.
DR eggNOG; ENOG502QUTD; Eukaryota.
DR GeneTree; ENSGT00390000016392; -.
DR HOGENOM; CLU_056188_0_0_1; -.
DR InParanoid; H3BH21; -.
DR OMA; TDFQILH; -.
DR TreeFam; TF329594; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000018617; Expressed in pelvic fin and 6 other cell types or tissues.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd22770; OTU_OTUD3; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12419:SF7; OTU DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 60..184
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 45008 MW; 4B735D621FF791FF CRC64;
MSRKQIIKGK PNKKAELERK RDEKAARRAL AKERKNRAQE GGEDDEEFVS FANQLQVMGL
KLREVPGDGN CLFRALGDQL EGHSLNHLKH RQETVDYMIQ HREDFEPFVE DDVPFDKHVS
NLAKPGTFAG NDAIVAFARI NQVNVVIHQL NAPLWQIRGT DKLNARELHI AYRYGEHYDS
VRRVSDNSES PAHLKMEDGF HLMRSIVFKF PVQGWGGHLT RRHSVFEEVS QFCSFDTSFE
AGFSCFRSSL VYPSIGTQNN KMESVSLSTM FANQGGSAVF EPSLGGDEEV RETQSSLWNE
HGSGSRIFGN QSFNTENNRV QSSTSEENKG NRNKAAKLSN KQRKEQQRLE KKRRQEERHR
QKVIEGKSNR ADNNENKPGS DTKVTLVKTF ATLNI
//
