OTU6B_DANRE
ID OTU6B_DANRE Reviewed; 293 AA.
AC Q7ZV00;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Deubiquitinase OTUD6B {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q8N6M0};
GN Name=otud6b; ORFNames=zgc:56305;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme that may play a role in the
CC ubiquitin-dependent regulation of different cellular processes.
CC {ECO:0000250|UniProtKB:Q8N6M0}.
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:0000250|UniProtKB:Q8N6M0};
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DR EMBL; BC046060; AAH46060.1; -; mRNA.
DR RefSeq; NP_956519.1; NM_200225.1.
DR AlphaFoldDB; Q7ZV00; -.
DR SMR; Q7ZV00; -.
DR STRING; 7955.ENSDARP00000110547; -.
DR MEROPS; C85.009; -.
DR PaxDb; Q7ZV00; -.
DR GeneID; 393194; -.
DR KEGG; dre:393194; -.
DR CTD; 51633; -.
DR ZFIN; ZDB-GENE-040426-974; otud6b.
DR eggNOG; KOG2606; Eukaryota.
DR InParanoid; Q7ZV00; -.
DR OrthoDB; 1541668at2759; -.
DR PhylomeDB; Q7ZV00; -.
DR PRO; PR:Q7ZV00; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..293
FT /note="Deubiquitinase OTUD6B"
FT /id="PRO_0000076282"
FT DOMAIN 147..284
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..158
FT /note="Cys-loop"
FT /evidence="ECO:0000250"
FT REGION 219..229
FT /note="Variable-loop"
FT /evidence="ECO:0000250"
FT REGION 267..277
FT /note="His-loop"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /evidence="ECO:0000250"
FT ACT_SITE 158
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N6M0"
FT ACT_SITE 277
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 33507 MW; D8BE7A4E2742F3AB CRC64;
MEEVETAEEQ LAKQHRKEKK DLQAKIQSMK NAVPKNDKKR RKQLTEDIAK LEAELSQKHE
NELKLQNTSS VEEVSDALDS MSVANHEEQS DPSKQSRTSK AQKRRDKKAA LEKEREMRIA
EAEVENLSGS RHQEGLKLRE KLVERHLQIK EISSDGHCMY RAVEHQLTER GLALGLKELR
DQTAQYMRSH ADDFMPFLTN PNTGDMYTAE EFEKYCSDVA DTAAWGGQLE LKALSQVLQL
PIEVIQADSP CITIGEEYDK PKITLIYMRH AYGLGEHYNS VEPLKDLANE EEG