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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
 
 
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