ID A0A091F5X5_CORBR Unreviewed; 1097 AA.
AC A0A091F5X5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Ubiquitin carboxyl-terminal hydrolase 8 {ECO:0000313|EMBL:KFO63969.1};
GN ORFNames=N302_16258 {ECO:0000313|EMBL:KFO63969.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO63969.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO63969.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO63969.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK719540; KFO63969.1; -; Genomic_DNA.
DR RefSeq; XP_017598099.1; XM_017742610.1.
DR AlphaFoldDB; A0A091F5X5; -.
DR STRING; 85066.A0A091F5X5; -.
DR GeneID; 103621270; -.
DR CTD; 9101; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR048498; WW_USP8.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF27; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 8; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR Pfam; PF20625; WW_USP8; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KFO63969.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976}.
FT DOMAIN 194..312
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 756..1088
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 122..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 125855 MW; CF496C0D7A34FEA7 CRC64;
MPAVASVPKE LYLSTSLKDL NKKTEVKPEK TSTKSYVQSA LKIFKAAEES RLDGDEEKAY
ILYMKYAAVY NLIRKRPDFK QQQDYFHSIL GPTNLKKALD EAEILSDSLK LRYEEAEVRK
KLEERDRQEL QKKQEPKDDG KSSAKNSSES AVDSKGKSQR INGETKHSLE RKDQSDSLSG
AVTPEKLFAM MSDKNTELLI MDARRLKDYQ ESCIPKSISV PEEAIHPGDT ANLIEARLPE
DSRDPWKRRG QFHYVILLDW FSTAEDLKLG TTLQSLKDAL FKWESKTILQ NEPLILEGGY
ENWLLCFPQY TTNARVTPPQ HGRTEAVTVS LDFTYPSLEE PAPVPPVVAV KPCPTETIEN
EEMGDNLEER LKSLNKPNIQ DAAVPKSDSS FVVNPVLSTR SIPEVDRTKK PSLKILDDNR
AKPPSTVSDS QSGENGRIVP DRSTKPVRDA RSALTEEEKS RVHAETAALL EKNRREKELR
ERQQQEQKER LKREKEEQER KEKEKQEQKA KEEQKEKEHK EKLQQSKEDR EQKERDEQIK
REQEEKEQER AHREAVEAKK QNKNEPENIG AKRIEFDKIS MEEREKGTPE TQKRALGDAS
QTFVTVPGKS QREPLMRARS EEMGRIVPGL PAGWVKFLDD ITGTYRYYHS PTNTVQMYPP
EMAPSSTPPS TPPTRKAKPK VTVEREREHS KLKRSYSSPD ITQAIQEEEK KRIPVTPAVN
RDNKPACYTK AEISRLSASQ IRNLNPVFGG SGPALTGLRN LGNTCYMNSI LQCLCNAPHL
AEYFNRNLYQ ADINRSNFLG HKGEVAEEFG VIMKALWAGQ YKYISPKDFK ITIGKINDQF
AGYSQQDSQE LLLFLMDGLH EDLNKADNRK RYKEENNDHL DDSSAAEIAW HKHKQLNESI
IVALFQGQFK STVQCLTCHK RSRTFEAFMY LSLPLASSSK CTLQECLRLF SKEEKLTDNN
RFYCSHCKTR RDSSKKIEIW KLPPVLLVHL KRFSYDGRWK QKLQTSVDFP LETLDLSQYV
IGPKTSLRRY NLFSVSNHYG GLDGGHYTAY CKNASKQRWF KFDDHEVSEI SASSVKSSAA
YILFYTSYEQ RAVDMAT
//
