GenomeNet

Database: UniProt
Entry: J4WB13_BEAB2
LinkDB: J4WB13_BEAB2
Original site: J4WB13_BEAB2 
ID   J4WB13_BEAB2            Unreviewed;      1017 AA.
AC   J4WB13;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000313|EMBL:EJP67315.1};
GN   ORFNames=BBA_03889 {ECO:0000313|EMBL:EJP67315.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP67315.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP67315.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP67315.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH725157; EJP67315.1; -; Genomic_DNA.
DR   RefSeq; XP_008597208.1; XM_008598986.1.
DR   AlphaFoldDB; J4WB13; -.
DR   STRING; 655819.J4WB13; -.
DR   GeneID; 19886901; -.
DR   HOGENOM; CLU_005922_0_0_1; -.
DR   InParanoid; J4WB13; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProt.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EJP67315.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002762}.
FT   DOMAIN          355..483
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          642..1016
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          132..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1017 AA;  113936 MW;  7FEC1DFAFBEC0A5B CRC64;
     MAANARYSLP PGYNNHAANG AGGKPALPHI DDVVALPTDV DIKKPLKSLL EQAEMSLRQS
     EMSRDFNRPA LALKDFIRAS VITVQLVYHH KDYLLLKEGR GDLAMRHNSL MTRIKQQSDT
     YDQIKKDIIA DNKRTGVLPR SQKSGQLQLN GNHSSATPTP ATTTSNGHAV TASGKVKPKV
     QPKPQSLQGN AVPGHGRTSS SNNANFDLAA RFANLRGPQT TPGQDPRIKT HPILPLKPAG
     PRDMPPSPQR SEPSAVNEVP SLPKMPDAIY HPARGSVSSD AGRPPATTPR GSFSRATPTS
     SLNNMPSPVS ARQSMEYFPP VPSNTTGSKL SPQKPAANDE TDTIAAEELF QAMKQSGSVL
     IIDVRSRAEF DEGHIMSSST ICVEASILLR DNISAAEITE SLVLSPNQEQ SQFNRRNEYE
     LVVFYDQDSE EIPRSPRSSD DMVIVSLHRA LVHLNYGRDL KRPPRILKGG LDAWVDLMGS
     ASLQTTSLNS SSHVPTSRAR SGTFQRRRSK YIRPLRADEV KVWQQTLENE DISANQPPEY
     HRSTESFLRR FPPVLTEQES MTSSPATEPP PRYSSLNSID PYTDLPSPPT RPAPSVPRLS
     YGSLSHTSDE ADRFEEPVAP RQSVRVKKVP EQMTGDGYRL YTGLNNPHNW CYANSTLQSL
     LASPDFGKEL SDSTWSTEYR APKKDTEKIE HAQLMIRIVS NLFHWMSTGN LEVMKAQTLM
     DYSQHICKKS RSNAQFGGTQ QQDAQEFMSF LMEHLHDETN SRRNRKGNAM QPNTKSQPLL
     YAAVQYWYNH LQYNESIVDK YWRGLELSTV KCLDCHTKTY TFSPFEWIPA PVALGSTRQT
     LEQSLHQHIA NNTLDDFSCD KCRRNTRAMQ SISFARLPPL LCVCFRRFNY NQATGDIKKS
     TAPVTWDFND FDFSPYFFEN GNGRPPPGTG DQHAYEGPFR YECYAVIVHA GSRTDNGHYF
     AYVRDQSTHD PYAWLCCNDS RVTRVRIGSG DRDDIQNEVF KSGQDRVPYL VFFRRKG
//
DBGET integrated database retrieval system