(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMQ2_DEBHA

ID   Q6BMQ2_DEBHA            Unreviewed;       697 AA.
AC   Q6BMQ2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   11-DEC-2019, entry version 84.
DE   SubName: Full=DEHA2F03520p {ECO:0000313|EMBL:CAG88832.2};
GN   OrderedLocusNames=DEHA2F03520g {ECO:0000313|EMBL:CAG88832.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 /
OS   IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88832.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88832.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|SAAS:SAAS01045498}.
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; CR382138; CAG88832.2; -; Genomic_DNA.
DR   RefSeq; XP_460519.2; XM_460519.1.
DR   STRING; 4959.XP_460519.2; -.
DR   MEROPS; C19.088; -.
DR   EnsemblFungi; CAG88832; CAG88832; DEHA2F03520g.
DR   GeneID; 2903423; -.
DR   KEGG; dha:DEHA2F03520g; -.
DR   HOGENOM; HOG000248158; -.
DR   InParanoid; Q6BMQ2; -.
DR   KO; K11873; -.
DR   OMA; ELSKRMW; -.
DR   OrthoDB; 561804at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; IEA:GOC.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:EnsemblFungi.
DR   GO; GO:0099114; P:chromatin silencing at subtelomere; IEA:EnsemblFungi.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0016578; P:histone deubiquitination; IEA:EnsemblFungi.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMQ2.
DR   SWISS-2DPAGE; Q6BMQ2.
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN          350..674
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          47..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..76
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..151
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..187
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..216
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..272
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  78185 MW;  E2593E8B15B5C7D8 CRC64;
     MSGQANVLSN SVTPLIDRIL ANPLTFISGK QIESDNFEKP ASYIVLSKSS KKGDSSESSK
     ASTQEKEPKS PEMRKPRSMA EAVAVYTGKK FLTKAEKKAA KKRKVTQPLV DSEEEDVGEV
     IGGDIKMAES DSDSISDSQY ESASEFQSDS NVELPFAEFK SESDVKSSSE SRSDSELKTE
     SESKSDSEST SESPAGGEED DEGNDDDDDD DNKDYSLEDN ESFSESDSGS ASDVEDSSND
     EEDLEALKHD LKQELQHDPR DISSKDPSLS GSDDDDEEKE EENSDKNTTP PTSPEDEPEK
     PPATVNASDD LHVLPLNKFY SINEVSSDRG SNNSTRIYKN WRELSKRKPV GLLNHGVTCY
     MNSAIQSLIH IPAVQHYLTD INSGKHNKTL KPRSVSHVLA ELSKRMWALD DNTSKAKQPK
     YVNPKRIIQR LDDINCMMSE WQQEDSHEYF MSLMSRLQED STPKGVKLNQ SIIYDIFGGL
     LHQSVTCKNC NYVSDTKQEF YDLSLGLNRK KNKDVTENSG PQRYTIEKSI QEFFSSELIK
     LDRKDKSSGY DCENCKQKSN ACKISTIDRS PETLTVHLKR FKFNGNSSSK VKQSISYPNY
     LDLTKFTTLK TPTKYQLVSV IVHEGRSISS GHYIAHCLQP DGTWSTYDDE YINKINEKEA
     LSDPSAYVLV YTKLTPRLMK RSNEGNDNLV NAKKLKR
//

If you have problems or comments...

PBIL Back to PBIL home page