(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMD9_DEBHA

ID   Q6BMD9_DEBHA            Unreviewed;       446 AA.
AC   Q6BMD9;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=CAAX prenyl protease {ECO:0000256|RuleBase:RU366005};
DE            EC=3.4.24.84 {ECO:0000256|RuleBase:RU366005};
GN   OrderedLocusNames=DEHA2F06248g {ECO:0000313|EMBL:CAG88960.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88960.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88960.1, 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   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   -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC       farnesylated proteins. {ECO:0000256|RuleBase:RU366005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The peptide bond hydrolyzed can be designated -C-|-A-A-X
CC         in which C is an S-isoprenylated cysteine residue, A is usually
CC         aliphatic and X is the C-terminal residue of the substrate
CC         protein, and may be any of several amino acids.; EC=3.4.24.84;
CC         Evidence={ECO:0000256|RuleBase:RU366005};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU366005};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU366005};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU366005}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU366005}.
CC   -!- SIMILARITY: Belongs to the peptidase M48A family.
CC       {ECO:0000256|RuleBase:RU366005}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|RuleBase:RU366005}.
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DR   EMBL; CR382138; CAG88960.1; -; Genomic_DNA.
DR   RefSeq; XP_460632.1; XM_460632.1.
DR   STRING; 4959.XP_460632.1; -.
DR   MEROPS; M48.001; -.
DR   EnsemblFungi; CAG88960; CAG88960; DEHA2F06248g.
DR   GeneID; 2903137; -.
DR   KEGG; dha:DEHA2F06248g; -.
DR   HOGENOM; HOG000257874; -.
DR   InParanoid; Q6BMD9; -.
DR   KO; K06013; -.
DR   OMA; RFEYQAD; -.
DR   OrthoDB; 878143at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071586; P:CAAX-box protein processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0071432; P:peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion; IEA:EnsemblFungi.
DR   CDD; cd07343; M48A_Zmpste24p_like; 1.
DR   InterPro; IPR027057; CAXX_Prtase_1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   InterPro; IPR032456; Peptidase_M48_N.
DR   PANTHER; PTHR10120; PTHR10120; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   Pfam; PF16491; Peptidase_M48_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMD9.
DR   SWISS-2DPAGE; Q6BMD9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU366005};
KW   Hydrolase {ECO:0000256|RuleBase:RU366005};
KW   Membrane {ECO:0000256|RuleBase:RU366005};
KW   Metal-binding {ECO:0000256|RuleBase:RU366005};
KW   Metalloprotease {ECO:0000256|RuleBase:RU366005};
KW   Protease {ECO:0000256|RuleBase:RU366005};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transmembrane {ECO:0000256|RuleBase:RU366005};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU366005};
KW   Zinc {ECO:0000256|RuleBase:RU366005}.
FT   TRANSMEM     16     36       Helical. {ECO:0000256|RuleBase:RU366005}.
FT   TRANSMEM    126    146       Helical. {ECO:0000256|RuleBase:RU366005}.
FT   TRANSMEM    172    191       Helical. {ECO:0000256|RuleBase:RU366005}.
FT   TRANSMEM    198    221       Helical. {ECO:0000256|RuleBase:RU366005}.
FT   DOMAIN       40    227       Peptidase_M48_N. {ECO:0000259|Pfam:
FT                                PF16491}.
FT   DOMAIN      232    435       Peptidase_M48. {ECO:0000259|Pfam:
FT                                PF01435}.
SQ   SEQUENCE   446 AA;  50606 MW;  8D44723CBF06B6C6 CRC64;
     MFSLANSFSF LDSASINWKS IIVGFTVGQF LFENYLDYRQ YQVLKRTTPP DTLKAEVSQE
     TFDKSQDYSR AKAKFGFLSD SINLFQNLAI IKYDLLPKFW NIAGTLMAKS SFILPKFMGG
     IITQSLFFLF STQIISTIVS LPLSYYSNFV LEEKYGFNKL TVGLWLTDKV KGIALGIALG
     SPVVAAFLKI IDYFGDSFIL YTCGFLFVVQ LVGMTIFPTL IQPLFNKFTT LDEGELKTAI
     ENLACEQKFP LTKLYVIDGS KRSSHSNAYF TGLPWSKQIV LYDTLIKHST KEETVAVLAH
     EIGHWKLSHL PQMLVFSQAH LFLSFSMFSA FIHNNSLYSS FGFTSVQPIM IGFMLFNDIF
     QPVECVAQFG MNLLSRKNEY EADAYAKKCG YSDDLAKALI KLLSENLSTM DADWLYSSYH
     HSHPILSERL RAINYVSKEK VGKKDE
//

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