(data stored in ACNUC6288 zone)

SWISSPROT: PFF1_DEBHA

ID   PFF1_DEBHA              Reviewed;        1016 AA.
AC   Q6BMD6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   10-APR-2019, entry version 65.
DE   RecName: Full=Vacuolar membrane protease {ECO:0000250|UniProtKB:P38244};
DE            EC=3.4.-.- {ECO:0000305};
DE   AltName: Full=FXNA-related family protease 1 {ECO:0000250|UniProtKB:P38244};
GN   OrderedLocusNames=DEHA2F06380g;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
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   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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: May be involved in vacuolar sorting and osmoregulation.
CC       {ECO:0000250|UniProtKB:P38244}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P80561};
CC       Note=Binds 2 Zn(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P80561};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane
CC       {ECO:0000250|UniProtKB:P38244}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
DR   EMBL; CR382138; CAG88967.2; -; Genomic_DNA.
DR   RefSeq; XP_460635.2; XM_460635.1.
DR   STRING; 4959.XP_460635.2; -.
DR   MEROPS; M28.A05; -.
DR   EnsemblFungi; CAG88967; CAG88967; DEHA2F06380g.
DR   GeneID; 2903146; -.
DR   KEGG; dha:DEHA2F06380g; -.
DR   HOGENOM; HOG000093779; -.
DR   InParanoid; Q6BMD6; -.
DR   OMA; YHTNQDD; -.
DR   OrthoDB; 166108at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007484; Peptidase_M28.
DR   Pfam; PF04389; Peptidase_M28; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMD6.
DR   SWISS-2DPAGE; Q6BMD6.
KW   Complete proteome; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix; Vacuole; Zinc.
FT   CHAIN         1   1016       Vacuolar membrane protease.
FT                                /FTId=PRO_0000411716.
FT   TOPO_DOM      1     57       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM     58     78       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM     79    408       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    409    429       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    430    438       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    439    459       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    460    481       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    482    502       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    503    511       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    512    532       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    533    547       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    548    568       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    569    646       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    647    667       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    668    681       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    682    702       Helical; Name=8. {ECO:0000255}.
FT   TOPO_DOM    703    706       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    707    727       Helical; Name=9. {ECO:0000255}.
FT   TOPO_DOM    728   1016       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   COMPBIAS    621    624       Poly-Ser. {ECO:0000255}.
FT   ACT_SITE    238    238       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       191    191       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       203    203       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       203    203       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       239    239       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       264    264       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       337    337       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   SITE        336    336       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   CARBOHYD    147    147       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    177    177       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    473    473       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    669    669       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    778    778       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    821    821       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    850    850       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    875    875       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    977    977       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
SQ   SEQUENCE   1016 AA;  114986 MW;  F51C4B51B3C8CF9E CRC64;
     MAETESGTGN SPSHRLSETS NASGNRSHQQ SKQIASYKSS KPNVFIRFIR AIFGYRKTSV
     TLFVFITIIA TLILVELSNS LDFSVKLPTN NLERTILDNS WLDLQKIGKE EHPYTSKGND
     YVHDYLEAKI TELIGKSLFI ECDNDVNYTN NIIFKTENDL YNQVTYYESN NLLVRINGSD
     SSLPALLVSA HFDSVPSSFG VTDDGMGIAS LLGILNYYSS DGIDQPMRTI ILNFNNNEEF
     GLMGATSFLH HPWFKQVRYF LNLEGTGAGG KAVLFRGTDY GIVKYFKHVR YPFGTSLFQQ
     GFNNHLIHSE TDYKIYKENG GIRGIDLAFY KPRDIYHTAS DSIKNIDIKS LWHMLSNSLD
     FVEIVSSQRI DLDDEDTSPE SDEKSREFAI FSSFFNWFFV IPASQLVLIN VTCLAVIPLI
     SLPLLVIIFN YKKNWHIGFI NAIKFPVSLV LSICILNIIT HNVIASINEF LPNSSYDSIV
     STLYSLFLLL NYLFLNGINF IFKGYKGLYH DEKLILIIQT SFIYWVLLIV STNKLSKNKI
     GNDHTGEFPL IMLFLLQSIG ALFGLFSWSF KKTTPDELRN NDDEACQALL SREEHNNYGS
     NEAELESGEP ISSNSSVSLN SSSSQVTNNL VKNLRKSFSY DWSIQYVVIV PLSSLIVYNT
     GSLLLSGLNK SIQESLNAEK LIFDLIQLVA VTLAIPFLPF IFKINRLLVT ALVLVFCSGF
     ISIFLKSPFD QLNPLKLRFV QSINLDESSD ISVVNVFGRY GSPMNNVLLD LPSLKETNES
     LECNNLQDGM QLCSYKTLLS PNLSPDVTDF NDYLDVQVLK NSSSDYPYGL LSGEIKINVP
     ENRVCRLSFN NSNFENSKQS LVRTILVYED NNYENSSNKL FPFEVSEFQL ANLPEGFSRD
     KKGTYIYKNL NGIDKLELNK LSWDKPYHVG FQWMPKFVDS VSAENENTNV PYTTDFNNLG
     IQVECFWGNL GYANNENKSE DERIPAYGEV LHYSPNYVSW ANKESGLVSV SKYVEI
//

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