(data stored in ACNUC8465 zone)

SWISSPROT: PFF1_CANGA

ID   PFF1_CANGA              Reviewed;         947 AA.
AC   Q6FK15;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 66.
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=CAGL0M01936g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62405.1; -; Genomic_DNA.
DR   RefSeq; XP_449429.1; XM_449429.1.
DR   ProteinModelPortal; Q6FK15; -.
DR   STRING; 284593.XP_449429.1; -.
DR   MEROPS; M28.A05; -.
DR   EnsemblFungi; CAG62405; CAG62405; CAGL0M01936g.
DR   KEGG; cgr:CAGL0M01936g; -.
DR   CGD; CAL0136615; CAGL0M01936g.
DR   EuPathDB; FungiDB:CAGL0M01936g; -.
DR   eggNOG; KOG2194; Eukaryota.
DR   eggNOG; COG2234; LUCA.
DR   HOGENOM; HOG000093779; -.
DR   InParanoid; Q6FK15; -.
DR   OMA; FAWSLTL; -.
DR   OrthoDB; EOG092C22R5; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Q6FK15.
DR   SWISS-2DPAGE; Q6FK15.
KW   Complete proteome; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix; Vacuole; Zinc.
FT   CHAIN         1    947       Vacuolar membrane protease.
FT                                /FTId=PRO_0000411708.
FT   TOPO_DOM      1     15       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM     16     36       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM     37    358       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    359    379       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    380    391       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    392    412       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    413    428       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    429    449       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    450    458       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    459    479       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    480    489       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    490    510       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    511    601       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    602    622       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    623    641       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    642    662       Helical; Name=8. {ECO:0000255}.
FT   TOPO_DOM    663    669       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    670    690       Helical; Name=9. {ECO:0000255}.
FT   TOPO_DOM    691    947       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   COMPBIAS    831    836       Poly-Asn. {ECO:0000255}.
FT   ACT_SITE    200    200       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       156    156       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       168    168       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       168    168       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       201    201       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       226    226       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       300    300       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   SITE        299    299       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   CARBOHYD     46     46       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD     92     92       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    108    108       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    121    121       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    319    319       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    742    742       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    784    784       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    801    801       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    833    833       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
SQ   SEQUENCE   947 AA;  107339 MW;  40D31ECDB228E936 CRC64;
     MRFKALLRAI FRFRKTNFSI LLIITYAIII ALLVFDRSRY KLDLPNATSD KLRRNLLEQA
     WSDLQVITQS PHPYSSRNND VVHDFLLQRV KNITRSNDNI YIDDDYRNKS SILFHQPDVF
     NSTSKVSRVV YYESSNIIVK VVGSNNELPA LLISGHFDSV PTSYGATDDG KGIATMLSLL
     NHFSSSQPKR SVIFNFNNNE EFGLLGAYAF TYHPWIRDIE YFINLEGMGA GDRAVLFRTS
     NVETAEIYKK AVKSRPFGNS IFQQGFNSRY IGSQTDYKVY DEYGLKGWDI SFYKPRDYYH
     TAKDSIQYTS KESLWSMLNQ SLQLAIYISN EKLIKKSSSN PAVFFDLLGL FFVVVDTKHL
     FYADIFMLIV GPILLMMKAH LDKRRRLERS RLVQLRLLLS LGLSVVFLLL LTKSLNSFNP
     FVYSADYRTP LTGLFLLFVT VNYLIVTLAE RLNPTESYKT VAINQIFIIA WLMQLYITLR
     MAKSDFTLTG TYPLSIFSGC LIVALSLGLF GTKNKAVNDA PNSSVRYASS QNDEDNPLPS
     QDRGENINQV RDTGNQEVTS NTNTDLHSNA EEVDERMPLL SNNHIGDSGK MDKNSDFSKH
     YNWIVQFLCI VPISSFIFLF SLDYTLDAIH KMVQETTDDV QLICIIITIG VILLALPILP
     FISKLNYQSS VIIAIIGVLL FGKSLVMQPF SEIAPLKVRF LQTVNQHDIS KSSVSLFTAK
     DTPIKEMIYD LPSVKSQSTL VNCTVFGGSK ICDYYGLPPN LVDSEGNRQN KNLMKIEVLK
     NDNNDTQRSP YAPLSAEIKI NVSENRVCSL AFWSQSSKQS PVKKFSVIKS NNNNTNSVSN
     SIKYADGIDE VLIHKLDFNG AHHFSIEWLP NIPFDLDYDP VIDGQGDNNI EITVACFTGE
     ADSLSVVNGH PLKKIPAFDE VVKYSPKWYT FTNRDRGLVV IKDKIQL
//

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