(data stored in SCRATCH zone)

SWISSPROT: PFF1_ASHGO

ID   PFF1_ASHGO              Reviewed;        1011 AA.
AC   Q750Z6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 81.
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=AGL209W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. {ECO:0000250|UniProtKB:P80561};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P38244};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
DR   EMBL; AE016820; AAS54282.1; -; Genomic_DNA.
DR   RefSeq; NP_986458.1; NM_211520.1.
DR   STRING; 33169.AAS54282; -.
DR   MEROPS; M28.A05; -.
DR   EnsemblFungi; AAS54282; AAS54282; AGOS_AGL209W.
DR   GeneID; 4622751; -.
DR   KEGG; ago:AGOS_AGL209W; -.
DR   HOGENOM; HOG000093779; -.
DR   InParanoid; Q750Z6; -.
DR   OMA; YHTNQDD; -.
DR   Proteomes; UP000000591; Chromosome VII.
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   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   InterPro; IPR007484; Peptidase_M28.
DR   Pfam; PF04389; Peptidase_M28; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750Z6.
DR   SWISS-2DPAGE; Q750Z6.
KW   Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW   Zinc.
FT   CHAIN           1..1011
FT                   /note="Vacuolar membrane protease"
FT                   /id="PRO_0000411697"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        15..35
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..352
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        353..373
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        391..411
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        412..420
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        421..441
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        442..451
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        452..472
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        473..487
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        488..508
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..647
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        648..668
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        669..681
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        682..702
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        703..708
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        709..729
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        730..1011
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   COMPBIAS        536..572
FT                   /note="His-rich"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00009"
FT   METAL           149
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   METAL           161
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   METAL           161
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   METAL           194
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   METAL           219
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   METAL           293
FT                   /note="Zinc 2; catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   SITE            292
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   CARBOHYD        671
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        751
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        825
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        854
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1011 AA;  115899 MW;  5B8AB7987CD73568 CRC64;
     MKLTKAVFRF RRTNLSTLLV ITYLVITTLY VWDHFRYHFT LPSDYNYAQM LADAWLDLEI
     ITQYPHPYAS HANDKVHDYL LDRVKEITRD SMFAEISDDY GMGLRTLFRQ EDAISGTKES
     TVVYYESSNV LARVQGRNSA LDGLLLSAHY DSVPSGYGAT DDGMGVVSML AILTHYVKNQ
     PERTLVFNFN NNQEFGLAGA SAFFEHPWSK EISYVINLEG TGAGGKAVLF RTSDVSTAQV
     YAEAVRQQPF GNSMYQQGFY NGHIGTETDF QVYEDQGLRG WDIAFYRPRN LYHTAKDTVL
     YTSKQALWHM LHTALQLTDY MAINKPDMED TSNAVYFDLF GKWFVVWSAR SLFYWNCIIL
     ALFPSILAIL FLVAYDMQLL KFNFWDAMLR LPVSVCLAYF CVKLFQVLVG QLNPYVFSRD
     YVSPILAEAS MFIFMNYVIL SSWERLRPLR DFKTVALVEV SMVLWIYLIS VTRWLRDSDY
     TATGLYPFTI GYTFVSIGAI IGVFCATFKA KLNPEDDSYV GDSKVDIEQQ QMLMQHQYQQ
     HSQKHSNQHS PHHSTHHSAQ HSVHHSPRQS IHQVPSSEQR QRDASETPHV IISVDHTAGH
     QEDSEVTPLL NTGTVAPFPK PVPERVSRKS FLRNVVTSIL NYDWSIQFMV VTPWVTYFTW
     ICLDLIMGAM NQTIQESAKG TTFVTHMALI GSLLLSLPML PFTYKLHSFA GMLFLLLAVT
     TAVWTIVAPP FTESSPLKLR FLQTIDLDKN NSSSVYLYGR ERTFMEPILD DIPSVTKYRC
     VEYAGDGVDI CEYNGMPPRM FNNHHEAESD WTKIMTLEIL KDDRNSTSRT PYQPITAELK
     INVEENRVCT LNFNSTAFKN WKQGVSPLRE VVILHENPSS NVTPSFYNTA MKNGYYQDEF
     GNDHYRWNNG ITELQLHKLD FKRGYYKIGL EWIPQLLYRG YDPATSSSEE DDALGVSVTC
     YWGEYDTDSI TDGFATTNVP AYDELRKYSP KNIIYSSKEK GMVSVTKYVE L
//

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