PFF1_PICGU
ID PFF1_PICGU Reviewed; 970 AA.
AC A5DDN8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 50.
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 ORFNames=PGUG_01389;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
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; CH408156; EDK37291.2; -; Genomic_DNA.
DR RefSeq; XP_001485718.1; XM_001485668.1.
DR AlphaFoldDB; A5DDN8; -.
DR SMR; A5DDN8; -.
DR STRING; 4929.XP_001485718.1; -.
DR EnsemblFungi; EDK37291; EDK37291; PGUG_01389.
DR GeneID; 5128270; -.
DR KEGG; pgu:PGUG_01389; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; A5DDN8; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..970
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411734"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 57..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..397
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 398..418
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 424..444
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..465
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 466..486
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 503..523
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..535
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 536..556
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 621..641
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..658
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 659..679
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 680..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 684..704
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 705..970
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 332
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 970 AA; 108907 MW; EF80CC9E7B3B8AA3 CRC64;
MTTADSNSSA TRGSHEMADG SNRVPNDEPY HRKSPESCEN ANFFVRAMRA SFGYRKTSLT
ILVFLSVIAT VLLSYYDSSL EFSVSLPTDK SESKILDHSW DVLQEIARDE HTYASEANDR
VHDYLEDIIG FLVDKKSYME YDNDLNNTHS FLRQTAPSTV TYYESNNLIV RINGSDPELP
ALLLSAHYDS VPSSFGVTDD GMGIASLIGI LNYFSAKQTS QPARTIIINF NNNEEFGLYG
ALAFLSHPWF KQIKYFLNLE GTGAGGKAIL FRGTDYGFAK YFKNVRFPYA SSLFQQAFSA
RLVHSETDYK YYAELGHLRG LDLAFFRPRD MYHTAKDNIA NVNKKSLWHM LSSTIDFTNG
VVGGEIDLDV EAKQKEAAAF TSIFNYFFVV PMTFVFGVNV LLMVLVPLVS LISLALIFAH
RKWSVSLVTF FKFPLSFILS IFLLDNFSSW FVVSVNNFLP NSSAGIIALT YFSFFVLANY
LLLNGINLLF WKFKGTRHDE KLVVILQISF MFWVSLIWST ANIAKSQFNG EHSGEFLLTL
LYILQAAGGV FGLLCWLFKR SRTVHTNNQE LEPLLEHAVE EGYGAHVEQE GHISSSASSA
ISVNVIESPP PTKHYSYDWS IQFLFIVPIS SFLSYNYGWL ILEGLKKTLQ ESATSEYLVF
RALKLLAVVV AVPYLPFIFK VNRIVFLVTI FLFVYGLGAI VISEPFTEAN PLKLRFLQTI
DLDNSPKSNL VSASGRANSS IAEILRDLPS VKESETEVVC NAKADGMTIC NYEGLNPHLA
PGTKNAQDLL SVKVLSNSSS SINYPFGMLS GKFEIRAEKN RECRLSFRED TGGKRSSGVV
KTVVVYKNDL KNSNKVNAMK APEGFSQDDY GNFVYKNMTG ISDLKLNKLD WNRPYRIGVE
WVASLDDSDT QPTLKVSVDC YWAEIGQIAE KGKIVDRIPA YTELLHYSPN YVTWANLDQG
LVNVKKSVLV
