PFF1_MAGO7
ID PFF1_MAGO7 Reviewed; 1011 AA.
AC A4R254; G4MLM1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 68.
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=MGG_06752;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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}.
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DR EMBL; CM001231; EHA56854.1; -; Genomic_DNA.
DR RefSeq; XP_003709466.1; XM_003709418.1.
DR AlphaFoldDB; A4R254; -.
DR SMR; A4R254; -.
DR STRING; 318829.MGG_06752T0; -.
DR GeneID; 2684925; -.
DR KEGG; mgr:MGG_06752; -.
DR VEuPathDB; FungiDB:MGG_06752; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; A4R254; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
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..1011
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411722"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..378
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 379..399
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 440..460
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..471
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 472..492
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 506..526
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..536
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 537..557
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 683..703
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..719
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 720..740
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 748..768
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..1011
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 595..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 159
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 171
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 171
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 206
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 231
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 304
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 303
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 872
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1011 AA; 111327 MW; C32CFF0BCA2A1790 CRC64;
MSNPFAFRSA QVTFWTTVVY LALLVPLVVI NEGVPPVQPD GSLFLDRGLN LTEAWLDLGH
ITERFHHQNS RENDVVRDYL RLRIEQIIAA NDAEARTTVF NDLTSNVTYL AWGSAVPTHY
QGNNLYVYIR GKDDDQGEWW HNARAGKLIG KGGVLVNAHF DSVSTAYGAT DDGMGTVTVL
QMIRYFTKPG NQPQRGIVAL LNNAEEPGLL GAAAFGKSPL LPFIHTFLNL EGAGAGSRCV
LFRSTDREVT SAFSNVQSPF GSVVGSDGFK MGLVRSGTDY SVWHDIYGQR GLDLAFYRPR
ALYHTNQDDT KHTSRESLWQ MMAASTTTLI NLSADTGSDY IGDRPDGDRS KAPNGSPSDG
VWFDLFGSTF VLFGLRGMFA WSLTVLIVGP LTLFGMMYLV HKQGKGYAFH TKLRATSDSS
SEDGDDEDGE VIRLGGWKGF FRFPFALIVA GALVTGAALL LRKMNPFIIY SSEYAVWAMM
ISLFYFGFWL IMRGSSYTRP SALHRLYVHI WLFILGWVAL VFATVLEDRM RIASGYIFVF
WESQVFLATL VAVCELFSLP RKIDFARGAA EEAEVRDHLE AVPHSDAVIA PSLEEATSPQ
RAGQSSNSPQ EDDEDDVPDE ETPLFRKAGR GNKLDTSFLR RGYRRSVSAI MDSNNEAEDG
PKRKQPFEGE QAWSGPMVTS TWILQFLLLG PFMVILGGQV GLLLTSAVNQ TGVDGSSLLA
PYLMIAALSA ILLMPLSPFI HRVTKHVPLF LLAVAFATLI YSLVAFPFSP RAPYKTFFRQ
TVDLDTGDTQ VHLAGVEQYL RKIIADVPSA LGQEIACDAS SSRRDLVDCT YDAAQVPPIP
TYGSGKKSFD LPPGVSPGPA YYGKLLTVTV VNTTAKIATQ GSKTARLKID AVDTRVVELR
FSKEGPPIRS FRVVGADSWD DRFGAFPDDG ARVLRLWRRD WESSFVVDIT WKVDGGNTRG
LEGRAVALWS DANDAVNTMP AFREVVRYAP AWATVSKAAP GLVEGSKAFK V
