PFF1_PYRTR
ID PFF1_PYRTR Reviewed; 957 AA.
AC B2W0S3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=PTRG_04058;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(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}.
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DR EMBL; DS231617; EDU46896.1; -; Genomic_DNA.
DR RefSeq; XP_001934391.1; XM_001934356.1.
DR AlphaFoldDB; B2W0S3; -.
DR SMR; B2W0S3; -.
DR STRING; 45151.EDU46896; -.
DR PRIDE; B2W0S3; -.
DR EnsemblFungi; EDU46896; EDU46896; PTRG_04058.
DR GeneID; 6342294; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; B2W0S3; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001471; 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..957
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411738"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..369
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 370..390
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..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..450
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 451..471
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 491..511
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..521
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 522..542
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 643..663
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664..685
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 686..706
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 714..734
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..957
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 560..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 152
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 164
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 164
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 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 224
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 297
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 296
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 957 AA; 105674 MW; DA5FC2231E1C32EB CRC64;
MARYNPFSFT PGPVVFFTTV IYVGLFAALL VTHLTVPDYP SDPPAGINLT EAWADLEHIT
RRFHPYNSHA NDHVRGYLLS RIQGVIATKA LDASQVEVID DLTSNATFSS GATSVYFEGT
NIIVVIRGSE DDEPFNSTDR KPNNGGVLVN AHYDSVSSGY GATDDGVGVV TVLQLLSYFT
ESHNWPKRTI ILLLNNGEED FLNGAKAFMR NPISQVPHTF VNLEGAGAGG RATLFRSTDT
EVTRFYSKSK YPFGTVVSGD GFKKGLIRSE TDYRVFHGEL GLRGLDIAFM EPRARYHTVE
DSTRETSMNS LWHMLSAALA STSGLAAVTG EEFSGSESLD NGRVNAGRGS DGVWFDLFGR
VFVVFQLHTL FALCVTLLVV APIALIGLTF GLSKADKNYL LARKAFVYSS DDDNPVQLYG
WRGFFRFPIV FVSATAVVVA LAYLLVRFNA FIIYSSPFAV WSMMLSAWFF VAWFFSRGAD
AMRPSALQRM YALIWLFIGS FVLLTIITVF VNNYQVVAGY PALFYFAVVF AALMLSYLEL
FFAPTKSAYA RHFEHDTSSR RNSESASRPL TGSTTAARSD DRPVADDDAT ETTSLLRGDR
RGFTRYGSRR DSTSEGDEDH AQGSRRLDLG NVYPGEQEWS GKLPSWIWII QLLLLAPLVI
VLVGQVALLL TSALYQTPSD GNSPLFIYLA IAALSVLLLA PTGPFIHRFT YHVPTFLFLV
CLATVIYNLV AFPFSRDHRL KVYFVQRVNC ETGANTVSLT GLDSYVQRIV GELPSAQDQP
LNCTTPDVAT RKELKTCEWE GLPAKVVPNA AGAAPFGNET NTDRWLEYSI HKGNRSNKAT
IRVVGLNTRA CRIVFDSPIT GLAVTGAVSD PRFKPVGAAG SREVRLWHRE FGQPWNVALT
WDAEEHAKLS GRVVCLWSDA NTGSIPAFDE VQHYLPVWAI PSKISDGLVE GFKQFEI
