PFF1_PYRTT
ID PFF1_PYRTT Reviewed; 957 AA.
AC E3RFJ1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 36.
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=PTT_06479;
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1;
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL532751; EFQ95514.1; -; Genomic_DNA.
DR RefSeq; XP_003296396.1; XM_003296348.1.
DR AlphaFoldDB; E3RFJ1; -.
DR SMR; E3RFJ1; -.
DR STRING; 861557.E3RFJ1; -.
DR EnsemblFungi; EFQ95514; EFQ95514; PTT_06479.
DR KEGG; pte:PTT_06479; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001067; 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_0000411739"
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, ECO:0000305"
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 559..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..627
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 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; 105701 MW; C90AA22DD58894FD CRC64;
MARYNPFSFT PGPVVFFTTV IYVGLFAALL VTHLTVPDYP SDPPAGINLT EAWADLEHIT
RRFHPYNSHA NDHVREYLLS RIQGIVATKH LDGSQVEIID DLTSNATFSS GATSVYFEGT
NIIVAIRGSE DDEPFNSTDR RPNNGGVLVN AHYDSVSSGY GATDDGVGVV TVLQLLSYFT
ESHNWPKRTI ILLLNNGEED FLNGAKAFMR NPISRVPHTF VNLEGAGAGG RATLFRSTDT
EVTRFYSKSK YPFGTVVSGD GFKKGLIRSE TDYRVFHSDL GLRGLDIAFM EPRARYHTVE
DSTRETSMNS LWHMLSAALA STSGLAAVTG EEFSGSESLD NGRVNAGRGS DGVWFDLFGR
VFVVFQLHTL FALCVTLLVV APITLIGLTF GLSKADKNYL LARKAFVYSS DDDNPVQLYG
WRGFFRFPII FISATAVVVA LAYLLVRFNA FIIYSSPFAV WSMMLSAWFF VAWFFSRGAD
AMRPSALQRM YALIWLFIGS FVLLTIVTVF VNNYQVVAGY PALFYFAVVF VAIMLSYLEL
FFAPTKSAYA RHFEHDANSR RNSDSASRPL TGSTTAARSD DRPVADDDAT EITSLLRGDR
RGFTRYGSRR DSASEGGEDQ AQGSQRLDLG NVYPGEQEWS GKLPSWIWII QLLLLAPLVI
VLVGQVALLL TSALYQTPSD GNSPLFIYLA IAALSVLLLA PTGPFIHRFT YHVPTFLFLV
CLGTVIYNLV AFPFSRDHRL KVYFVQRVNC ETGANTVSLT GLDSYVQRIV GELPSAQDQP
LNCTTPDVAT RKELKTCEWE GLPAKVVPNA AGAAPFGNET NTGRWLEYSI HKGNRSNKAT
MLVVGLNTRA CRIVFDSPIS GLAVTGAVSD PRFKPVGAAG SREVRLWHRE FGQPWNVGLT
WDAEEHAKLS GRVVCLWSDA NTGSIPAFDE VQHYLPVWAI PSKISDGLVE GFKRFEI
