PFF1_PHANO
ID PFF1_PHANO Reviewed; 959 AA.
AC Q0URQ5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=SNOG_05559;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445332; EAT86623.1; -; Genomic_DNA.
DR RefSeq; XP_001795964.1; XM_001795912.1.
DR AlphaFoldDB; Q0URQ5; -.
DR SMR; Q0URQ5; -.
DR STRING; 13684.SNOT_05559; -.
DR PRIDE; Q0URQ5; -.
DR EnsemblFungi; SNOT_05559; SNOT_05559; SNOG_05559.
DR GeneID; 5972841; -.
DR KEGG; pno:SNOG_05559; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; Q0URQ5; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001055; 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; IBA:GO_Central.
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..959
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411733"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 14..34
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..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..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 433..453
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..463
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 464..484
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 499..519
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..524
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 525..545
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 646..666
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..688
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 689..709
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 717..737
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 738..959
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 128..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 158
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 170
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 170
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 205
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 230
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 303
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 302
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 102
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 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 785
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"
FT CARBOHYD 864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 959 AA; 106393 MW; 8E035FE59EC66242 CRC64;
MARLNPLSFT PGPVIFFTCA VYIALFAALL TVHLRVPDYP SKTPDGVNLT QAWSDLEKIT
RRFHPYNSHA NDDVRDYLLT RVKSIIASKK LGGDQVELID DNESNATFSS GSTTVYFEGT
NIIVAIRGSE DDEPYHSPQS SPPGERRLDN GGVLVNAHYD SVSSGYGATD DGVGVVTVLQ
LLSYFTESKN WPKRTVILLL NNGEEDFLNG AKAFMRHPIS QIAHTFVNLE GAGAGGRATM
FRSTDTEVTR YYKASSHPFA SVVSGDGFKK RLIRSETDYK VFYEELGLRG LDIAFMEPRA
RYHTVEDSTR ETSLNSVWHM LSAAIATTSG LASDTSEQFS GSEDEHEPYT GKVKTGHGTD
AVWFDLFGKV FVVFQLHTMF ALCVTLLVVA PLFLIGLTFG LSKADKNYLF ARKAYMYSSD
DDHPVHLYGW RGFFRFPIVF SIATAVVVGL AYLMVRLNPL ILYSSPYAVW SMMLSAWFSV
AWFFSRGASA MRPSALQRMY ALIWLFAGSF ALLAFVTVLS NNYQVAGGYF ALFYFAGIFL
ALVLSYLELF FAPTKTAFAR YSAQGDEPVS RPLTGTTTAA RSEEPPIADD DATETTSLLR
GDRRSFARHS GRRDSIDDEN GNRDEEPVQL DLKQPYPGEQ DWSGKLPGWL WLLQLLLVAP
IVVILVGQIA LLLTSALHQT PADGNSSLFV YLAFALLTTL LLAPIGPFIH RFTWHVPTFV
FLVCVATVIY NLVAFPFSRE HRLKVYFVQQ VDLATGNNRV SLTGVDGYVQ RIVADLPSAQ
GEQINCTTPE AANRKELMTC TWPGLPAQVV TRASRFSNKT DTDGWLDFSI TTSNKTNEAT
ISVAGQNTRA CRIVVDSHHS GVTNVTVAGA VSDPRFKAVG ETGSREIRLW HREWSHPWNV
SVTWPRENSK PSGRIICLWS DANAGDIPAF DEVQHYLPVW AIPSKISDGL VEGFKYFQV
