PFF1_LEPMJ
ID PFF1_LEPMJ Reviewed; 802 AA.
AC E4ZQC4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
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=Lema_P032730;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929116; CBX93599.1; -; Genomic_DNA.
DR RefSeq; XP_003837039.1; XM_003836991.1.
DR AlphaFoldDB; E4ZQC4; -.
DR SMR; E4ZQC4; -.
DR STRING; 985895.E4ZQC4; -.
DR EnsemblFungi; CBX93599; CBX93599; LEMA_P032730.1.
DR GeneID; 13284452; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; E4ZQC4; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002668; Genome.
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..802
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411720"
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..357
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 358..378
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 390..409
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TOPO_DOM 410..423
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 424..444
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 458..478
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..490
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 491..511
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 610..630
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..649
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 650..670
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 678..698
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 699..802
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 528..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
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 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 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 802 AA; 89157 MW; F1FCC250243917B4 CRC64;
MARYNPLAFT SGPVVFFITI TYTALLIALL LTHLTLPSYP SHPPLGINLT QAWSDLEHIT
REFHPYNSHA NDNVRAYLLS RIEHMMASKK LGSDQVQIID DNISNATFSS GNTTVYFEGT
NLIVAVRGSH DDQAFNDRNR RPDNGGVLVN AHYDSVSSGY GATDDGVGVV SVLQLLSFFT
EPKNWPKRTV VLLLNNGEED FLNGAKAFMR HDISQVPHTF VNLEGAGAGG RAAMFRSTDT
HVTRFYRKSE HPFGTVVSGD GFKKGLVRSE TDYKVFFEEL GLAGLDIAFI EPRAKYHTIE
DSTRETSLNS VWHMLSAAIA TTSGLAADTS TPDRESHDDA VWFDIFGKVF IVFQLHTFFA
LCVTLLVVAP LTLIGLAWSL HKADRNYLFA RKAFVYSADD DEPIHLYGWR GFFRFPIAFG
IATSIVVGLA MMLSAWFAVS WFLLHGADAM RPSALQRMYS LLWLFIGSFC LLVFFTILAN
NHQVAAGYPS LFCFATVFLA NVLSFLELFL APPKSAYAWN VHQNADGGSR PLTSSATAAR
SDNRATTDDD ATETTSLLSG NRRSFARHDA GRRDAINEGA NSQEPESRRR LDLGQPHSGE
QEWSGKLPSW IWIVQFSLLA PMIVILVGQI ALLLTSALYQ TPSDGNSPLY IYTSIAALAV
FLVAPIGPFI HRFTHHVPTF LFLLCVATTI YNLVAFPFSE QHKLKVYFVQ RVDCDTGVNT
VSLTGLDGYV QRIAGNMPSA QQSSLNCSTP DIVTRKELRM CEWEGLHPNV VSPTSQYSNK
TRATDWIDYE IFHDDSNNRG RR
