PFF1_FUSV7
ID PFF1_FUSV7 Reviewed; 1032 AA.
AC C7Z274;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
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=NECHADRAFT_96958;
OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS 45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex; Fusarium vanettenii.
OX NCBI_TaxID=660122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA VanEtten H.D.;
RT "The genome of Nectria haematococca: contribution of supernumerary
RT chromosomes to gene expansion.";
RL PLoS Genet. 5:E1000618-E1000618(2009).
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; GG698906; EEU42122.1; -; Genomic_DNA.
DR RefSeq; XP_003047835.1; XM_003047789.1.
DR AlphaFoldDB; C7Z274; -.
DR SMR; C7Z274; -.
DR STRING; 140110.NechaP96958; -.
DR EnsemblFungi; NechaT96958; NechaP96958; NechaG96958.
DR GeneID; 9671620; -.
DR KEGG; nhe:NECHADRAFT_96958; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; C7Z274; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000005206; 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..1032
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411725"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..426
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 427..447
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 483..503
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..511
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 512..532
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 546..566
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..573
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 574..594
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 709..729
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..745
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 746..766
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 774..794
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..1032
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 616..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 207
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 219
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 219
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 254
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 279
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 352
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 351
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 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1032 AA; 115781 MW; 1AD96ED492831F6C CRC64;
MRFQNPFAFR PGPVSFWTTV IYLALVIPLI YVHETVPPAP SDRSLYQGLN LTEAWLDLQT
ISRAFHPYNS HENDVVRQFL IDRTKEILDR NSMPYTTETI GGVDWHTRNA FVQTQDSDLN
PRDEFIQSRP RGATLFDDKI SNVTWTYNTA RPTGTNIAKG TWMGQYFEGN NYYVYIHGKD
DPEGEWWRSE SAYKKFRGQG GVLVNCHFDS VSTGYGATDD GMSCVSMLQL LSYFTLQGRQ
PKNGIVLLFN NAEEDGLLGA RAFGYSPLLH FTHTFVNLEG AGAGGRAILF RTTDLQAAKV
YAKSPHPFGS VVAANAFERG VIKSATDYEI FADIFGQRGM DIAFYAPRAR YHTNQDDTRH
TSVNSIWHML SAALASTERF SQITGTTFHG DRSDGKSDLV QNGKKAEGVW FDIFGSAWAV
FALRGLFAWS LTLLVATPLI LVAITYILAR KDKYYFFSRD IKMHHDINDD PVVLGGWKGF
LRFPFALVFA GALTIASTLL LAKFNPLIIY SSPYAVWSMT LSIFYFSFWL IMRGASFIRP
SALHRGYVLI WLFALGWGLQ VVGAVAEDRL HIAALYATVF LQSAVFLALF ISLLEQFALL
GKHDFAMQLH DAHQARDISS HGTDHESRPQ PEEEPAQPEG DEDESEDATE TTPLRANEPG
YGSSTRTSFA ATYRRSVADN APSPPRMRRY QPYEHEQSWS GRLPSWTWII QFLLLAPVPV
ILFGNLGLVA MSALQMTGTD GGSLLVPVLT LGIVSIFLLL PLTPFIHRVS HHVPMFLLCV
FAGTFIYNLV AFPFSDSHRF KFYFQQVVDL DNGTDTVSIV GLERFSRSVI KSLPSASSQD
IKCEKAVGRD LMECLYDSSS LSPHLVEGKT PRELITFETV DGTNASKGRL RIDALDSRLC
YLHTSRPIYG FAVDGGAARD PRFGGFPSEG FKTIQLWRRD RDRPWTVNLY LDEHSQQADK
SFEGEHKKLG DGSVVHRRAD DPLEVTVRCA WSDANKPGTI PALDELLKYM PTWAAVTKKN
VGLVEVRKTY KV
