PFF1_TRIVH
ID PFF1_TRIVH Reviewed; 962 AA.
AC D4D8C1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 35.
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=TRV_03357;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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; ACYE01000173; EFE41897.1; -; Genomic_DNA.
DR RefSeq; XP_003022515.1; XM_003022469.1.
DR AlphaFoldDB; D4D8C1; -.
DR SMR; D4D8C1; -.
DR EnsemblFungi; EFE41897; EFE41897; TRV_03357.
DR GeneID; 9581091; -.
DR KEGG; tve:TRV_03357; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR Proteomes; UP000008383; 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; Transmembrane; Transmembrane helix; Vacuole; Zinc.
FT CHAIN 1..962
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411745"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..390
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 391..411
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 441..461
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..472
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 473..493
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 504..524
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..534
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 535..555
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 668..688
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..704
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 705..725
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 726..731
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 732..752
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 753..962
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 568..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 169
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 181
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 181
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 216
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 241
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 314
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 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 113
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 962 AA; 107068 MW; 76511C61DC75BF38 CRC64;
MVSSRRGFNP IAFTPWPVTI LSSLVYLALI IPIIVVHHLV PPAPKESPAG VDLEEAWHDL
QHLTRQYHPY NSHSNDEVHQ WLLKRIHAIS ATSARSESQS GPEVFVFDDN QTNLTFSSAG
VAATAITGVY FESRNIVVYI RGTEDEPGEW WKSPDGEPSG KGGVLVNAHY DSVSTGYGAT
DNGVGVITTL QLLKYFTTPG HYPRKGLVLL FNNGEEDFLN GAYAYSQHPM SKFTHTFLNL
EGAGAGGRAV LFRSTDTEVT RFYGKSEHPF GTVLARDAFK LKFIRSETDY HVFDGVFGMR
GLDVAFMEPR SRYHTDQDDA RHTSIDSVWH MLSAAITTTE GLVSYTGDAF DGDSGDGGKL
NNGIGTLGVW FDFFGSSFAV FQLNTLFGHS VALLVVAPLL LIITSVALFA VDKMYMFSMY
TYISESGGQV SLYGLRGMFR FPLILGISTA LTIALAFLIM KVNPFIIYSS PYAVWSMMLS
TCMFFAWFIS CVADFARPSA LHRAYAFSWM FGIMWVFLVI ATVYQKQHGI ASSYFIVFYF
AGVAVATWIS YLELFGLPKT QDYARRQGRL SDRTPSSDSH FLAPSADELP SSSSAAGRDF
NPEDVEDEEP TESTSLLRGQ QRTTFANYAS ARGSQESNIS NQGNNSLHPK DHRLEQKWSI
YLMSSAWILQ FLLVAPIVII LLGQLGLFLT SATYQIGADG GSQLVIYIGI AVLSVLILLP
LFPFIHRFTY HIPTFLLFIL IGTLVYNLTA FPFSHSNRLK LAFVQEMDLA TGNNQASLVG
VEPYIHDAVH AIPSVQDGKI SCTSHGYGGR TKCSWPGLKP KVAEGPYKDW VSYNISQTKD
DKITRFEVSG KNTRACKLLF DSPIADFHVQ GSVVDKRIPH TGPKGVSEIR LWSRNWENTW
TVDVEWTKKN SERTGKVMCL WSDDNDLHVI PELDLARKFA PWWVAITKLR DGLVEGSYSF
EL
