PFF1_AJEDR
ID PFF1_AJEDR Reviewed; 986 AA.
AC C5G8H4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=BDCG_00606;
OS Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER-3 / ATCC MYA-2586;
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; EQ999973; EEQ83801.1; -; Genomic_DNA.
DR AlphaFoldDB; C5G8H4; -.
DR SMR; C5G8H4; -.
DR STRING; 559297.C5G8H4; -.
DR EnsemblFungi; EEQ83801; EEQ83801; BDCG_00606.
DR VEuPathDB; FungiDB:BDCG_00606; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000002039; 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..986
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411692"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..392
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 393..413
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 448..468
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..477
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 478..498
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 510..530
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..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..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 666..686
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 687..702
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 703..723
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 730..750
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 751..986
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 595..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 175
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 187
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 187
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 222
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 247
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 320
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 319
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 986 AA; 108896 MW; 0C230EDCB3F5CF22 CRC64;
MATPRAQKFN PIAFTPGPVT LITTIVYLAL LIPILVISLV VPPAPETSPE GVNLTEAWRD
LQHLTGGFHP YNSRRNDDVH QWLLRRIDSI LRPTVEAGER PSANNDIPDV FVFDDNQSNL
TYSNGGVGKA AIVGVYFEGT NIIVYIRGTE DDPENWWERS NGKPKGKGGV LVNAHYDSVS
TGYGATDNGM GVVSLLQLLK YFTTPGNKPR KGLVLLFNNG EEDYLNGAHV FSQHPLSNFT
HTFLNLEGAG AGGRAALFRT TDTEVTRFYQ NAKHPFGSVL AADGFKMGLL RSQTDYVVFN
GILGLRGLDL AFIAPRSRYH TDQDDARHTS VDSLWHMLSA AIGTTEGLVS YTGTDFDGKS
QGLDKVNSGT GTLGVWFDMF GSAFAVFRLH TLFALSVTLL IVAPLVIFIT AIVLSKTDRM
YLFSMSKSLG GTDERVSLRG LRGLFRTPII LAVATVIPIG LAYLLEKVNP YIVHSSQFSV
WSMMISVWIF LAWFLACAAD FFRPSALHRA YSYTWIFIAT WVMLVINTVY ANQKGIAAGY
FVFFYFSGSF LATWVSYLEL FALPRKGDFA RQAIMHSGRP PSSLRSRLLT PSADELPSDT
GPHAEYPGDA DETDPTESTS LLRGQRTTFA NYRTGGTDGV VEGTDEGPSF KHEQSWSWTL
PRWTWVLQLL LLAPIVLILV GQLALFLTTS MSQVGSDGVS TFIVYLACAV FTTLLFAPLF
PFIHRFTYHI PTFLFLVFVG TLIYNLVAFP FSPANRLKMF FIQEVNLDDG SNTVSLSGIQ
PYLTDAINSI PSAAGQNITC DQSAFGKLEK CSWAGLPPRV LGQDHDRDTG IVSSDWMSYN
ITKTVGENKA RIEISGRNTR ACKLKFDKPV ADFQVSGSAV DHRMPHTSGQ GVAEIRLWSR
TWDRTWVVDI CWHDSHDKPE DDDGDDEKQD APRNGLSGKV ICLWSDSNQS DVIPALDELR
LYTPNWVAIS KSADGLVEAS HGITIQ
