PFF1_ASPFC
ID PFF1_ASPFC Reviewed; 965 AA.
AC B0XPG0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=AFUB_006350;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP55933.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XPG0; -.
DR SMR; B0XPG0; -.
DR EnsemblFungi; EDP55933; EDP55933; AFUB_006350.
DR VEuPathDB; FungiDB:AFUB_006350; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR PhylomeDB; B0XPG0; -.
DR Proteomes; UP000001699; 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..965
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411699"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..387
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 388..408
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 442..462
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..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..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 508..528
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..532
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 533..553
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 662..682
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 683..698
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 699..719
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 726..746
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..965
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 577..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 171
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 183
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 183
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 218
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 243
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 316
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 315
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 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 965 AA; 106578 MW; B180E8FBCF5B9E5C CRC64;
MARPSLSPSN PLGFTPWPVT VITAVVYLAL VVPLLVVHHV VPSAPSSSPK GLNLTEAWAD
LQELTHGFHP YNSHRNDEVH EWLLKRILEL IDSAPPASEY GSVGEEKPDI VVFDDTQSNL
TFSGRGSGLG VYFESTNIMV YIRGWEEDRE RWWEDPHGRP AGKGGVLVNA HYDSVSTGYG
ATDDGVGVVS CLQLIKYFTT PGHVPRRGLV LLFNNGEEDF LNGARVYSQH PISQLPHTFL
NLEGAGAGGR ATLFRSSDAE VTKPYMRAPH PFGSVLSANG FEAGLISSQT DYVVFEGDLG
LRGLDVAFME PRARYHTDED DARHTSLASV WHMLSAAVAT TEGLVSDASS RFEGLPREDG
RIASGSGPKG VWFDLFGSAF VVFELHTLFA LSVTLLVVAP LVLLVTSIAL ARADKMYLFR
SSASPEDSDG SEVVPLHGVR GFFRFPFLLV IPTAVTVGLA YLVTKFNPYI IHSSEYAVWS
MMISAWVFLA WFVSRVADFA RPSAFHRVYT LTWLFLVEWV FLVISTVYEN QYGLAGGYFV
LFVFAGTFLA TWISYLELFA LPRKSDYATQ LALPSRRTSS HGSRLGTASG EDVEDGEDED
DDGTTAEATE TTSLLRGQRT TFANYVRVTG DYLRDDDEEP RQPNLYGHEQ AWSIHLPKWV
WVLQFLLTAP LVLIFVGPLA LLLTSALRQT GQDGSPSLFI YIAVAALTTL LFIPLLPFIH
RYTHHIPLFL LCVFAGTLIY NLVAFPFSPA NRLKLFFIQE VDLDTGVNHA SLSGAYPFVH
DVARRLPSTA GQNITCDLAM LRPKCSWHGI PPQVVQPAAA SKMEDWLSYN ITKSDSEPKA
QLSISGRNTR ACKVVFDRPV LDFQVADSAY DPRFPHVSPD GTKEIRLWSR EWGHTWTVDV
EWAADAEETD EKGPGLSGRV VCLWSDGNSA GVIPALDEVR RYAPVWAGVS KLSDGLVEGS
RRFEV
