PFF1_NEOFI
ID PFF1_NEOFI Reviewed; 967 AA.
AC A1D432;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=NFIA_018760;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027688; EAW23175.1; -; Genomic_DNA.
DR RefSeq; XP_001265072.1; XM_001265071.1.
DR AlphaFoldDB; A1D432; -.
DR SMR; A1D432; -.
DR STRING; 36630.CADNFIAP00002120; -.
DR EnsemblFungi; EAW23175; EAW23175; NFIA_018760.
DR GeneID; 4591208; -.
DR KEGG; nfi:NFIA_018760; -.
DR VEuPathDB; FungiDB:NFIA_018760; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000006702; 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..967
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411726"
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..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 664..684
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..700
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 701..721
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 722..727
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 728..748
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..967
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 579..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..608
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 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 967 AA; 106979 MW; 66DFE52D5698AFB8 CRC64;
MARPSLSRSN PLGFTPWPVT VITAVVYLAL VVPLLVVHHV VPSAPSSSPK GLNLTEAWTD
LQVLTNGFHP YNSHRNDEVH EWLLKRILEL INSAPPASEY ESVDEAKPDI VVFDDTQSNL
TFSGRASGLG VYFESTNIMV YIRGWEEDKE RWWEDPHGRP AGKGGVLVNA HYDSVSTGYG
ATDDGVGVVS CLQLIKYFTT PGHVPRRGLV LLFNNGEEDF LNGARVYSQH PISQLPHTFL
NLEGAGAGGR ATLFRSSDAE VTKPYMRAPH PFGSVLSANG FEAGLISSQT DYVVFEGDLG
LRGLDVAFME PRARYHTDED DARHTSLDSV WHMLSAAVAT TEGLVSDASG RFEGLPREDG
RIASGSGPRG VWFDLFGSAF VVFELHTLFA LSVTLLVVAP LVLLVTSIAL NRADKMYLFR
ASASPEDSDG SEAVLLHGVR GFFRFPFLLV IPTAVTVGLA YLVTKFNPYI IHSSEYAVWS
MMISAWVFLA WFVSRVADFA RPSAFHRVYT LTWLFLVEWV LLVISTVYEN KYGLAGGYFV
FFAFAGTFLA TWISYLELFA LPRKSEYATQ LALPSRRASS HGSRLGTASG EDVEDGEDED
EDDDGTTAEA TETTSLLRGQ RTTFANYVRV TGDYLRDDGD EPRQPNLYGH EQAWSIHLPK
WVWVLQFLLT APLVLTFVGP LALLLTSALR QTGQDGSSSL FIYIAVAALT TLLFIPLLPF
IHRYTHHIPL FLLCVFAGTL IYNLVAFPFS PANRLKLFFI QEVDLDTGVN HASLSGAYPF
VHDVASSLPS TAGQNITCDL DLLRPKCSWH GIPPQVVQPA EASKMKDWLS YNITRSDAEP
KAQLSISGRN TRACKLVFDR PVLSFTVADS AYDPRFPHVS PDGTKEIRLW SREWGHTWTV
DVEWAADTEE TDEKGLRLSG RVVCLWSDGN TAGVIPALDE VRRYVPVWVG VSKLSDGLVE
GSRRFEI
