PFF1_ASPFN
ID PFF1_ASPFN Reviewed; 878 AA.
AC B8NSP6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=AFLA_049970;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(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; EQ963483; EED46944.1; -; Genomic_DNA.
DR RefSeq; XP_002383124.1; XM_002383083.1.
DR AlphaFoldDB; B8NSP6; -.
DR SMR; B8NSP6; -.
DR STRING; 5059.CADAFLAP00010989; -.
DR EnsemblFungi; EED46944; EED46944; AFLA_049970.
DR VEuPathDB; FungiDB:AFLA_049970; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000001875; 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..878
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411700"
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..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..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 443..463
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..473
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 474..494
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 509..529
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..533
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 534..554
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 660..680
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..693
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 694..714
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..721
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 722..742
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..878
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 577..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 174
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 186
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 186
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 221
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 246
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 319
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 318
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"
SQ SEQUENCE 878 AA; 96655 MW; 280FC7D166990149 CRC64;
MASLRLPRAN PLAFTRWPVT VITAIVYLAL LIPLLVVHHV VPSAPSSPPS GLNISEAWAD
LQVLTNGFHP YNSRRNDVIH SWLLRRINEI LDSTPLEQEY RALDEEKPDV FVFDDVYSNL
TTYGGTLKDA DLGVYFEGTN VIVYIRGWED DTEHWWEAPN GVPTSRGGVL VNSHYDSVST
GFGATDDGVG VVTCLQLVKY FTTPGHAPRR GLVVLFNNGE EDFLNGARVY SQHPISKLPH
TFLNLEGAGA GGRATLFRSS DFEVTGPYMR SPHPFGSVLS ANGFDTGLIA SQTDYVIFQG
NMGLRGLDVA FMEPRARYHT NQDDTRHTSK DSVWHMLSAA VATTEGLVSD STDRFDGAPN
TDGGVPSGSG SQAVWFDLFG STFVLFQLHT LFALLVTLLI VGPLTLLFTS IALTKADKMY
LFRSSAKSED RLDVVPLQGL RGFFRFPFLF GIPTVVTVGL AYLVTKVNPY IIHSSAYAVW
SMMVAAWVFL AWFVSRVADF ARPSAFHRIY TLTWMYVLSW VSAVIATVYA NQRGLAGGYF
IFFFHAGIFL ATWISYLELF ALPSKTEYAN QLRSVSGRAS GHGSRRGTTS GEDDGEEAEE
EPTESTSLLG SGQRTTFANY VRVGGDNHAV AEEEVIDPNV YGREQAWSYA LPKWTWGLQL
LLTAPITLIM VGPLALLTIS AISQTGQDGG HPLFAYVAIA IFTTIMLTPL LPFIHRYTYH
VPLFLLAVFL GTLIYNLVAF PFSDSNRLKL YYVQEVDLDT GVNSATFAGL SPFVKDVSQE
LPSAAGQTVS CEWHTKRRNL LSCSWEGIAP QPVEGDHPMK DWGALKGNVV CLWSDHNQPG
VLPALDEAIQ FLPVWAAVTK GSDGLVEGRR AFEIGNDD
