PFF1_PARBD
ID PFF1_PARBD Reviewed; 992 AA.
AC C1G0X0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
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=PADG_00510;
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(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; KN275957; EEH44221.1; -; Genomic_DNA.
DR RefSeq; XP_010756377.1; XM_010758075.1.
DR AlphaFoldDB; C1G0X0; -.
DR SMR; C1G0X0; -.
DR STRING; 121759.XP_010756377.1; -.
DR EnsemblFungi; EEH44221; EEH44221; PADG_00510.
DR GeneID; 22580340; -.
DR KEGG; pbn:PADG_00510; -.
DR VEuPathDB; FungiDB:PADG_00510; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000001628; 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..992
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411729"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..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..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 447..467
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..474
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 475..495
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..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..671
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 672..692
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 693..708
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 709..729
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..736
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 737..757
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..992
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 579..620
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 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 992 AA; 110052 MW; 219336D7507B66E7 CRC64;
MSPAMANPRV RKFNPIAFTP LPVTFITTIV YLAVLILVLV TYLVVPPAPT LEMSPKGVNL
TEAWRDLQHL TEGFHPYNSR RNDDVHAWLL HRIEAIVRES AAADGGPEVF VFDDNLSNLT
YSNGGVSKSP IVGVYFESTN IIVYIRGSED DPQNWWEWSN GKPKGKGGVL VNAHYDSVST
GYGATDDGMG VVSLLQLLRY FTTAGNKPRK GLVLLFNNGE EDYLNGARVY SQHAMSNFTH
TFLNLEGAGA GGRACLFRST DTEVTRFYKN AKHPFGSVLA GDGFKLGLIR SQTDYVVFNG
VLGLRGLDVS FIAPRSRYHT DQDDARHTNV DSLWHMLSVA IGTTEGLVSY TGTDFDSKTT
DQDKVNSGGG TLGVWFDIFG SAFAVFRLHT LFALSVTLLV IGPLVLFITS IALSKTDRMY
LFSMSKSLGG ASETVSLRGL RGLFRTPIIL TVTTVISIGL AYLLEKINPY IVHSSQFAVW
SMMLSVWIFV AWFLARVADF FRPSALHRAY SYTWIFIVTW IMLVISTVYA NQKGIAAGYF
TFFYFAAVFL ATWVSYLELF SLPRKGYYAR QASRRQRRRS SSLSSRLLTP SADELPSDIG
PNGAENVGDP DETDPTESTS LLRGQRTTFA NYRTGGDDGV TEYTAEDEHV REASIFGHEQ
SWSWTLPRWT WILQLLLLAP IVIILVGQVG LLLTTAMSQI GSDGVSTFIV YLACALFSTL
LFAPLLPFIH RFTYHVPIFL LLIFIGTLIY NLVAFPFSPA NRLKIFFIQE VNLDDGTNKV
SLTGIQPYLT DTINAIPSAA GQTANCTQGP FGSLVRCSWS GLPPRVVKED PGNDQTMGPY
TWISYNITRT VGKNEARIKV SGRNTRACKL KFDNPVADYR ISGSAVDHRL PHTSRQGVEE
IRLWTRTWEN TWVVDVDWHS NPVNPGESKD GDEKQDVSKN ELSGKVICLW SDNNESGVIP
ALDEVRLYAP AWVAISKSAD GLVEASHDFI IQ
