PFF1_PARBA
ID PFF1_PARBA Reviewed; 993 AA.
AC C1GTI3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=PAAG_01828;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
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; KN293995; EEH39639.1; -; Genomic_DNA.
DR RefSeq; XP_002795940.1; XM_002795894.1.
DR AlphaFoldDB; C1GTI3; -.
DR SMR; C1GTI3; -.
DR STRING; 502779.C1GTI3; -.
DR EnsemblFungi; EEH39639; EEH39639; PAAG_01828.
DR GeneID; 9099321; -.
DR KEGG; pbl:PAAG_01828; -.
DR VEuPathDB; FungiDB:PAAG_01828; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002059; Partially assembled 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..993
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411728"
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..391
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 392..412
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..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..475
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 476..496
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..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..672
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 673..693
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..709
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 710..730
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 738..758
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..993
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 579..621
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 59
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 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 955
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 993 AA; 110019 MW; 94C9E48AD2F61DAB CRC64;
MSPAMANPRV RKFNPIAFTP LPVTLITTIV YLAVLILVLV TYLVVPPAPT LEMSPRGVNL
TEAWRDLQHL TGGFHPYNSR RNDDVHAWLL HRIEAIVREH SAAADDVPEV FVFDDNLSNL
TYSNGGVSKS PIVGVYFEST NIIVYIRGSE DDPQNWWEWS NGKPKGKGGV LVNAHYDSVS
TGYGATDDGM GVVSLLQLLR YFTIAGNKPR KGLVLLFNNG EEDYLNGARV YSQHAMSNFT
HTFLNLEGAG AGGRACLFRT TDTEVTRFYK NAKHPFGSVL AGDGFKLGLI RSQTDYVVFN
GVLGLRGLDV SFIAPRSRYH TDQDDARHTN VDSLWHMLSV AIATTEGLVS YTGTDFDSKT
TDQDKVNSGD GTLGVWFDIF GSAFAVFRLH TLFALSVTLL VSAPLVLFIT SIALSKTDRM
YLFSMSKSLG GTSETVSLRG LRGLFRTPII LTVTTVITIG LAYLLEKINP YIVHSSQFAV
WSMMLSVWIF VAWFLARVAD FFRPSALHRA YSYTWIFIAT WIMLVISTVY ANQKGIAAGY
FIFFYFAAVF LATWVSYLEL FSLPRKGYYA HQTSRGQRRR SSSLSSRLLT PSADELPSDI
GPNGAENLGD PDETDPTEST SLLRGQRTTF ANYRTGGNSG VTEYTAEGEH VREAGIFGHE
QSWSWTLPRW TWILQLLLLA PIVIILVGQV GLLLTTAMSQ IGSDGVSTFI VYLACALLST
LLFAPLFPFI HRFTYHVPTF LLLIFIGTLI YNLVAFPFSP ANRLKIFFIQ EVNLDDGTNK
VSLTGIQPYL TNTINAIPSA AGQTANCTQG PFGSLVRCSW SGPPPRVVKE DPGNDQTMGP
YTWISYNITK TVGKNEARIK VSGRNTRACK LKFDNPVADY RISGSAVDHR LPHTSRQGVA
EIRLWSRTWE NTWVVDVDWH SNPVKPGESK DGDEKQDVSK NELSGKVICL WSDNNESGVI
PALDEVRLYA PAWVAISKSA DGLVEASHDF IIQ
