PFF1_COCPS
ID PFF1_COCPS Reviewed; 1012 AA.
AC E9CZZ9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 33.
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=CPSG_03427;
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; GL636489; EFW20252.1; -; Genomic_DNA.
DR AlphaFoldDB; E9CZZ9; -.
DR SMR; E9CZZ9; -.
DR STRING; 443226.E9CZZ9; -.
DR PRIDE; E9CZZ9; -.
DR EnsemblFungi; EFW20252; EFW20252; CPSG_03427.
DR VEuPathDB; FungiDB:CPSG_03427; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR Proteomes; UP000002497; 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..1012
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411713"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 61..81
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..432
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 433..453
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 488..508
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..518
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 519..539
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 551..571
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..575
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 576..596
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 711..731
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..743
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 744..764
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 778..798
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 799..1012
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 614..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 215
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 227
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 227
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 262
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 287
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 360
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 359
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1012 AA; 112308 MW; D6907BCC4EFD917C CRC64;
MRRSTDPRNL LVRRGPLLVD GESAISELDP GFFPTGDAPK MSSTTRRRFN LIAFTPGPVT
VISSLVYLAL LIPLLLVHTI VPSAPKSNPK GVDLSEAWND LQHLTSGFHP YNSHRNDEIH
QWLLQRVGHI LDASRKAHED DAMGSVAPDV FVFDDQQSNL TFSGGGVGNK PITGVYFEGK
NIIVYIRGLE DDKENWWDSP GGKPKGKGGV LVNAHYDSVS TGFGATDDGV GVVSVLQLIK
FFTSPGNLPR KGLVLLLNNG EEDYLNGARA YSQHPLSKYT HTFLNLEGAG AGGRAALFRT
TDTEVTRFYK SSPHPFGSVL AADGFKMGLI RSETDYAVFK GVLGLRGLDV AFIEPRARYH
TDQDDVRHTS IDSVWHMLSA AIATTKGLVS YTGSEFDGRA PGKGMVNSGV GTHGVWFDLF
GSSFAVFRLH TLFAISVTLL VVCPIVLFVI GIILSKMDKM YLFSIHETIP ETKEKVSVRG
LRGLFRYPII LVVSSGILIG LSYLLAKVNP FIVHSSSYAV WSMMLSSWIF MTWFLSCIAD
FFRPSALHRA YTFTWQLLVM WVLLVISTVY VNQHDIAAGY FIVFYFAGTF LATLISYLEL
FALPNKTQYA REQSQYPSRL GSNRSSRILS PSADELPTGG DNNGEIYDGE EEPTESSSLL
GRQRRTTFAN YTRTGRDLAS SESGTYEDHS ETGVFGEEQK WSASLPTWTW VLQFLFVGPV
VIMFIGQLGL FLTSAMNQVG ADGVGLLVVY IAIAVFSVLL LIPLSPFIHR FTYHVPTFLL
LVFIATLIYN LAAFPFSAEN RLKIFFVQEL NLDTGRNQVS LTGVDPYVQD IIRAIPSASK
ENISCDSELD SGRRKCSWPG LAPEVVQDEP TDRWLSFNIS KPSSQETKDT PVLHARLHVS
GKNTRACRVN FERPIRDYSL PGSALDDRMP HTLPQGISEI RLWSRTWENV WTVDVQWDAE
DMDELHGRVV CLWSDANQLG SIPALDELRL FAPPWVAISK LKDGLVEVSR GF
