PFF1_AJECG
ID PFF1_AJECG Reviewed; 985 AA.
AC C0NU79;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=HCBG_06910;
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) 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; GG663372; EEH04959.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NU79; -.
DR SMR; C0NU79; -.
DR STRING; 447093.C0NU79; -.
DR EnsemblFungi; EEH04959; EEH04959; HCBG_06910.
DR VEuPathDB; FungiDB:HCBG_06910; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; C0NU79; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001631; 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..985
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411689"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..388
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 389..409
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 441..461
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..470
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 471..491
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 503..523
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..527
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 528..548
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 667..687
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 688..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..985
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 563..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..595
FT /note="Polar residues"
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 53
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 767
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 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 985 AA; 109043 MW; 1D6D51B37DA33C83 CRC64;
MASSRAQRFN PIAFTPWPVT CITTIVYLAL LIPILVINLV VPSAPETNPK GVNLTEAWRD
LQHLTGGFHP YNSRRNDEVH EWLLSRINSI IRPTVEAGQR SSATDNLPEV FVFDDNRSNL
TYSNGGVGKT SIVGVYFEST NIIVYIRGSE DDLENWWERS NGKPKGKGGV LVNAHYDSVS
TGYGATDDGI GVVSLLQLLR YFTTPGNNPR KGLVLLFNNG EEDYLNGAHV FSQHPLSNFT
HTFLNLEGAG AGGRAALFRT TDTEVTRFYG NTKHPFGSVL AADGFKMGLL RSQTDYVVFN
GILGLRGLDL AFIAPRSRYH TDQDDTRHTS IDSLWHMLSA SIGTTEGLVS YTGMDFDGKS
KDQNKVNSGA GTLGVWFDMF GTAFAVFRLH TLFAISVALL VIAPLVIFVT NRMYLFSMSK
SLEGTGDQVS LRGLRGFSRT PIILVTATTI PICLAYLLEK VNPYIVHSSQ FSVWSMMFSA
WIFLAWFLAC AADFFRPSAL HRAYSYTWIF IATWIMLVIN TVYANQKGIA AGYFLLFYFA
GAFLATWISY LELFALPRKG DFARQTTGRR PSSLSSRLLT SSADELRSNA SPSTAEFPGA
AGEDTDPTES TSLLRGQRTT FANYRTSGPG GAAEETDERE DINKGGTFEH EQSWSWTLPR
WTWVLQLLLL APIVLILVGQ LALFLTASMC QVGSDGVSTF VVYLACAVFT TLLCIPLFPL
IHRFTYHIPT FLFLVFIGTL IYNLVAFPFS PANRLKTFFI QEVDLDNGSN TVSLTGIQPY
LTDAINSIPS AAGQNITCDK TTPFGKLERC SWSGLSPNVL GQGRERDTEI VPDKWITYNI
TKTVGKNKAR IEISGRNTRA CKLKFDRAVA NFQVSGSAVD HRMPPTSRQG VAEIRLWSRT
WENTWVVDIN WHESADESDD DDDDDEKHDA PQNVLSGKAI CMWSDANQPG VIPALDEVRL
YAPSWIAISK AADGLVEASH SFTIQ
