PFF1_AJECH
ID PFF1_AJECH Reviewed; 920 AA.
AC C6H1N5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-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=HCDG_00617;
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143;
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.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-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; GG692419; EER45038.1; -; Genomic_DNA.
DR AlphaFoldDB; C6H1N5; -.
DR STRING; 544712.C6H1N5; -.
DR EnsemblFungi; EER45038; EER45038; HCDG_00617.
DR VEuPathDB; FungiDB:HCDG_00617; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000002624; 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..920
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411690"
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..378
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 379..399
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 434..454
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..463
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 464..484
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 496..516
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..520
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 521..541
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..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..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 721..741
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 742..920
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 556..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..588
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 306
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 305
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 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 920 AA; 101617 MW; 7C016B74B4670D65 CRC64;
MASSRAQRFN PIAFTPWPVT CITTIVYLAL LIPILVINLV VPSAPETNPK GVNLTEAWRD
LQHLTGGFHP YNSRRNDEVH EWLLSRINSI IRPTVEAGQR SSATDNLPEV FVFDDNRSNL
TYSNGGVGKT SIVGVYFEST NIIVYIRGSE DDSENWRERS NGKPKGKGGV LVNAHYDSVS
TGYGATDDGI GVVSLLQLLR YFTTPGNNPR KGLVLLFNNG EEDYLNGAHV FSQHPLSNFT
HTFLNLEDTE VTRFYGNTKH PFGSVLAADG FKMGLLRSQT DYVVFNGILG LRGLDLAFIA
PRSRYHTDQD DTRHTSIDSL WHMLSASIGT TEGLVSYTGM DFDGKSKGQN KVNSGAGSLG
VWFDMFGTAF AVFRLHTLFA ISVALLVIAP LVIFITSVIL SKTDRMYLFS MSKSLEGTGD
QVSLRGLRGF SRTPIILVIA TTIPICLAYL LEKVNPYIVH SSQFSVWSMM FSAWIFLAWF
LACAADFFRP SALHRAYSYT WIFVATWIML VINTVYANQK GIAAGYFLLF YFAGAFLATW
ISYLELFALP RKGDFARQTT GRRPSSLSSR LLTSSADELR SNASPSTAEF PGAAGEDTDP
TESTSLLRGQ RTTFANYRTS GPGGAAEETD EREDINKGGT FEHEQSWSWT LPRWTWVLQL
LLLAPIVLIL VGQLALFLTA SMCQVGSDGV STFVVYLACA VFTTLLCIPL FPLIHRFTYH
IPTFLFLVFI GTLIYNLVAF PFSPANRLKT FFIQEVDLDN GSSTVSLTGI QPYLTEAINS
IPSAAGQNIT CDKTTPFGML ERCSWSGLSP NVLGQGRERD TEIVPDKWIT YNITKTVGKN
KARIEISGRN TRACKLKFDR AVANFQVSGS AVDHRMPPTS RQGPGVIPAL DEVRLYAPSW
IAISKAADGL VEASHSFTIQ
