PFF1_AJECN
ID PFF1_AJECN Reviewed; 850 AA.
AC A6QS12;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=HCAG_00168;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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}.
CC -!- CAUTION: Although related to the peptidase M28 family, it lacks some
CC conserved zinc-binding and active site residues and therefore has
CC probably lost hydrolase activity. {ECO:0000305}.
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DR EMBL; CH476655; EDN02304.1; -; Genomic_DNA.
DR RefSeq; XP_001543122.1; XM_001543072.1.
DR AlphaFoldDB; A6QS12; -.
DR SMR; A6QS12; -.
DR STRING; 339724.A6QS12; -.
DR EnsemblFungi; EDN02304; EDN02304; HCAG_00168.
DR GeneID; 5449652; -.
DR KEGG; aje:HCAG_00168; -.
DR VEuPathDB; FungiDB:HCAG_00168; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000009297; 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; 2.
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..850
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411691"
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..282
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 283..303
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 309..329
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..363
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 364..384
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 394..414
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..425
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 426..446
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 530..550
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..563
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 564..584
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 591..611
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..850
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
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 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 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 850 AA; 94074 MW; D2964471A4FC3A66 CRC64;
MASSRAQWFN PIAFTPWPVT CITTIVYLAL LIPILVINLV VPSAPETNPK GVNLTEAWRD
LQHLTGGFHP YNSRRNDEVH EWLLSRINSI IRPTVEAGQP SSANDNLPEV FVFDDNRSNL
TYSNGGVGKT SIVGVYFEST NIIVYIRGSE DGLENWWEHS NGKPKGKGGV LVNAHYDSVS
TGYGATDDGI GVVSLLQLLR YFTTPGNNPR KGLVLLFNNG EEDYLNGAHP PEADTTQAQD
DTRHTNIDSL WHMLSASIGT TEGLVSYTGM DFDGKSKDQN KVNSGTGTLG VWFDMFGTAF
AVFRLHTLFA ISVALLVIAP LVIFVTSVIL SKTDRMYLFS MSKSLEGTGD QVSLRGLRGF
SRTPIILVIA TTIPICLAYL LEKVNPYIVH SSQFSVWSMM FSAWIFLAWF LACAADFFRP
SALHRAYSYT WIFIATWIML VINTVYANQK GIAAGPSTAE FPGAAGEDTD PTESTSLLRG
QRTTFANYRS SRPGGAAETD EREDINKGGT FEHEQSWSWT LPRWTWVLQL LLLAPIVLIL
VGQLALFLTA SMCQVGSDGV STFVVYLACS VFTTLLCIPL FPLIHRFTYH IPTFLFLVFI
GTLIYNLVAF PFSPANRLKT FFIQEVDLDN GSNTVSLTGI QPYLTDAINS IPSAAGQNIT
CDKTTPFGKL ERCSWSGLSP NVLGQGRERD NEIDPDKWIT YNITKTVGKN KARIEISGRN
TRACKLKFDR AVANFQVSGS AVDHRMPPTS RQGVSEIRLW SRTWENTWVV DINWHESADK
SDDDDDDHDD ENHDAPQNIL SGKAICMWSD GNQPGVIPAL DEVRLYAPSW IAISKAADGL
VEASHSFTIQ
