PFF1_ASPCL
ID PFF1_ASPCL Reviewed; 973 AA.
AC A1CR68;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=ACLA_028640;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW08139.1; -; Genomic_DNA.
DR RefSeq; XP_001269565.1; XM_001269564.1.
DR AlphaFoldDB; A1CR68; -.
DR SMR; A1CR68; -.
DR STRING; 5057.CADACLAP00002006; -.
DR EnsemblFungi; EAW08139; EAW08139; ACLA_028640.
DR GeneID; 4701187; -.
DR KEGG; act:ACLA_028640; -.
DR VEuPathDB; FungiDB:ACLA_028640; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000006701; 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..973
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411698"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..383
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 384..404
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 439..459
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..469
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 470..490
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 505..525
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..529
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 530..550
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 675..695
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696..708
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 709..729
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 736..756
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..973
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 572..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..612
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 167
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 179
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 179
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 214
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 239
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 312
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 311
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 803
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 973 AA; 107169 MW; 77377B5DA524BADB CRC64;
MARQYSRTNP LGFTPWPVTI ITALVYLALV IPLLVVQHVV PSAPGSDPAG LNLTEAWADL
QVLTNGFHPY NSHRNDDVHK WLLQRVHEII DSAPARSTDS AHPPAVFVFD DDQSNLTFSG
RGNELGVYFE STNILVYIRG TEDDETQWWA DPQGQPASKG GVLVNAHYDS VSTGYGATDD
GMGVVSCLQL LRYFTTPGHA PRRGLVVLLN NGEEDFLNGA RVYSQHPLSR LPHTFVNLEG
AGAGGRASLF RSSDTEVTRP YARAPHPFGS VLSANGFEAG LISSQTDYVV LEGDLGLRGL
DIAFIEPRAR YHTDQDDARH TSVDSLWHML SAAVATTEGL VDDASDQFDG APREDGKVAS
GSGSKAVWFD LFGSTLAVFE LHTLFALSVT LLIVAPLVLL ATSIALVRAD RMYLFRSTAR
VPGSDDFDEG VSLQGVRGFF RFPFLLVIPT GVAVGLAYLV TKINPYIIHS SEYAVWSMMI
SAWVFLAWFV SRVADFARPS AFHRVYVLTW MFVAEWVLLV IATVYENRYG LAGGYFVFFA
LSGTFLATWI SYLELFALPR KSEYARQIAP PSRYASNHGS RLGTSSGEHG MDDAEDEEDD
DGDDEDEARN VEEEPTESTS LLRGRGQRTT FANYVRVTGD YLHGAGDDEP RETHVYGREQ
AWSAGLPKWT WVLQFLLSAP IVLILVGPLA LLLTAALRQT AQDGSSPLFV YIAIAVLTTL
LVTPLLPFIH RYTHHIPLFL LLVFTGTLIY NLVAFPFSPS NRLKLFFLQE VDLDTGVNRA
FLSGAHPFVY EVARSLPSAA GQNVSCDLSA ARPKCSWYGI PPQVQATATP DTADWVSFNI
TRSADQPTRA RFSVAGQNTR ACRLVFDDPV RSFAVLDSAY DPRFPHLSPQ GTQEIRLWSR
EWGHTWTVDV EWTVPAVDGE SRGVSGRVVC LWSDGNAPGV IPALDEVRRY SPVWTAVSKL
SDGLVEGSRR FEV
