PFF1_METAQ
ID PFF1_METAQ Reviewed; 1029 AA.
AC E9E6S9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
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=MAC_05577;
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698512; EFY88368.1; -; Genomic_DNA.
DR RefSeq; XP_007811917.1; XM_007813726.1.
DR AlphaFoldDB; E9E6S9; -.
DR SMR; E9E6S9; -.
DR STRING; 92637.XP_007811917.1; -.
DR EnsemblFungi; EFY88368; EFY88368; MAC_05577.
DR GeneID; 19249888; -.
DR KEGG; maw:MAC_05577; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; E9E6S9; -.
DR OMA; RIHCDED; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002499; 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..1029
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411723"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..415
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 416..436
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 470..490
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..493
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 494..514
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 533..553
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..560
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 561..581
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 699..719
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..735
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 736..756
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 764..784
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 785..1029
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 596..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 194
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 206
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 206
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 241
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 266
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 339
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 338
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1029 AA; 114089 MW; B57A6C7D5E7C6634 CRC64;
MKLSNPFVFR PGPVSFWTTI VYLAIIIPLI YVQETVPPAP PEKDLPQGVN LTEAWLDLEV
ITRSYHPFNS HSNDIVRQYL VRRSRDILER NGIDYTTDLT GGVPWESRYL SSAEHPAQAA
EASARPRGAT LFDDRISNVT MTNPQPNDTM GRYFEGNNFY VYIHGSEDPE GDWWTSDNVQ
RVARNGAGVL VNCHFDSVST GYGATDDGVA CVSLLQLLSH FTSKGHQPKN GIVLLFNNAE
EDGLLGAKAF GYSPLVQFCN TLVNLEGAGA GGRAMLFRTT DLEAAEAYSK SPHPFGSVVA
SNAFERGVIK SGTDYSVFVD NYGQRGLDIA FYSPRSRYHT EEDDARHTSV DSIWHMLSAA
LATTESLART TSTKFNGPRS DGRKDLVQSG RPTAGVWFDW YGSSWSAFSL RGLFAWTLTL
LITTPIVLFV VTYVLVRDDK WYFFATRVDS SVGDGEETVS FGGWKGFVRF PFALVVATAL
TIGSVFLLAK VNPLIIYSSG YSVWAMMLSL FYFVSWLLLR GAHFVRPSAL QRGFTLIWLF
IITWVLSVFA AVAEDRMNMG AVYSLAFLHT LVFAAVLISL LEQYALPAKQ DFARQLSGEN
EEGEEQEQEN LSGDGGNEQN HEDRGEADIA AAPTETTPLR ADEEGQGSSE QTTTFANTYR
RPVPETRGAT HSGNNRKRSF PPYENEQAWS GRLPTWTWFI QLLLLVPLYV TVLGNLALVQ
TTSMGMTGTD GSSLLVPLMG VGILTILLLL PLTPFIHRVS HHVPLFLLLV FIGTLIYNLT
AFPFSANNRF KFYFKQVVDL DKGSNVVTLN GLEKFVRPVI GSLPTPAGQR IHCDEDPFLS
NLRNCQYDAS LLPPDVANGE KLENLISFEA SKSKNGKTVL VSLDALNTRV CFLDTSSPIF
GFSVDGGAKR DDRFGSFPPE GLQQIQLWRR DWEKGWNVTL YLGGNVLPTN QDSVEATEVD
EVDDDPSGGE LKRRAVREFV VTARCAWSDV NSANTIPAFH EVKQFMPRWA IVAKKSVGLV
EITKKIKVT
