PFF1_METRA
ID PFF1_METRA Reviewed; 1032 AA.
AC E9EYB5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 28.
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=MAA_05014;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADNJ02000001; EFZ00086.1; -; Genomic_DNA.
DR RefSeq; XP_007820716.1; XM_007822525.1.
DR AlphaFoldDB; E9EYB5; -.
DR SMR; E9EYB5; -.
DR EnsemblFungi; EFZ00086; EFZ00086; MAA_05014.
DR GeneID; 19259300; -.
DR KEGG; maj:MAA_05014; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR Proteomes; UP000002498; 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; Transmembrane; Transmembrane helix; Vacuole; Zinc.
FT CHAIN 1..1032
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411724"
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..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 702..722
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..738
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 739..759
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 760..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 767..787
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 788..1032
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 595..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
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 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1032 AA; 114636 MW; 6D9713BE45BABFAD CRC64;
MKLGNPFVFR PGPVSFWTTI VYLAIIIPLI YVQETVPPAP SEKELPQGVN LTEAWLDLEV
ITRSYHPFNS HSNDIVREYL MRRSRDILER NGIDYTTDLT GGVPWESRYL SSAEHPVQAA
EVSARPRGAT LFDDRISNVT MTNPQPNNTM GRYFEGNNFY VYIHGSEDPE GDWWTSDNVQ
RVARNGAGVL VNCHFDSVST GYGATDDGMA CISLLQLLSH FTSEGHQPKN GIVLLFNNAE
EDGLFGAQAF GYSPLVQFCN TFVNLEGAGA GGRAMLFRTT DLEAAEAYSK SPHPFGSVVA
SNAFERGVIK SGTDYSVFVD NYGQRGLDIA FYSPRSRYHT EEDDARHTSV DSIWHMLSAA
LATTESLART TSTQFNGPRS DGRKDLVQSG RPTAGVWFDW YGSSWSAFAL RGLFAWTLTL
LITTPLVLFV VTYLLVRDDK WYFFATKVDS TVGDGEETVS FGGWKGFVRF PFALVVATAL
TIGSVFLLAK VNPLIIYSSG YSVWAMMISL FYFVSWLLLR GAHFVRPSAL QRGFTLIWLF
IITWVLSVFA AVAEDRMNMG AVYPLAFLHT FAFAAVLISL LEQYALPAKQ DFARQVSGEN
EEEEEQEQEN LLGDGGNDAN EQNNEDRGDT DIAATPTETT PLRAGEEGHG SSEQTTTFAN
TYRRPVPETR VETRSGNNRK RSFPPYENEQ AWSGRLPTWT WFIQLLLLVP LYVTVLGNLA
LVQTTSIGKT GTDGSSLLAP LMGVGILAIL LLLPLTPFIH RVSHHVPLFL FLVFIGTLIY
NLTAFPFSDN NRFKFYFKQV VDLDKGSNVV TLNGLEEFVR PVISSIPTPA GQRIHCDEDP
FLSNLRNCQY DASLLPPDVA DGEELESLIS IEASKSKNGK TILVSLDALN TRVCYLDTSF
PIFGFSVHGG AKRDDRFGSF PPEGLQQIQL WRRDWEKGWN VTLHLGGHVL PMNEDSVEAT
EVDEVDDDPS GGELKRGAAK ELIVTARCAW SDANSANTIP AFHEVKQFMP RWAIVAKKTV
GLVEITKKIK VA
