PFF1_VERA1
ID PFF1_VERA1 Reviewed; 1020 AA.
AC C9SXB4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
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=VDBG_09414;
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136;
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(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; DS985228; EEY23304.1; -; Genomic_DNA.
DR RefSeq; XP_003000219.1; XM_003000173.1.
DR AlphaFoldDB; C9SXB4; -.
DR SMR; C9SXB4; -.
DR STRING; 526221.C9SXB4; -.
DR PRIDE; C9SXB4; -.
DR EnsemblFungi; EEY23304; EEY23304; VDBG_09414.
DR GeneID; 9527919; -.
DR KEGG; val:VDBG_09414; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000008698; 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..1020
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411748"
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..410
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 411..431
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 468..488
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..491
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 492..512
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 530..550
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..561
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 562..582
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 691..711
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..724
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 725..745
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..750
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 751..771
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 772..1020
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 609..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..631
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 191
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 203
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 203
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 238
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 263
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 336
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 335
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 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1020 AA; 112418 MW; 7010804CC6E35FDF CRC64;
MKCHNPFGFR VGPVTFWTII IYLALLVPLL WIHETVPPAP SSPTPTPGIN LTEAWHDLTT
ITKHYHPYNS RDNERVGDYI LERIAAILDR NDVNWTLEKT GARNVDVTLE LSSRSSSAPS
VTVFDDNLAN VTWATDIGML GDHTAGVGTY FEGTNKLVYI RGTEDEQGEW WKSGKNDVRV
IGKGGVLVNA HYDSVASGYG ATDDGMGCVS ILQILNYFTT QGRQPKRGLL LLFNNGEEDG
LLGAKAFANS PLFSFPTTFV NLEGAGAGGR AVLFRSSDEQ VTKAYQKAPH PFGLVVASDG
FSMGLVKSQT DFVVWDDIFG QRGLDIAFYR PRPRYHTDQD DTRHASPASL WHMLSNSIAA
VKSLSDNTHT FSGQRSDGDR RKVPSGSHAS KGVWFDMFGK GFAVFGLRGL FAWSLTLLIV
SPLILAILVF ILNRHDKLYF FSRKINVHNE GSEDPVSIGG FRGFTRFPIA VGFSGALTLA
SAFLLTKINP MIVYSSEYAV WGMMLSLFYV SLWMTLKGSS AVRPSALQRG YIHIWLFIVS
WGLLIVVAVT EDRLKIASGY PVVFLHSALF LSTVISFLEL FGLTKKHDYA RRAHDDHQVR
DRIGELPHDD ALIAPDTPND EAEDSDGEDS EHEPTETTPL RAGGDSRVRS TFGTAYRSVF
TRKSSPDKHK PFENEQPWSG RLPGWTWILQ FLLLAPINVI LWGQIGLFAV AATQAGGADG
GSVLTTYLII AVLSIVILVP LAPFIHRVHY YVPIILFAAF AGTLIYNLIA FPFSANNRYK
IYFVQEIDVS DGSTKVSLTG LDKYVHSVIG ELPSTSGKVI TCTDSNARSG LVDCSYDGSA
VPPLLHGGLE NGTVTVTNKR YQHLVSVNIT RSNDSKNRAT LSINAADSKV CTVIFDQPVS
NFAIRGSEGL DSRLGQYPDA GVGSLRLFRR DWTSPWVVDV EWNDQHKVGE VALETDKPVD
KDAVEELRKR AGISGTIKCH YSDANVPETI PAFHECLQYS PDWAAFSKAD VGLVRPVKRF
