PFF1_SCLS1
ID PFF1_SCLS1 Reviewed; 1076 AA.
AC A7F4S1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=SS1G_12596;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(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; CH476641; EDN97742.1; -; Genomic_DNA.
DR RefSeq; XP_001586609.1; XM_001586559.1.
DR AlphaFoldDB; A7F4S1; -.
DR SMR; A7F4S1; -.
DR STRING; 665079.A7F4S1; -.
DR PRIDE; A7F4S1; -.
DR EnsemblFungi; EDN97742; EDN97742; SS1G_12596.
DR GeneID; 5482541; -.
DR KEGG; ssl:SS1G_12596; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; A7F4S1; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000001312; 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; IBA:GO_Central.
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..1076
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411742"
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..437
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 438..458
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 492..512
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..525
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 526..546
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 557..577
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..584
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 585..605
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 739..759
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 760..771
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 772..792
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 800..820
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 821..1076
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 619..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 220
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 232
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 232
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 267
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 292
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 364
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 363
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 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1076 AA; 120160 MW; B4546DE97BE5A967 CRC64;
MKCYNPSAFV PMAVTLVTVV IYLGVFIPLL IIHETVPSAP DDPTLYNGLN LTEAWLDLQS
LSDGYHPFNS RKNDDVRNWL LKRIDEILDH NQIQYTTENE TADTSDVQLE SDFDKDVPES
MSGPNNFNDD SVEYHEDLRT RKVSPAVTVF NDLRSNYSSN ALTSIGVKGR RLGISTYFEG
NNIICYVRGN DDEEGEWWKT GSVNSKGKMH GRGGVMVNAH FDSVSTGFGA TDDGVGVVTA
LQLIRYFTTP ENRPQKGFVA LFNNGEEDGL YGAKAFLSHP MAKFVHTFLN LEGAGAGGRA
TLFRSTDTEV TRAYAHAKHP FGTVVSSDGF SSGFVRSETD YVVFRAEGYR GLDVAFWQPR
SQYHTDQDDA KHTSIDSLWH MLSASVATTR SLTRDTSNTF VGPRSDDKIG KVSNGKGSDG
VWFDIFGTVF AVFRLRTLFA WSLTLLIASP LILFAVSYLL NRQEKFYFFA GSIKSKNPED
EPISLGGWRG AFRFPITLFI TSAITFACAS LINKINPMII YSSPYAVWSM SATLFFSVFW
FIMAGCNFVR PSALQRGYAF MWMFVFGWIL LVVATVYEDR FKISGGYLFV FYEAAIFLAT
LIAICEQFAL PRKSTYIEDS QNDHSDNQDH HHQAVMGTDG ANGADEPNAD DEAAEEDQEE
TVNATAFPHE TTPLIGGGQP SHRASVSTSF ANRYRQVVPE SYDGPADHDD KKGHKKHPYG
GEQEWSAKLP IWTWLVQYLL VGPFILVILG QVGLFLVAAL HQTGTDGSPL FLPYLIVAIF
SILLLLPVTP FIHRLTHHMP TFFFLVFIGT LIYNLVAFPF SPNNRYKAYF QQTVDLDTGV
NRVTLVGIEQ YIRNIITNIP SAAGQSINCE ANPRIRSGLS FCSYEGIPPQ VVDNVVEGVP
PEKGYSDWLS FNVSRVPNEN KATFHISGVE TRACILRFDD PFSEFKVHGG AKSEERWDDV
PDSGSDQIKL WHRDWNKEWV VDVEWAVGED MKPGDEGRSG RVVCLWSDAN KRGVIPALDE
AQRFSPQWTS VVKLMDGLVE GSKRRVGELV RVGGWKKGRR DDFSLALGLA FLLAYV
