PFF1_SORMK
ID PFF1_SORMK Reviewed; 1040 AA.
AC D1ZV85; F7VYW2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
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=SMAC_04453;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000014; CCC10708.1; -; Genomic_DNA.
DR RefSeq; XP_003343795.1; XM_003343747.1.
DR AlphaFoldDB; D1ZV85; -.
DR SMR; D1ZV85; -.
DR STRING; 771870.D1ZV85; -.
DR PRIDE; D1ZV85; -.
DR EnsemblFungi; CCC10708; CCC10708; SMAC_04453.
DR GeneID; 10801050; -.
DR KEGG; smp:SMAC_04453; -.
DR VEuPathDB; FungiDB:SMAC_04453; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; D1ZV85; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001881; 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..1040
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411743"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..405
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 406..426
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 437..456
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TOPO_DOM 457..462
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 463..483
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 491..511
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..521
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 522..542
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 716..736
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..758
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 759..779
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 780..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 786..806
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 807..1040
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 563..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 186
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 198
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 198
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 233
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 258
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 331
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 330
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1040 AA; 114823 MW; 0C1EDC2509EA0EC0 CRC64;
MINPISFRPG PVTFWTTLIY LALLIPIVII NEEPPAAPKT AEPFKGVNLT EAWLDLTTIT
RAYHPYNSKF NEEVRRYLLE KVESILEENG ATWVFDDQMA AAAKDGKSAA VTVFDDNVSN
STFVMGKSNG TTFTRTESIN NAAYFEGTNI LVYIRGKEDD DGDWWEADYV HGMRRNAKGL
TLVNAHYDSV STGFGATDDG MGVVTCLQVL KYFTTPGNQP QRGIVVMLNN GEEDWLYGAR
ALGQHKLNPF IHTFLNVEGA GAGGRAIVFR ATDREVMAAY ARTSHPFGTV IASDAFGMGF
ISSGTDYSVL VDAYGQRGID LAFFKPRARY HTNQDDTRHA SKESLWHILS ASIHTTKQLS
GDTGNTFIGQ RPDKAHGKVA NGRPSNGVWF DLFGKSFVLF GLRGMFAWSL TLLIATPLIL
VGITWLLRNL DKDYFFTSTV KTKEHPEYEA VPIGGWKGFF RWAMMVSIFY FSFWMIMRGA
NFVRPSALHR GYANLWLFVF GWIVLVAVTA LEDRRRIAAG YIFVFLESAI FLSCLISFVE
LLALPRKSAY ALQVQEDYDG HDHSGYQGYR DSTDGLSSGA RAESSASAGS PSSPTVAQEP
SKPTAPAGTT NGLSTAPSVA AHSSQPQPAP ATPTPGRSTS APIPSTTPRD EDESEDDDDE
ATERTPLVGG NGTNDRGRTT FATTYRRSIT ALVHGARKME EDGEPYEHEQ DWSGHLPSWA
WFFQFLLLGP FMIILAAQTG LMLTDAVYQT GSDGSKLFTP YLMIFFFTLL LILPLTPFIH
RVTHHIPVFL LVVFIVTLTY NLIAFPFSAN NRYKAFFGQY IDVATGENKV CYTGIEEYVR
PIIAELPSAS GRDVTCGKSL RRGSTIATCC FDGSAVPPKL GSEDLDGLPQ DNYADIITVN
ATRSHKKGDS SRTTARIEIT ADNTKSCFLQ FKKPVSALTI ESGSGWDDRF GQYPEDGVGL
VRLWHREFDK TWVVNAEWKG SETRKGDDEN DGTVICMWSD ANTPGTIPAL DEALQFVPSW
AAVTKFSEGL VEGRKAFKIV
