PFF1_TALMQ
ID PFF1_TALMQ Reviewed; 977 AA.
AC B6Q656;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=PMAA_024220;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995899; EEA27551.1; -; Genomic_DNA.
DR RefSeq; XP_002144066.1; XM_002144030.1.
DR AlphaFoldDB; B6Q656; -.
DR SMR; B6Q656; -.
DR STRING; 441960.B6Q656; -.
DR EnsemblFungi; EEA27551; EEA27551; PMAA_024220.
DR GeneID; 7021878; -.
DR KEGG; tmf:PMAA_024220; -.
DR VEuPathDB; FungiDB:PMAA_024220; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 166108at2759; -.
DR PhylomeDB; B6Q656; -.
DR Proteomes; UP000001294; 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..977
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411732"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..383
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 384..404
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 439..459
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..469
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 470..490
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 501..521
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..525
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 526..546
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 660..680
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..696
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 697..717
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 727..747
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..977
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 566..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 166
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 178
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 178
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 213
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="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 311
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 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 977 AA; 108491 MW; B054960A6440A71A CRC64;
MARSRTAGRC NPFAFYRVPV TVFVTLIYVA LLAPIIVVHH ILPAVPESDV EGLDLHEAWR
DLQHLTNGFH PYNSHKNDEV RSWLLTRIDE IVSTNVKDAK QQDGVRTFVF DDNQSNLTVV
QSNLGVYFEG TNIIVYICGQ EDDKREWWKE PGLSPSGKGG VLVNAHYDSV STGYGATDDG
VGVISCLQLI KYFTTPGHEP TRGLVVLLNN GEEDFLNGAR VYSQHPISKL PHTFLNLEGA
GAGGRATLFR SSDTEVTKFY QRSPYPFGSV FSDAGFKLGM IRSQTDYIVF EGDMGLRGLD
VAFMEPRARY HTNQDDAKHT SQQSLWHMLS AAVATTEGLV SDTSHDFEGR PQGPGKVPSG
TGSGAVWFDL FGTAFAVFEI HTLFALSVTL LIVGPLTLFI TSIILANQDR MYLFGISVPV
DDGFGSVPLR GWRGFFRFPF IFGSTTASVV ALAYLMAKIN PMIAHSSEYA VWSMMISAWV
FVAWFLSRIA NFARPSALHR IYVLTWMFLL TWVLLVITTV YENRDGIASG YFVIFYAFGT
FMATWISYLE LFSLPKKSDF ANKVSGQISS RPTSLGGSRL LTPSGESVGQ HPEDEEPTES
TSLLRGQRTS FANYTRPVED DGDGDLLSTG VSTDVSEARD FNVYGYEQPW SANLPKWTWI
LQFLLIAPIV IILIGQLGLL ITSAIHQTMQ DGSSTLVPYL IIALLTTFLF MPTLPFIHRY
TYHIPTFLFL IFVATLVYNL VAFPFSGNNR TKLFFLQEVD LDTGANRVSL TGIQPFVSDA
VASIPSADGQ NISCIPKMDR TECSWESSLV PHVITHPGSE KEETPLNEWV KYKATRLEPG
SQNSNRAQIK ISGLNTRGCL LHFDKPITRF HVTGSAIDSR FPSNPSLEDG TEDGVREIRL
WSRTWGNQWV VDAEWASDED VNNEEDTLTG KATCLWSDAN TQGAIPALDE VIQYSPDWVA
ITKLDAGLVK GSRSFEV
