PFF1_EMENI
ID PFF1_EMENI Reviewed; 953 AA.
AC C8V4D5; Q15I80; Q5B5I0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=AN10522;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAA59299.1; Type=Erroneous gene model prediction; Note=The predicted gene AN4200 has been split into 2 genes: AN10516 and AN10522.; Evidence={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; AACD01000068; EAA59299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF74498.1; -; Genomic_DNA.
DR RefSeq; XP_661804.1; XM_656712.1.
DR AlphaFoldDB; C8V4D5; -.
DR SMR; C8V4D5; -.
DR STRING; 162425.CADANIAP00004465; -.
DR EnsemblFungi; CBF74498; CBF74498; ANIA_10522.
DR EnsemblFungi; EAA59299; EAA59299; AN4200.2.
DR GeneID; 2873613; -.
DR KEGG; ani:AN4200.2; -.
DR VEuPathDB; FungiDB:AN10522; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_003436_0_0_1; -.
DR InParanoid; C8V4D5; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; 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..953
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000413172"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..382
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 383..403
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 438..458
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..464
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 465..485
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 500..520
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..524
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 525..545
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 651..671
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..684
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 685..705
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 706..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 712..732
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 733..953
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 570..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 165
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 177
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 177
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 212
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 237
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 310
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 309
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 953 AA; 106352 MW; DC9DECF166A8BACC CRC64;
MDQTKPPRRN PLAFTPWPVT LITAVVYLAF VIPLLVIHHV VPSAPTSSPD GLNITEAWND
LQVLTAGYRP YNSRQNDKIH DWLLHRINEI LGAAPPATTD EKKPDVFVFD DTRSNLTFAR
DNLAVYFEGT NILVYIRGED DDQEQWWELP EGSPKGKGGV LVNAHYDSVS TGYGATDDGV
GVVTCLQLVK YFTTPKNAPR KGLVVLFNNG EEDFLNGARV YSQHPLSRFP HTFLNLEGAG
AGGRAVLFRS SDAEVAASYM RSKHPFGSVL GSDGFKAGLI RSQTDYVVFE GDMGLRGLDV
AFLEPRARYH TDQDDTRHTS KDSLWHMLST AVATTEDLVS DTSDRFDGPA RNDHKIASGT
GHQAVWFDLY GSTFVLFRLH TLFALSVTLL VVAPIVLLLT SIILTKVDKM YLFRTSIRPE
GSLEVLPLYG DRGVIRYPFL LGIPTAVTIG LAYLLTKFNP YIVHSSQYAV WSMMVSVWIF
LAWFVSRVAD FARPSAFHRV YTLTWTFVVM WVLQVIATVY QDRWALGGSY FIFFAYAGTF
LATWISYLEL FALPRKSEYA NHLRPVSRHA SSHSSRRGLS EEDEEDEDEA PTESTSLLGS
RQRTTFANYV RVNADTADLS DSEEHTQDVN VYGLEQRWSA SLPKWLWLLQ FLLAAPIVLI
LVGPIALLLT GSLHQTGQDG SSSLFIYIAI VALTTLLLSP MLPFVHRCTY HIPLFMLAVF
AGTLIYNLVA FPFSDSNRLK LFFIQEVDLD TGLNTASLTG VQPFVHDVAV GLPSAAGQNV
TCGPFGDRFK CSWTGIPPHV LTEDKPVEEW LSFEVSRSID KPRHAQLQIS GQNTRACKVV
FDSPIKNFHV AGSAYDPRFP HTYAKGIKEI RLWSRVWDNT WTVDVEWFNP DSSSDHSKTS
GSLTGQVVCL WSDYNQPGTI PALDEVRQYG PAWIGVSKLA DGLVEGRKSF EIA
