PFF1_CHAGB
ID PFF1_CHAGB Reviewed; 995 AA.
AC Q2GXG8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=CHGG_07336;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(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}.
CC -!- CAUTION: Although related to the peptidase M28 family, it lacks some
CC conserved zinc-binding sites involved in catalysis and therefore has
CC probably lost hydrolase activity. {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; CH408033; EAQ86083.1; -; Genomic_DNA.
DR RefSeq; XP_001224992.1; XM_001224991.1.
DR AlphaFoldDB; Q2GXG8; -.
DR STRING; 38033.XP_001224992.1; -.
DR EnsemblFungi; EAQ86083; EAQ86083; CHGG_07336.
DR GeneID; 4394163; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; Q2GXG8; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001056; 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..995
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411710"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..349
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 350..370
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 403..423
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..437
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 438..458
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 469..489
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..499
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 500..520
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..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..693
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 694..714
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..721
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 722..742
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..995
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 538..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
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 202
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 275
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 274
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 995 AA; 109277 MW; 4A5288DFACCCDF4D CRC64;
MVKNPFSFRS APVTFWTTVT YLALLIPIII INEGTPPAPS EESPIRGTNL TQAWLDLSTL
TRGYHPYNSH YNDDLRGSGS DNSEAAVTVF DDLSSNCTFL MSSGVAPAPN TPQVAAYFEG
TNILVYIRGK SDDQGRWWDT AAVHDSKQNE KGLTLYFTRS ENQPERGIVV MLNNGEEDYL
YGARALGQHP LNPYIHTFLN LEGAGAGGRA ILFRTTDREV TAAYAGSPDP FGTVIGSDAF
GLGFIRSGTD YSVLYDVFGQ RGLDLAFFKP RARYHTDQDD ARHASKGSLW HMLSASIHTA
TRLSSDTGDT FIGPRSDGAS GKVHNGSPSD GVWFDLFGKG FVLFGLRGMF AWSLTVLIAT
PLILMLLSYL LHRADKYYLF SSSVKPGDQP DDEALPVGGW KGFFRFPFAL VVAGSLTIGA
AFLMRKVNPF IIYSSRYSVL AMMVSLFYFS FWAIMRGANF ARPSALHRVY VQIWLFILGW
AMLVAVTVAE DRLRIGAEYM FVFLESSVFL SLFIALCELF ALPKKNAWAQ KMRDEQEERD
FHRGRLHSPL SSSQIPPPVP NQESTPPGTR HSNHTASTPT IRNEDEDDDA APTERTPLVG
GNADPTRTTF ATTYRRSISA LVTRARRYSD SDGAGLHHDP FEREQAWSGR LPSWTWFLQF
LLLGPFTITL AAQTALMLVD AVHQTGADGS SLLMPYLIAA LGVVLLLLPL APFVHRVSHH
VPVFLAAVFA ATLVYNLVAF PFSAAARYKV YFVQAVDLET DANRVCYHGV EEYVRAVVDS
LPSASGRDVD CAGGSKKAGL VSCCFDGVAT PPRLTAGASG GSGKHEEEGY GHLVAVNASR
TGEHAARIEI VANNTKACFL EFEKPVSGLS VHGSSGWDER FGQYPDAGVK NVRLWHRRWD
EKWVADVQWK DAEGEAASSS SSSSSFSDGD WEVLGDEDLR KRAEGLKGTV VCMWSDANVP
GTIPALDEAL RFVPAWVAVT KLSEGLVEGR RRFEV
