位置:首页 > 蛋白库 > PFF1_ASPFC
PFF1_ASPFC
ID   PFF1_ASPFC              Reviewed;         965 AA.
AC   B0XPG0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
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=AFUB_006350;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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   ---------------------------------------------------------------------------
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; DS499594; EDP55933.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XPG0; -.
DR   SMR; B0XPG0; -.
DR   EnsemblFungi; EDP55933; EDP55933; AFUB_006350.
DR   VEuPathDB; FungiDB:AFUB_006350; -.
DR   HOGENOM; CLU_006412_1_0_1; -.
DR   PhylomeDB; B0XPG0; -.
DR   Proteomes; UP000001699; 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; Transmembrane; Transmembrane helix; Vacuole; Zinc.
FT   CHAIN           1..965
FT                   /note="Vacuolar membrane protease"
FT                   /id="PRO_0000411699"
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..387
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        388..408
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        409..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        442..462
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..472
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        473..493
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        494..507
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        508..528
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        529..532
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        533..553
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        554..661
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        662..682
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        683..698
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        699..719
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        720..725
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   TRANSMEM        726..746
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        747..965
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250|UniProtKB:P38244"
FT   REGION          577..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..606
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P80561"
FT   BINDING         171
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         183
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         183
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         218
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         243
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         316
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            315
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        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        793
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        830
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   965 AA;  106578 MW;  B180E8FBCF5B9E5C CRC64;
     MARPSLSPSN PLGFTPWPVT VITAVVYLAL VVPLLVVHHV VPSAPSSSPK GLNLTEAWAD
     LQELTHGFHP YNSHRNDEVH EWLLKRILEL IDSAPPASEY GSVGEEKPDI VVFDDTQSNL
     TFSGRGSGLG VYFESTNIMV YIRGWEEDRE RWWEDPHGRP AGKGGVLVNA HYDSVSTGYG
     ATDDGVGVVS CLQLIKYFTT PGHVPRRGLV LLFNNGEEDF LNGARVYSQH PISQLPHTFL
     NLEGAGAGGR ATLFRSSDAE VTKPYMRAPH PFGSVLSANG FEAGLISSQT DYVVFEGDLG
     LRGLDVAFME PRARYHTDED DARHTSLASV WHMLSAAVAT TEGLVSDASS RFEGLPREDG
     RIASGSGPKG VWFDLFGSAF VVFELHTLFA LSVTLLVVAP LVLLVTSIAL ARADKMYLFR
     SSASPEDSDG SEVVPLHGVR GFFRFPFLLV IPTAVTVGLA YLVTKFNPYI IHSSEYAVWS
     MMISAWVFLA WFVSRVADFA RPSAFHRVYT LTWLFLVEWV FLVISTVYEN QYGLAGGYFV
     LFVFAGTFLA TWISYLELFA LPRKSDYATQ LALPSRRTSS HGSRLGTASG EDVEDGEDED
     DDGTTAEATE TTSLLRGQRT TFANYVRVTG DYLRDDDEEP RQPNLYGHEQ AWSIHLPKWV
     WVLQFLLTAP LVLIFVGPLA LLLTSALRQT GQDGSPSLFI YIAVAALTTL LFIPLLPFIH
     RYTHHIPLFL LCVFAGTLIY NLVAFPFSPA NRLKLFFIQE VDLDTGVNHA SLSGAYPFVH
     DVARRLPSTA GQNITCDLAM LRPKCSWHGI PPQVVQPAAA SKMEDWLSYN ITKSDSEPKA
     QLSISGRNTR ACKVVFDRPV LDFQVADSAY DPRFPHVSPD GTKEIRLWSR EWGHTWTVDV
     EWAADAEETD EKGPGLSGRV VCLWSDGNSA GVIPALDEVR RYAPVWAGVS KLSDGLVEGS
     RRFEV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024