(data stored in SCRATCH zone)

SWISSPROT: Q4WNH5_ASPFU

ID   Q4WNH5_ASPFU            Unreviewed;       278 AA.
AC   Q4WNH5;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=Proteasome endopeptidase complex {ECO:0000256|PROSITE-ProRule:PRU00808};
DE            EC=3.4.25.1 {ECO:0000256|PROSITE-ProRule:PRU00808};
GN   ORFNames=AFUA_6G06350 {ECO:0000313|EMBL:EAL88489.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88489.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL88489.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000256|PROSITE-ProRule:PRU00808};
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00808}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL88489.1}.
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DR   EMBL; AAHF01000006; EAL88489.1; -; Genomic_DNA.
DR   RefSeq; XP_750527.1; XM_745434.1.
DR   STRING; 746128.CADAFUBP00007035; -.
DR   PRIDE; Q4WNH5; -.
DR   EnsemblFungi; EAL88489; EAL88489; AFUA_6G06350.
DR   GeneID; 3508843; -.
DR   KEGG; afm:AFUA_6G06350; -.
DR   EuPathDB; FungiDB:Afu6g06350; -.
DR   HOGENOM; HOG000091086; -.
DR   InParanoid; Q4WNH5; -.
DR   KO; K02727; -.
DR   OMA; SMYMHAY; -.
DR   OrthoDB; 1222564at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR037555; Proteasome_alpha_3.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF10; PTHR11599:SF10; 1.
DR   Pfam; PF00227; Proteasome; 2.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WNH5.
DR   SWISS-2DPAGE; Q4WNH5.
KW   Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Proteasome {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000313|EMBL:EAL88489.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Threonine protease {ECO:0000256|PROSITE-ProRule:PRU00808}.
FT   REGION          227..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..256
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   278 AA;  29727 MW;  03A43D58D2193D97 CRC64;
     MLQVEYAVKA VENGGTAIGI RCKDGVVLAV EKIVTSKLLK PGANKRIATV DRHVGIVSAG
     LVPDGRHFVS RARDEASSWR SVYKGPIPIS ALANRLGSYV QAYTLYSSVR PFGVTAIVGG
     WDSETELAVD GQVGTGPASG SGGKTSDAKV GGPGLYMIEP SGLYWGYYGA ATGKGRQAAK
     AELEKLDLAS EKLTLLEAVR EAARIIYVAH EDSKDKEFEL EMSWISSLDG PTKGKHEAVP
     RELLEEAEKA AKRALEGEDE DEEETTKNDG NGGERMEE
//

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