(data stored in SCRATCH zone)

SWISSPROT: Q4WDH7_ASPFU

ID   Q4WDH7_ASPFU            Unreviewed;       262 AA.
AC   Q4WDH7;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
DE            EC=3.4.25.1 {ECO:0000256|RuleBase:RU000551};
GN   ORFNames=AFUA_6G04790 {ECO:0000313|EMBL:EAL85561.1};
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:EAL85561.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85561.1, 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         ECO:0000256|RuleBase:RU000551};
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. {ECO:0000256|RuleBase:RU000551}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000551}.
CC       Nucleus {ECO:0000256|RuleBase:RU000551, ECO:0000256|SAAS:SAAS00594407}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00808, ECO:0000256|RuleBase:RU000551}.
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:EAL85561.1}.
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DR   EMBL; AAHF01000012; EAL85561.1; -; Genomic_DNA.
DR   RefSeq; XP_747599.1; XM_742506.1.
DR   STRING; 746128.CADAFUBP00009087; -.
DR   MEROPS; T01.976; -.
DR   EnsemblFungi; EAL85561; EAL85561; AFUA_6G04790.
DR   GeneID; 3505183; -.
DR   KEGG; afm:AFUA_6G04790; -.
DR   EuPathDB; FungiDB:Afu6g04790; -.
DR   HOGENOM; HOG000091080; -.
DR   InParanoid; Q4WDH7; -.
DR   KO; K02725; -.
DR   OMA; TQEMVAC; -.
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   CDD; cd03749; proteasome_alpha_type_1; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR035144; Proteasome_alpha1.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF12; PTHR11599:SF12; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDH7.
DR   SWISS-2DPAGE; Q4WDH7.
KW   Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551, ECO:0000313|EMBL:EAL85561.1};
KW   Nucleus {ECO:0000256|RuleBase:RU000551, ECO:0000256|SAAS:SAAS00136223};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551};
KW   Proteasome {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551, ECO:0000313|EMBL:EAL85561.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Threonine protease {ECO:0000256|PROSITE-ProRule:PRU00808,
KW   ECO:0000256|RuleBase:RU000551}.
FT   DOMAIN          6..28
FT                   /note="PROTEASOME_ALPHA_1"
FT                   /evidence="ECO:0000259|PROSITE:PS00388"
SQ   SEQUENCE   262 AA;  28755 MW;  12A1CB6ADB3F42E4 CRC64;
     MFRNNYDNDA VTFSPQGRIF QVEYAQEAVK QGSVVVGLVN KTHAVLVGLK RNAEELSSYQ
     KKIIEVDSHM GIAIAGLASD ARVLSNYMKQ QCLSSRMTYG RPLPVDRIVT QIGDRAQTNT
     QQYGKRPYGV GLLVAGVDEA GPHLFEFQPS GMTQEMLACA IGARSQMART YLERNLDKFA
     DCSREELISH GLRALKETLS HDKELTVDNT SVGVVGLAGE GAQGKIETFK LYDGQSISPL
     LEALEQTDSG ETKEEESMEV DS
//

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