(data stored in SCRATCH zone)

SWISSPROT: C5DDA1_LACTC

ID   C5DDA1_LACTC            Unreviewed;       233 AA.
AC   C5DDA1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=Proteasome endopeptidase complex {ECO:0000256|PROSITE-ProRule:PRU00808};
DE            EC=3.4.25.1 {ECO:0000256|PROSITE-ProRule:PRU00808};
GN   OrderedLocusNames=KLTH0B09504g {ECO:0000313|EMBL:CAR21762.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21762.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21762.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00594407}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00808}.
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DR   EMBL; CU928166; CAR21762.1; -; Genomic_DNA.
DR   RefSeq; XP_002552200.1; XM_002552154.1.
DR   STRING; 381046.XP_002552200.1; -.
DR   EnsemblFungi; CAR21762; CAR21762; KLTH0B09504g.
DR   GeneID; 8291043; -.
DR   KEGG; lth:KLTH0B09504g; -.
DR   HOGENOM; HOG000091080; -.
DR   InParanoid; C5DDA1; -.
DR   KO; K02725; -.
DR   OMA; KYMRNEC; -.
DR   OrthoDB; 1222564at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; C5DDA1.
DR   SWISS-2DPAGE; C5DDA1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Nucleus {ECO:0000256|SAAS:SAAS00136223};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Proteasome {ECO:0000256|PROSITE-ProRule:PRU00808};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Threonine protease {ECO:0000256|PROSITE-ProRule:PRU00808}.
FT   DOMAIN        6     28       PROTEASOME_ALPHA_1. {ECO:0000259|PROSITE:
FT                                PS00388}.
SQ   SEQUENCE   233 AA;  25636 MW;  BD1C3233061D8CAC CRC64;
     MFRNNYDGDT VTFSPTGRLF QVEYALEAIK QGSVTVGVRS KKFAVLVALK RNADELSSYQ
     KKIIKCDEHL GLSLAGLAPD GRVLSNFLRQ QCNYSSLVYN RKLSLEKAGN LLSDKAQKNT
     QSYGGRPYGV GLLLAGYDNS GPHLLEFQPS GNTLELYGSA IGARSQGAKT YLERTLQDYL
     ELDDADDLIR VAVEALRQCL KDEVLSTKNL SIAVVGQDKP FTILDDEAVS PYL
//

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