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Database: UniProt
Entry: Q6CQM8_KLULA
LinkDB: Q6CQM8_KLULA
Original site: Q6CQM8_KLULA 
ID   Q6CQM8_KLULA            Unreviewed;       511 AA.
AC   Q6CQM8;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 119.
DE   SubName: Full=KLLA0D15917p {ECO:0000313|EMBL:CAH00857.1};
GN   ORFNames=KLLA0_D15917g {ECO:0000313|EMBL:CAH00857.1};
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590 {ECO:0000313|EMBL:CAH00857.1, ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAH00857.1, ECO:0000313|Proteomes:UP000000598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37 {ECO:0000313|Proteomes:UP000000598};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; CR382124; CAH00857.1; -; Genomic_DNA.
DR   RefSeq; XP_453761.1; XM_453761.1.
DR   AlphaFoldDB; Q6CQM8; -.
DR   STRING; 284590.Q6CQM8; -.
DR   PaxDb; 284590-Q6CQM8; -.
DR   GeneID; 2892957; -.
DR   KEGG; kla:KLLA0_D15917g; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_9_1_1; -.
DR   InParanoid; Q6CQM8; -.
DR   OMA; GIGYKTN; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000598};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..511
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004272841"
FT   DOMAIN          60..404
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          417..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        333..369
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   511 AA;  55775 MW;  A2B5E2B3605A27F9 CRC64;
     MILPSLTILC LLTSLINCRQ IEFDHDSKVI QLQLLKPADR SLQKRSKSFE SKLNPQDYFY
     TVELGVGTPS QKINCIFDTG SSDLWVPAKS NPFCLGNKLD TNGTNEFHGT EITPILDCDK
     IGVFDPGSSY SLSATGYNFS TQYFDGSYSD GFWVVDDISI ADQQVPDLQF AVANISSAPS
     GVLGVGLPRL EAVRGYDGAP NANYDNFPQT LKSNRLINRV LYSLYFDSGD LESGTVLFGG
     IDEKKYDGVL YTLPLVNIYE QIDEPAAFDI TLQGLGIRSE SNCKDTVIAH KKAPALLDSG
     STIMGAPQEA LESIAQELGA AFSESDGLYV LDCPASNDDR TFYFDFGELK LKVPIHDLLY
     LPESGQNYCG LAIIASGEEW ILGDLVLKSA YVVYDLDNLE ISIAQVKTTS GSRIQTVSAT
     GSLPQTRKSN STPWSLSGST NSSTDSVFDK PLPKKCQKSP SKTCPAKKKG NKREVLINIH
     DNLIMLENSG SSSLRPSYLL CALLVLFHSL L
//
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