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}.
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; 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
//