ID Q6CFM9_YARLI Unreviewed; 476 AA.
AC Q6CFM9;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=YALI0_B05522g {ECO:0000313|EMBL:CAG82764.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG82764.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG82764.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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; CR382128; CAG82764.1; -; Genomic_DNA.
DR RefSeq; XP_500533.1; XM_500533.1.
DR AlphaFoldDB; Q6CFM9; -.
DR STRING; 284591.Q6CFM9; -.
DR EnsemblFungi; CAG82764; CAG82764; YALI0_B05522g.
DR GeneID; 2907621; -.
DR KEGG; yli:YALI0B05522g; -.
DR VEuPathDB; FungiDB:YALI0_B05522g; -.
DR HOGENOM; CLU_019532_2_0_1; -.
DR InParanoid; Q6CFM9; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 476 AA; 52891 MW; 9041C18F35B31481 CRC64;
MSHFKAAAND FIDFVNACPT PYHVVHDVRA RLVKNGFKEL KEKASWNIEP NGRYFVTRNE
SSIVAFTVGG KWKPGNPMAI VGAHTDSPTF RVKPVSKRSP SGNFLQIGVE CYGGGIWHSW
FDRDLSVAGR VFVKDPTTGK SQIRLVKVDK PILKIPTLAI HLDRSVMEKF EFNKEQHLTP
VLGLLEKNLN KKKEEEPVES ESDATPHQAL EQCHDPALLG LLASELDVTP EQIDNFELYL
FDTQKSCIGG LNDEFIFSPR LDNQVSSYCA TEALIKSLDT VEKDESIRVI GLFDHEEVGS
LSYQGADSNF LPAVLSRLAG APGQNDGSDV SINYQSLASS FLLSADQAHA FHPNYPTSYE
SAHRPDMNRG PVIKINGNQR YTTDGVGMVL IQKIAEKANL PMQKFVVKND SSCGSTIGPM
LASKLGLRSI DIGNPQLSMH SVRETGGSKD IYYLEKLFIE FFNNFVETDK QIVYDE
//
