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Database: UniProt
Entry: J7R218_KAZNA
LinkDB: J7R218_KAZNA
Original site: J7R218_KAZNA 
ID   J7R218_KAZNA            Unreviewed;       488 AA.
AC   J7R218;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   Name=KNAG0B04250 {ECO:0000313|EMBL:CCK68860.1};
GN   OrderedLocusNames=KNAG_0B04250 {ECO:0000313|EMBL:CCK68860.1};
OS   Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS   17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS   naganishii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK68860.1, ECO:0000313|Proteomes:UP000006310};
RN   [1] {ECO:0000313|EMBL:CCK68860.1, ECO:0000313|Proteomes:UP000006310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC   / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2] {ECO:0000313|Proteomes:UP000006310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC   / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Kazachstania naganishii.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; HE978315; CCK68860.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7R218; -.
DR   STRING; 1071383.J7R218; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   HOGENOM; CLU_019532_2_0_1; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000006310; Chromosome 2.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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:UP000006310};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   488 AA;  53918 MW;  3F499C9661B3C276 CRC64;
     MLRLHLRKMS STATNYPQEF VKFLNASHTP YHATHNIKCH LLDNGFQELS ERDSWNGKVL
     KCGKYFVTRN NSSIIGFVVG GMWAPGNPIA IVGGHTDSPT LRIKPISKRT AEGYLQVGVE
     CYGGGIWHSW FDKDLAVAGR VMVSDPETGK TVAKLVDINK PLLKIPTLAI HLDIDVNQKF
     EFNKESQLLP VAGLVKETNA TETADSVRKD YFSSIKETIE RHHEELLNLI AKELDIKSTK
     EIEDFELILY DHNEACLGGL SEEFVFSGRL DNLTSCFTSM HAMTLAADTG IESETGIRLF
     ACFDHEEIGS SSAQGADSNF LPNILERLAL LRGNEKDKDE PLTKSMNLET SAKSFFLSSD
     VAHAVHPNYA GKYESQHKPM IGSGPVIKIN ANQRYMTNSP GIVLLKKLAD KVQVPLQLFV
     VANNSPCGST IGPILASKTG IRTLDLGNPI LSMHSIRETG GAADLAYQIK LFQAFFEDYS
     LLESKIEV
//
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