ID C4R6N8_KOMPG Unreviewed; 504 AA.
AC C4R6N8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN OrderedLocusNames=PAS_chr4_0913 {ECO:0000313|EMBL:CAY71263.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY71263.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY71263.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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; FN392322; CAY71263.1; -; Genomic_DNA.
DR RefSeq; XP_002493442.1; XM_002493397.1.
DR AlphaFoldDB; C4R6N8; -.
DR SMR; C4R6N8; -.
DR STRING; 644223.C4R6N8; -.
DR EnsemblFungi; CAY71263; CAY71263; PAS_chr4_0913.
DR GeneID; 8201129; -.
DR KEGG; ppa:PAS_chr4_0913; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_2_0_1; -.
DR InParanoid; C4R6N8; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000000314; Chromosome 4.
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:UP000000314};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 504 AA; 55944 MW; CB3BDC0F43253E2E CRC64;
MPNLPSSLNK MTAQACLRLY PLTLDFITFL NNSPTPYHAV DSVKSKLVES GFNELSERVN
WAGKVKKNGA YFVTRNNSSI IAFTVGGHWQ PGNGVSIVGA HTDSPTLRIK PISHSTKEGF
NQVGIETYGG GLWHTWFDRD LGVAGRVFIE EEESGNIVSK LVKIDKPVLR IPTLAIHLTK
ERAKFEFNKE TQFHPISSLE NSSEKEKNKD EEHDACAGED LTTEEFKSIQ SVVERHNKQL
LDLVAADLDC SISQIVDFEL ILFDHNKPVL GGLNEEFVFS GRLDNLTSCF CATEALINAS
KDTNRLDLDT NIQLISLFDH EEIGSVSAQG ADSSFLPDIL QRITRLTGNE VSTDLEGQPN
SFFLESMAKS FLLSSDMAHG VHPNYGEVYE KLNRPRINEG PVIKINANQR YSTNSPGIVL
LKKIGELGKV PLQLFVVRND SPCGSTIGPM LSAKLGLRTL DLGNPQLSMH SIRETGGARD
VKKLVDLFES YFENYYTLEP KIKV
//