ID A0A1I8I4X2_9PLAT Unreviewed; 480 AA.
AC A0A1I8I4X2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00015118};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=BOX15_Mlig019903g2 {ECO:0000313|EMBL:PAA91477.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0009911-snap-gene-0.3-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0009911-snap-gene-0.3-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:PAA91477.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA91477.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA91477.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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 -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC {ECO:0000256|ARBA:ARBA00011395}.
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; NIVC01000085; PAA91477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I8I4X2; -.
DR STRING; 282301.A0A1I8I4X2; -.
DR WBParaSite; maker-uti_cns_0009911-snap-gene-0.3-mRNA-1; maker-uti_cns_0009911-snap-gene-0.3-mRNA-1; maker-uti_cns_0009911-snap-gene-0.3.
DR Proteomes; UP000095280; Unplaced.
DR Proteomes; UP000215902; Unassembled WGS sequence.
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:UP000215902};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 480 AA; 51278 MW; C4C98EF70A52F22B CRC64;
MSTSSAPSVA AAAAAAWKTA DLSQQLCEFV NRSPSPFHAV AESRRMLEAA GFAQLREDQS
WSLRPNQKGF VTRNGSTIFA FATGGKWKPG NGFSIVGAHT DSPCLRLKPV SLRESAGELL
QCGVETYGGG LWYSWFDRDL TVAGRVIVRS GSGGSSDSSR LTERLVNLEA PVFKVPSLAI
HLNRTVNDEG FAPNKENHLA PILCRKLAAE ASGAGTGSDT SAPPQRHPVG LLARVAEKLG
CQPADILDWD LYLADTQPAA VTGLNGDFVS SPRLDNLLSC YSALTALIEA PGLESDPNCR
VVCLYDHEEI GSESAQGAGS ALTLHFLRRL SQGGEFETAV PKSLLVSADV AHAVHPNYEE
KHERKHRPSL FGGVVIKENA NQRYATNCLT SSLLRECLRL SDPAAQLQDF VIRQDMACGS
TIGPILAAKV GLPTIDVGSP IFGMHSIRET GAAAAPGQGV QLFSAFFKHF PALREAMETQ
//