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Database: UniProt
Entry: W1NDQ7_AMBTC
LinkDB: W1NDQ7_AMBTC
Original site: W1NDQ7_AMBTC 
ID   W1NDQ7_AMBTC            Unreviewed;       344 AA.
AC   W1NDQ7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Aspartyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMTR_s00138p00074300 {ECO:0000313|EMBL:ERM93847.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM93847.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KI397561; ERM93847.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1NDQ7; -.
DR   STRING; 13333.W1NDQ7; -.
DR   MEROPS; M18.A01; -.
DR   EnsemblPlants; ERM93847; ERM93847; AMTR_s00138p00074300.
DR   Gramene; ERM93847; ERM93847; AMTR_s00138p00074300.
DR   eggNOG; KOG2596; Eukaryota.
DR   HOGENOM; CLU_019532_1_1_1; -.
DR   OMA; IREIACT; -.
DR   Proteomes; UP000017836; 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   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF16; ASPARTYL AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
FT   REGION          55..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  37540 MW;  F7F645AD6CC679BC CRC64;
     MFISGIEGIE ASKQGYTLSL SSSIQKLLVL AFVHDVQGIG IRRLAHNASE LLKVPPESDA
     IEGRPNTDGN EADEKKNSNK QKHHPLLLML LASEACCEPD EICDFELQAC DTQPSIIGGA
     AKEFMFSGRL DNLCMSFCSL RALFDSTAEG SLANETGVRM VALFDHEEVG SDSAQGAGSP
     IILDALARIT NSFCSSGSKV LEKAVQRSFL VSADMAHALH PNYMDKHEEN HQPRLHGGLV
     IKHNANQRYA SNSVTSFIFR EIAKQHKLPV QEFVVRNDMA CGSTIGPILA SGVGIRTVDV
     GAPQLSMHSI REMCSVDDVK HSYEHFKAFF HEFAQLDAKI SVDV
//
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