ID A0A212EYH5_DANPL Unreviewed; 721 AA.
AC A0A212EYH5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=AMP deaminase {ECO:0000256|PIRNR:PIRNR001251};
DE EC=3.5.4.6 {ECO:0000256|PIRNR:PIRNR001251};
GN ORFNames=KGM_212863 {ECO:0000313|EMBL:OWR46546.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR46546.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR46546.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR46546.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6;
CC Evidence={ECO:0000256|PIRNR:PIRNR001251};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR001251};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676,
CC ECO:0000256|PIRNR:PIRNR001251}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWR46546.1}.
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DR EMBL; AGBW02011505; OWR46546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212EYH5; -.
DR STRING; 278856.A0A212EYH5; -.
DR KEGG; dpl:KGM_212863; -.
DR eggNOG; KOG1096; Eukaryota.
DR InParanoid; A0A212EYH5; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032264; P:IMP salvage; IEA:InterPro.
DR Gene3D; 4.10.800.20; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01429; AMP_deaminase; 1.
DR PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001251};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR001251};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 84466 MW; F642777F34D1C64F CRC64;
MFGTSKDVKN WNRERSETRR NQWGSTRMKI RGPGDGPRRS VPFQRISITG IHITGVPLDD
LKRSASFLIN ALSLRKNYME ISNQSFPDDL AYYLTHNEGP PYFNDNKEKP QNNEAYLRFH
PDLDEKYCDL TTCSSEELLN FQQIDRHNLR SETDRRIQDS QEDLQDEGPG DEDPWNCPTP
PDRHLVYRWK HGVVQVYKNK EDAYENKKMN YRYLSFKQYV EDMSLLTDMI SDGPLKSFCY
RRLSYLSSKF KMHVLLNELH ELALQKAVPH RDFYNVRKVD THIHAASCMN QKHLLRFIKR
TLRAQPGQVV ALRDGLPITL KAVFEEMQLD AYDLNVDILD VHADRNTFHR FDRFNAKYNP
VGESRLREVF LKTDNYMNGA YFADILKEVI SDLEDSKYTY AEPRISVYCK RASEWGELAA
WALRRRVYSS HVRWLVQVPR LYDVYRINNL LKNFQEFLNN LFDPLFKVSI DPHSNPELHK
FLTHVIGFDS VDDESKPENP NLTENMKTPE EWDDEENPPY AYYLYYMYAN IVMLNQLRKE
QGLNTFVLRP HCGEAGPPAH LCAAFLLAEN ISHGLILRKV PALQYIYYLS QIFIAMSPLS
NNSLFLRYHR NPLPDYFSRG LRVTLSTDDP LQFHYTKEPL MEEYGIAAQA WKFSSCDMCE
LARNSVLMSG FPREMKQRWV GLTYERAGAA GNDIARTNVP DLRLTYRLET LRAELNNLFG
V
//