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Database: UniProt
Entry: A0A162SSY8_9CRUS
LinkDB: A0A162SSY8_9CRUS
Original site: A0A162SSY8_9CRUS 
ID   A0A162SSY8_9CRUS        Unreviewed;       147 AA.
AC   A0A162SSY8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Adenosine 5'-monophosphoramidase HINT3 {ECO:0000256|ARBA:ARBA00039802};
DE   AltName: Full=Histidine triad nucleotide-binding protein 3 {ECO:0000256|ARBA:ARBA00042361};
GN   ORFNames=APZ42_011556 {ECO:0000313|EMBL:KZS21601.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS21601.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS21601.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS21601.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS21601.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+);
CC         Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57890, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00024472};
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:KZS21601.1}.
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DR   EMBL; LRGB01000024; KZS21601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162SSY8; -.
DR   STRING; 35525.A0A162SSY8; -.
DR   EnsemblMetazoa; XM_032921747.2; XP_032777638.1; LOC116916494.
DR   OrthoDB; 2782915at2759; -.
DR   Proteomes; UP000076858; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.428.10; HIT-like; 1.
DR   InterPro; IPR001310; Histidine_triad_HIT.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   PANTHER; PTHR12486:SF5; ADENOSINE 5'-MONOPHOSPHORAMIDASE HINT3; 1.
DR   PANTHER; PTHR12486; APRATAXIN-RELATED; 1.
DR   Pfam; PF11969; DcpS_C; 1.
DR   PRINTS; PR00332; HISTRIAD.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT   DOMAIN          11..122
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   MOTIF           102..106
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601310-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        104
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601310-1"
SQ   SEQUENCE   147 AA;  16940 MW;  9AAE3AB6426AF74B CRC64;
     MSVVQQSLKC VFCQICQGLA PASIVHQDLK YLAFRDIKPA SKNHLLIIPR EHITDVKSLT
     VETVKIVEEM VEIGQQLVKE HLGTLVDYRM GFHWPPFNSV KHLHLHVIFP EQSMSFIGRQ
     VFRPGTFYFA TPETTIDWIK KHRSSSL
//
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