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Database: UniProt
Entry: A0A1Y3BLU5_EURMA
LinkDB: A0A1Y3BLU5_EURMA
Original site: A0A1Y3BLU5_EURMA 
ID   A0A1Y3BLU5_EURMA        Unreviewed;       264 AA.
AC   A0A1Y3BLU5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   SubName: Full=Adenosylhomocysteinase-like protein {ECO:0000313|EMBL:OTF80974.1};
GN   ORFNames=BLA29_005690 {ECO:0000313|EMBL:OTF80974.1};
OS   Euroglyphus maynei (Mayne's house dust mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC   Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX   NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF80974.1, ECO:0000313|Proteomes:UP000194236};
RN   [1] {ECO:0000313|EMBL:OTF80974.1, ECO:0000313|Proteomes:UP000194236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF80974.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OTF80974.1};
RA   Arlian L.G., Morgan M.S., Rider S.D.;
RT   "Genome Survey of Euroglyphus maynei.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122}.
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:OTF80974.1}.
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DR   EMBL; MUJZ01015787; OTF80974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3BLU5; -.
DR   OrthoDB; 120477at2759; -.
DR   Proteomes; UP000194236; Unassembled WGS sequence.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   SMART; SM00996; AdoHcyase; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194236}.
FT   DOMAIN          25..186
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
SQ   SEQUENCE   264 AA;  29187 MW;  BCCD91CC9944ED99 CRC64;
     MLKNGELKVP SFNVNDSVTK SKFDNLYGCR ESLVDGIKRA TDIMLAGKVA VVAGFGDVGK
     GSARSLLGFG CKVIITEIDP INALQAAMEG YEVTLLEETL SRASIFVTTT GCKDIIRGEH
     FMKMKDNSIV CNIGHFDCEI DVKWLEDNAI EKVNIKPQVD RYTLSNGRHI ILLASGRLVN
     LGCATGHPSF VMSNSFTNQV LAQMELFNKK YDLGIYTLPK ILDEEVAALH LPHLGVKLTK
     LTDDQANYLG INKNGPFKPE HYRY
//
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