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Database: UniProt
Entry: A0A1X7UWM4_AMPQE
LinkDB: A0A1X7UWM4_AMPQE
Original site: A0A1X7UWM4_AMPQE 
ID   A0A1X7UWM4_AMPQE        Unreviewed;       565 AA.
AC   A0A1X7UWM4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=S-adenosyl-L-homocysteine hydrolase NAD binding domain-containing protein {ECO:0000259|SMART:SM00997};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.31929_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20686567; DOI=10.1038/nature09201;
RA   Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA   Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA   Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA   Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA   Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA   Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The Amphimedon queenslandica genome and the evolution of animal
RT   complexity.";
RL   Nature 466:720-726(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.31929_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2017) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A1X7UWM4; -.
DR   STRING; 400682.A0A1X7UWM4; -.
DR   EnsemblMetazoa; Aqu2.1.31929_001; Aqu2.1.31929_001; Aqu2.1.31929.
DR   eggNOG; KOG1370; Eukaryota.
DR   InParanoid; A0A1X7UWM4; -.
DR   Proteomes; UP000007879; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00401; SAHH; 1.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 2.
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.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        519..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          323..504
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  61412 MW;  30CEB03D022F6E4E CRC64;
     MSSNKSDTSS ISPVPLKGTG TSPEPGSVSS SLPGGKNGVP HIPLGPLASV KLDPTDHHTI
     SPTAPSHKAA RPLPVEETSK PSPRRNRKMS RLRFTSLSSS ASIEEDSSGS YSDSYSSDDE
     SNPRDQQLSN SNGFRDFCIK DINLASYGRK EIEIAEKEMP GLMLLRKKTT TTGDRPLKGA
     CIVGCTHITA QAAVLIETLV SCGASVRWCA CNVHSTQDEV AAALAEAGYP IFAWRGESED
     DFWWCIDKCL DAPKWKCDMI LDDGGDATCL MLQKYPGAAK YMKGVVEESI TGIHRLYQLS
     KEGKLPMPAI NIHDSVVKTK FDNLYSCRES VIDSLKRTMD IMFGGKIICV CGYGEVSSNE
     FKMKMINFIN FIINVLQVGK GCCSALKGLG AICFVTEVDP ICALQACMDG FRVVRLEDVA
     STVDIVITAT GTKHVVRREH MNKLKDGCIL ANMGHTTNEI DVSSLKDLNK EKIRPHVSHI
     IWPDGKAIIL LADGKLVNQV CSRVPSLVFS ITSATQVNIL VNILVNILVN ILVNILVNIL
     VNILVNILVN ILVNILVNIL VNILG
//
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