ID D8SBT2_SELML Unreviewed; 515 AA.
AC D8SBT2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=5'-nucleotidase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=SELMODRAFT_113562 {ECO:0000313|EMBL:EFJ17975.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ17975.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR017434-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2};
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000256|ARBA:ARBA00009589}.
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DR EMBL; GL377611; EFJ17975.1; -; Genomic_DNA.
DR RefSeq; XP_002980790.1; XM_002980744.1.
DR AlphaFoldDB; D8SBT2; -.
DR EnsemblPlants; EFJ17975; EFJ17975; SELMODRAFT_113562.
DR Gramene; EFJ17975; EFJ17975; SELMODRAFT_113562.
DR KEGG; smo:SELMODRAFT_113562; -.
DR eggNOG; KOG2469; Eukaryota.
DR HOGENOM; CLU_017845_4_1_1; -.
DR InParanoid; D8SBT2; -.
DR OMA; EIQMPHE; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07522; HAD_cN-II; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016695; Pur_nucleotidase.
DR NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR12103:SF15; CYTOSOLIC PURINE 5'-NUCLEOTIDASE; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017434-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR017434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT COILED 365..433
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT ACT_SITE 26
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT BINDING 26
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFJ17975.1"
SQ SEQUENCE 515 AA; 60343 MW; 3D55BD89E36A264E CRC64;
LDHRTMIYCN RALNMRSISA VGFDLDYTLA QYRPETFELL AYQATAKKLV YNLGYPRQAR
ILDWKFDWKY MVRGLVLDKR RGNILKMDRH KYVKVAYHGF QELSREERTA AYGNTLSRDS
YDEPDYALID TLFSLAEAHL FAQLVELKDT DPELFPSQPE YAEIYKDVRA AVDLCHRDGT
LKQAVADDPS KYIYADEQLI SMLKMLRESG RLTFLVTNSL WDYTHVVMNF LFSADKNWLD
YFDLVITGSA KPSFFMDGNQ APLFAVDVKT GMLHNTDNGT PVPQVRQELH HTVWIWKLTF
SSYQMRQGGT VSHLHKLLAI DAGAQVLYCG DHIYGDILRS KKQLGWRTML VVPELDREVE
LLQSSRAVQK EIQRLRHSRE EIEDELQKLE WTLKYALYFK GTKEEEGPLQ EKREALQRER
DEVQKSHRTM QRKFHEQFHK TWGQLMKAGH QTSRFAHQVE RFACLYTSQV TNLSCYSPEK
CFRTAEDFMP HELRGSVVFV TKIFAYDQSP HFNDR
//
