ID A0A1Q3D0D3_CEPFO Unreviewed; 535 AA.
AC A0A1Q3D0D3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=5_nucleotid domain-containing protein {ECO:0000313|EMBL:GAV85950.1};
GN ORFNames=CFOL_v3_29384 {ECO:0000313|EMBL:GAV85950.1};
OS Cephalotus follicularis (Albany pitcher plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV85950.1, ECO:0000313|Proteomes:UP000187406};
RN [1] {ECO:0000313|Proteomes:UP000187406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA Fukushima K., Hasebe M., Fang X.;
RT "Cephalotus genome sequencing.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:GAV85950.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDDD01003737; GAV85950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3D0D3; -.
DR STRING; 3775.A0A1Q3D0D3; -.
DR InParanoid; A0A1Q3D0D3; -.
DR OrthoDB; 3626840at2759; -.
DR Proteomes; UP000187406; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 2.
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 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:UP000187406}.
FT ACT_SITE 63
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT ACT_SITE 65
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT BINDING 63
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT BINDING 65
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
SQ SEQUENCE 535 AA; 62194 MW; C15669058730C2C1 CRC64;
MDRSVGTVFG DSSSHIQHVD CIDDVQKTCI WSSPEGGQKI DIRKQIFCNR SLNMKNIIAV
GFDMDYTLAQ YKPETFESLA YEGTIRKLVY DLGYPQELLE WSFDWKYMVR GLVLDKKRGN
ILKMDRHKYV KVAYHGFREM SKENKVGTYG STLIRDSFDE PDYALIDTLF SLAEAYLFAQ
LVDFKDKNPG KVPRDADYAH MYKDVRAAVD LCHRDGTLKR MVAKDPKKYI NDDTCIVPML
KLLRDSGRST FLVTNSLWDY TNVVMNFLCG SRTLVDCNFD WLQYFDVVIT GSAKPSFFHE
DNRANLFEVE PESGMLLNTD NGTPMPQVGN MSPTLSLKGN KTFRVFQGGS VGHLHKLLSI
ESSSQVLYVG DHIYGDILRS KKVLGWRTML VVPELERELE LLWELRDTRK QLRLLRNERD
LIEDQIHHLK WSLKFDTLNI DENQKISSAI VNLESQRDQV RITHQQAQRD CHRKFHNVWG
QLMKTGYQNS RFAHQVERFA CLYTSQVSNL GFYSPDKYYR PNEDFMPHEF HILPL
//
