ID   A0A068S6M1_9FUNG        Unreviewed;       564 AA.
AC   A0A068S6M1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=5-nucleotidase domain-containing protein 3 {ECO:0000313|EMBL:CDH56916.1};
GN   ORFNames=LCOR_07918.1 {ECO:0000313|EMBL:CDH56916.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH56916.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH56916.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) 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:CDH56916.1}.
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DR   EMBL; CBTN010000042; CDH56916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068S6M1; -.
DR   STRING; 1263082.A0A068S6M1; -.
DR   VEuPathDB; FungiDB:LCOR_07918.1; -.
DR   OrthoDB; 3626840at2759; -.
DR   Proteomes; UP000027586; 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   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:SF39; FI20020P1; 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:UP000027586}.
FT   ACT_SITE        112
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         114
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         398
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
SQ   SEQUENCE   564 AA;  65124 MW;  172A2541F9DD54E5 CRC64;
     MLRLQSHRLT PLVTLSTLRP FHSTPCHHHA TTIVDSLRSN FNAKKQEHIQ LAKRDRATIL
     SVTGSCDGLT TRKNYGQGGP SADVYGLGIT SPTEVFINNE LNLRHVNVYG FDYDYTLANY
     TDNLSKAIYD ILKDILVDMM RYPKHIKDLQ FDPTFAIRGL HFDVNKGWLM KIDNYANIQL
     NTVHLGRMPV NDPEEVIQHF GGTHISPDYL ANNMFQLSDL FSVPQACLLS DILQYFKEHN
     ISFHPRYLSD DVGQAARILH TGSHMDGEFG VGGRLHMAVI DDIAQYLEKS PKLVGFIERL
     RKHGKKTFLL TNSSLPFIDQ GMKYLTSNSD WRDLFDAVIV SARKPEFYRS RRPFRRAQEP
     TWDSVDVFEP GEVYQGGNLT DFTRLTGWSG QNVLYFGDHV FSDLIDPIVE QGWRTGAIIH
     ELDAEIQTRN TASYRHTLAW LIRIENLINE AQTYYGHEET DGLYSLINEW REQRRQARHE
     LRNVFNSAFG SVFRTYHNPT YFAGKIRQFA DIYMSSVTNL DHISMDYVFY PDRTYLPHER
     LVESLIDTGR IKELLRSSRH MMIV
//