ID   A0A0D2VU15_CAPO3        Unreviewed;       511 AA.
AC   A0A0D2VU15;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=5'-nucleotidase domain-containing protein {ECO:0000313|EMBL:KJE94852.1};
GN   ORFNames=CAOG_005423 {ECO:0000313|EMBL:KJE94852.1};
OS   Capsaspora owczarzaki (strain ATCC 30864).
OC   Eukaryota; Filasterea; Capsaspora.
OX   NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE94852.1, ECO:0000313|Proteomes:UP000008743};
RN   [1] {ECO:0000313|Proteomes:UP000008743}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL   Submitted (FEB-2011) 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}.
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DR   EMBL; KE346368; KJE94852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2VU15; -.
DR   EnsemblProtists; KJE94852; KJE94852; CAOG_005423.
DR   eggNOG; KOG2470; Eukaryota.
DR   InParanoid; A0A0D2VU15; -.
DR   OMA; WSRYKEA; -.
DR   PhylomeDB; A0A0D2VU15; -.
DR   Proteomes; UP000008743; 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:UP000008743}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   ACT_SITE        83
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         83
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         359
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
SQ   SEQUENCE   511 AA;  59160 MW;  56CA57888E1DDCF9 CRC64;
     MASQHNTTTP TATTTTTTAR TTMTASGIRT YTLDELRFLK AQMQQQIFAD RPLLQGPRED
     PADVFVTNEV DLSHIDAFGF DYDYTLASYN NELQALIYQL AAQSLINNNK YPAECANLQY
     DPNFAIRGLH YDVKKGLLMK IDAFQNVQLG TVYSGHRPLD DDETRRIYNG VHIPLEYMHS
     FMPQLTDLFS LPEACLLANL TQFMHDTQLP FHPEYLYMDV AHAVSEVHSR RQMHLEVIRN
     VGHYVHPSPN LENLLSTMRQ HGKKVFLLTN SSFSFVNVGM SHIVGPHWRD LFDVIVVDAL
     KPRFFNESRP FRQFDTTLNS MTWTKVSRFA RGGVYCHGNS LDFARITGWT PGRVMYVGDH
     VLSDLQDPSR KHGWRTGAII RELDEEITIL NSPEHHQSLT WLLNLQRLIK KLQHVQHHEK
     HSLLRAWQAE KNEVSAHLKD MFNPQFGSVF RTFHNPTYFA HRMSRVADLY TSDVCNFLRY
     SLDHTFYPQR MYLPHEPAPR RDDQGFFKCG P
//