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Database: UniProt
Entry: A0A0L8ICS0_OCTBM
LinkDB: A0A0L8ICS0_OCTBM
Original site: A0A0L8ICS0_OCTBM 
ID   A0A0L8ICS0_OCTBM        Unreviewed;       215 AA.
AC   A0A0L8ICS0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643};
DE            EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
GN   ORFNames=OCBIM_22022744mg {ECO:0000313|EMBL:KOF98825.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF98825.1};
RN   [1] {ECO:0000313|EMBL:KOF98825.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF98825.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF98825.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000815};
CC   -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00008389}.
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DR   EMBL; KQ416074; KOF98825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L8ICS0; -.
DR   EnsemblMetazoa; Ocbimv22022743m; Ocbimv22022743m.p; Ocbimv22022744m.g.
DR   EnsemblMetazoa; XM_014924015.1; XP_014779501.1; LOC106875755.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 1.10.150.340; Pyrimidine 5'-nucleotidase (UMPH-1), N-terminal domain; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR   PANTHER; PTHR13045; 5'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR13045:SF0; CYTOSOLIC 5'-NUCLEOTIDASE 3A; 1.
DR   Pfam; PF05822; UMPH-1; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   215 AA;  24475 MW;  C78820E5C2C5DD79 CRC64;
     MAAKLRDIYA PIEFDPHIET EKKAPKMEEW WTQVHELLGT LNISKSLINK MVAQSSVRLR
     IGCDELFKSL DKWNVPVLII SAGLGDILSE ILTQQSAVYS NMKIVSNFMK FKEDKMVGFY
     DEIIHTFNKN KCAIHKSGYF NNQRSNIILL GDSVGDLHLA DGAKDSSTIL KIGYLNERVD
     ESLEIYKNAF DIVLVKTENV DLMNALMKRM TDNKV
//
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