ID A0A026X1F4_OOCBI Unreviewed; 542 AA.
AC A0A026X1F4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=DMN91_008287 {ECO:0000313|EMBL:RLU19730.1}, X777_05442
GN {ECO:0000313|EMBL:EZA62115.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA62115.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA62115.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
RN [2] {ECO:0000313|EMBL:RLU19730.1, ECO:0000313|Proteomes:UP000279307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU19730.1};
RX PubMed=30249741; DOI=10.1101/gr.237123.118;
RA McKenzie S.K., Kronauer D.J.C.;
RT "The genomic architecture and molecular evolution of ant odorant
RT receptors.";
RL Genome Res. 28:1757-1765(2018).
RN [3] {ECO:0000313|EMBL:RLU19730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU19730.1};
RA Mckenzie S.K., Kronauer D.J.C.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU363067};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
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DR EMBL; KK107031; EZA62115.1; -; Genomic_DNA.
DR EMBL; QOIP01000008; RLU19730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026X1F4; -.
DR STRING; 2015173.A0A026X1F4; -.
DR EnsemblMetazoa; XM_020031744.2; XP_019887303.1; LOC105279816.
DR OMA; TFTIMEK; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR Proteomes; UP000279307; Chromosome 8.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR040844; PDE4_UCR.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR PANTHER; PTHR11347:SF219; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE, ISOFORM I; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF18100; PDE4_UCR; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|ARBA:ARBA00023149};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT DOMAIN 139..468
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 461..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 215..219
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 256
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 373
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 424
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 542 AA; 60341 MW; 8ABC7F3FFF99E662 CRC64;
MVRQTTNGEV ETGNVDESAR YFNYLRTLAD LTAIASIMTV QFKRMLNKEL SHFSESSKSG
NQISEYICST FLDKQQELDL PSLRIEDAVA AAGSADARAA KKKDRAQRGP AAMSHISGVK
RPLTHTNSFT GERVPLHGVE TPHEEELGKL LSDIDKWGID IFRIGELSSN RPLTCVAYTA
FQSRDLLKSL AIPPKTFVTF MMTLEDHYVK DNPFHNSLHA ADVTQSTHTL LNTPALESVF
TPLEITAALF AATIHDVDHP GLTNQFLINS SSELALMYND ESVLENHHLA VAFKLLQNEG
CDIFVNMTKK QRQTLRKMVI DMVLSTDMSK HMSLLADLKT MVETKKVAGS GVLLLDNYTD
RIQVLENLVH CADLSNPTKP LPLYRRWVGL LMEEFFLQGD REREQNMDIS PMCDRHSATI
EKSQVGFIDY IVHPLWETWA DLVHPDAQEI LDTLEENRDW YQSMIPPSPP SDDQQQSTNE
NQQQQQSDSR IHFEVTLEEG DESGEAVEGG DSGGGGGGGE STTFSSEDAG GETEENATEA
GM
//
