ID K0S1L0_THAOC Unreviewed; 531 AA.
AC K0S1L0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=THAOC_19743 {ECO:0000313|EMBL:EJK59978.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK59978.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK59978.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK59978.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
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}.
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:EJK59978.1}.
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DR EMBL; AGNL01021882; EJK59978.1; -; Genomic_DNA.
DR AlphaFoldDB; K0S1L0; -.
DR EnsemblProtists; EJK59978; EJK59978; THAOC_19743.
DR eggNOG; KOG3689; Eukaryota.
DR OMA; NCREWEL; -.
DR Proteomes; UP000266841; Unassembled WGS sequence.
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:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR PANTHER; PTHR11347:SF198; CAMP-SPECIFIC 3',5'-CAMP PHOSPHODIESTERASE 4; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000266841}.
FT DOMAIN 155..467
FT /note="PDEase"
FT /evidence="ECO:0000259|Pfam:PF00233"
FT REGION 16..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 59899 MW; CC1762BE02D46326 CRC64;
MAQNLSDFSM EKLVLPSNGG SAGRRRSNSW TLHDPTGFDD IHDEDGPPCP LASKLTNQRW
HEIGNSPDQS ICSTSNFDVM VEQLAAVMGM HLLELLLYWL RPKDDDGTKK EVITDVLEYL
EIDPNIGNYV LTTSIKNSIR DYVAEIGKLY KDVGFHSLEH AIHVTMSMNK LLSMVSDSHH
QVSKSFENDG EGHNCGSPRR VAQSYGIDDP RIKFAMFFSA LIHDVGHTGV PNSVLVEEED
ELAILHNDVS VAEQNSLNIA FSLLHAPQFA RLKHCIGPNP TQRKFFRKRV IASVMVTDIS
DQERIQIVKS RWETAFPPVE DEEKNQTERR QARAAAPTPP EAPRTELRQS RLRRRATMHS
SEAVAEGFLA RSRRLGIRTS MDFSGNLIDA YGTNNQLQQH AVLETMMNVA DVAHTMQSFN
TFVKWNRRLF RELHAARSAE RLPFDPSARW YENQIGFFNH YILPLAGKMK SCGVLGTTGD
VFELFAAENL KRWKEEGEAI SEEIIRSETS MMVGPNPLRG PVQRRGGRTT S
//
