ID C5LJI4_PERM5 Unreviewed; 537 AA.
AC C5LJI4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=Pmar_PMAR023225 {ECO:0000313|EMBL:EER03113.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER03113.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG682453; EER03113.1; -; Genomic_DNA.
DR RefSeq; XP_002771297.1; XM_002771251.1.
DR AlphaFoldDB; C5LJI4; -.
DR EnsemblProtists; EER03113; EER03113; Pmar_PMAR023225.
DR GeneID; 9051856; -.
DR InParanoid; C5LJI4; -.
DR OMA; EYANIHT; -.
DR OrthoDB; 199847at2759; -.
DR Proteomes; UP000007800; 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 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; 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 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 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:UP000007800}.
FT DOMAIN 156..511
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 119..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 60237 MW; C9DF0EC4CE32A102 CRC64;
MMLIELGAHT PRDPAQFMCD YIRANLPSER YGAVEDNDYA NSCHQADEFM HHDDDDEEEE
DLVPPAPPPQ LAISRHVSHR LSHDLTSTAI RSIVLRRVSR QLEKENPSVH AFVQQWMRPG
MGGGRGSSTS SGRGSISGAS RRASDSVAYH EARLTAKMLE VPVMEALELP DLLSWNIKLF
TLDRSELVRR AYSVFDRWSF VGEGKLVEAS RLWGFINLIA NDYHADNPYH NFYHAYQVMS
CVGYVMFNAG CSVRPGGPAG GPRDVICTPL EEFSLLIAAL CHDVNHPGFN NDYFIKGRKH
LAVRYNDSAV LENMHAARAF ELLLGGAVDF TATWPAAAAA DETGEPSDYE VFRQTVISVI
LATDMKAHFD ITIKLQELLL DRNDGSKRAA REWVDGALAE TRPTLLKGIV HAADISNPLM
PYDEYYEWSY RVVSEYYHQA EAERLEGLPF APFMAHRPDD AVELAKLQVG FINFVVSPLW
NTLDGLLDGL HDRVEVMETN LQRMKEVEDR EQGRRDSCAG HAQLDDITSE EEAVVAD
//
