ID W7ANT4_PLAVN Unreviewed; 794 AA.
AC W7ANT4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=PVPCR_1303950 {ECO:0000313|EMBL:CAD2111859.1}, YYG_04398
GN {ECO:0000313|EMBL:EUD70429.1};
OS Plasmodium vinckei petteri.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=138298 {ECO:0000313|EMBL:EUD70429.1, ECO:0000313|Proteomes:UP000030659};
RN [1] {ECO:0000313|EMBL:EUD70429.1, ECO:0000313|Proteomes:UP000030659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:EUD70429.1,
RC ECO:0000313|Proteomes:UP000030659};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium vinckei petteri CR.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAD2111859.1, ECO:0000313|Proteomes:UP000515268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ramaprasad A.;
RL Submitted (AUG-2020) 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; LR865418; CAD2111859.1; -; Genomic_DNA.
DR EMBL; KI965405; EUD70429.1; -; Genomic_DNA.
DR AlphaFoldDB; W7ANT4; -.
DR EnsemblProtists; EUD70429; EUD70429; YYG_04398.
DR VEuPathDB; PlasmoDB:PVPCR_1303950; -.
DR eggNOG; KOG3688; Eukaryota.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000030659; Unassembled WGS sequence.
DR Proteomes; UP000515268; Chromosome PVPCR_13.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
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 PRINTS; PR00387; PDIESTERASE1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 346..607
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 425
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
SQ SEQUENCE 794 AA; 93530 MW; D86633ED625F4497 CRC64;
MDEENEKDME KITTGLINRK FFLFPQFSNK KNEIEYNVLR NYNAKEYIYI HLVVSLLVIL
IEFISFSFNL SKKDATVMEI FVFIFSVLNC IMHIVVIIKF YFFSPRNIYS KSLFIGYIII
NQIFQFLSLY FFTKKNKEFK EGSIQIVAYN NKLSLYIHFF IDSVCIICLP TLKYIVSVIF
MILYASGTTI LILLTNFKKE ENASELISIY ILSVVLLMFI FLRYLAEKRN RILLYIINEF
LLNNYKADID TKTQCSNENE SISVNIDKEN DKTCNNSKTL FAEKSMIFKD FTINACYKDF
CSVSYFLKKI SVSNNDILEM EKNKENTGAK KTFDEIKKRL NESDILQIAY EADVLKNIKK
INSDEIGRNW DYSFIDSEYG KSTLVILEVG YHLISPYIEN NEDKKHKLKL FLLLINSMYF
PNPYHNANHG ATVCHLSKCL AHITDFDKHL NKTYMICYLI ASIAHDVGHP GKTNAYLSET
NHILSIRYND MSILENYHCS ITFSILQLIG FDFLINNEDT KLVDKNNYAN MRKFIIELII
STDMKLHFEY LDIFKKRKRS ENFDVADRDA INMGTINIKL ADIGHTCLKW RDHAKWTMLV
SEEFFSQKKV EELYRKNKDT DPNNFNGILN DTSIDDSMIF NYENIYINYS NNINNINEYH
FSYIKLNFIH NHDFVKSIPS TQVYFFEIIV MPLIQELQSI EQANKEITHK VLHNLNVNLK
TWKLLEKNIN LFYNTDKMKG TDYYKNLEKQ QLLRGVRLLD IGEEDVMSLT KNIFNEKSME
KTGENKKKEK KKKQ
//
