ID A0A0N0P788_LEPSE Unreviewed; 760 AA.
AC A0A0N0P788;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE Flags: Fragment;
GN ORFNames=ABL78_2405 {ECO:0000313|EMBL:KPI88509.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI88509.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI88509.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI88509.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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:KPI88509.1}.
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DR EMBL; LJSK01000048; KPI88509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0P788; -.
DR EnsemblProtists; KPI88509; KPI88509; ABL78_2405.
DR VEuPathDB; TriTrypDB:Lsey_0048_0290; -.
DR Proteomes; UP000038009; 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; 3.30.450.40; -; 2.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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 cGMP {ECO:0000256|ARBA:ARBA00022535};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3}.
FT DOMAIN 603..760
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 683
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT NON_TER 760
FT /evidence="ECO:0000313|EMBL:KPI88509.1"
SQ SEQUENCE 760 AA; 83649 MW; 0E02AF4394294467 CRC64;
MYCSVNNTQS VPQHFAEGSN HLCEAVALCQ SILARYRRTG SSYSPTELSL LRALRDALPD
APRDAESRKV SQREVSNAFL RSLDTDNGAS EEEGMVAFVE KCCDCTMGVK ELFHCVNRQL
SYALNINGIN TFVVNENDQL LLDPVHGVAS PLENTTPVGK SSTTRDMYVI SNMLYIPIWS
NKEFVGAVEV PGGTPSQCIT PAITLLLRAV TVTLKNVKAM FAKETAAQEA EAMVGMATRL
AHDTLDETVL VQSIINTAKM LTESDRCSIF LVKDDGSLEA HFEDGKVVVM SAGAGIAGYV
AQTGKVVNIP NAYEDERFNR AVDKQTGYCT RTILCLPIIY EGTIVAVAQL INKLDRVTES
GLRLPRVFGK RDEKLFETFS MFAAASLRNC RINETLMAEK RKSDAILDVV TLLSNTDIRD
VDGIVRHVLH GAKKLLNADR SSLFLLDKER NELYSRMADS VAGNEIRFPS GQGIAGTVAA
SKVGENILDA YADPRFNDSV DRTLGYRTQS ILCEPIVLDN EVLAVVQLVN KLDENGSVLS
FTTVDQDTFK VFSLFAGISI NNSHLLEFAV KAGQEAMALN LQRSNVTMGN QKAGKTTKLA
GISKEECDTV LAIDFQGAYD FTSPSFNLFD VRESFGQPLD AAAAVALQLL WNTGLPEKFG
CRKETLLNFI LQCRRKYRRV PYHNFYHVVD VCQTLHTFLY TGKASDYLTE LECYVLLVTA
LVHDLDHMGV NNSFYLKTDS PLGILSSASG NNSVLEVHHC
//
