ID A4HWN7_LEIIN Unreviewed; 940 AA.
AC A4HWN7; A0A2K4YQM3; A0A381ME53;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=LINJ_15_1550 {ECO:0000313|EMBL:CAM66867.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM66867.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAM66867.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM66867.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM66867.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM66867.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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; FR796447; CAM66867.1; -; Genomic_DNA.
DR RefSeq; XP_001464478.1; XM_001464441.1.
DR AlphaFoldDB; A4HWN7; -.
DR SMR; A4HWN7; -.
DR STRING; 5671.A4HWN7; -.
DR GeneID; 5067873; -.
DR KEGG; lif:LINJ_15_1550; -.
DR VEuPathDB; TriTrypDB:LINF_150023000; -.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; A4HWN7; -.
DR OMA; RDAYKHE; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000008153; Chromosome 15.
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 SMART; SM00471; HDc; 1.
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 Hydrolase {ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR623088-3,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000008153}.
FT ACT_SITE 681
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 681..685
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 722
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 835
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 835
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 887
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 940 AA; 103899 MW; FDF78C561D9D2776 CRC64;
MYSAVFSPAA PYCGVAGSSH LCEAVALCQS ILARYRRTGT SFSSTELKAI QALRTELPDT
AQGPAANSAG SPHQTTNDLL NILDDATDMP HNPHDDIVAF VEECCDNTKD PTVLFAAINE
RISAVTCSRN VRTYMVITND NLLWDPVNGV AALIDDVTPL GKCAQAHNML TIASTLYIPL
WFRSELVGCV EAPSGCIPRD KATYAQLLLR SVTVAVRNSI NISIRKSEAN KIEAMVSMAT
RLARDTLEES VLVQSIINTA KKLTESDRCS IFLVKADGSL EAHFEDGNVV VLPAGTGIAG
HVVESGAVVN IPNAYEDERF NRSVDKVTGY HTRTILCLPI AFEGTIVAVA QLINKLDMVT
QSGQRLPRVF GRRDEELFET FSMFAAASLR NCRINETLLK EKKKSDAILD VVALLSNTDI
RDVDSIVRHV LHGAKKLLNA DRSSMFLLDK ERNELYSKMA DSANEIRFPC GQGIAGTVAE
SGVGENIMDA YADSRFNSAV DRQLGYRTQS ILCEPIMLNG EVLAVVQLVN KLGDDGSVTC
FTPMDRETFQ VFSLFAGISI NNSHLLEFAV NAGREAMTLS LQRNSITAQR APKRVKVIAV
TPEEREAVMS IDFGDAYDFT SPDFNLFEVR EKYSEPMDAA AGVVYNLLWS SGLPEKFGCR
EQTLLNFILQ CRRRYRRVPY HNFYHVVDVC QTLHTYLYTG KASELLTELE CYVLLVTALV
HDLDHMGVNN SFYLKTDSPL GILSSASGNN SVLEVHHCSL AIEILSDPAA DVFEGLSGQD
VAYAYRALID CVLATDMAKH ADALSRFTEL ATSGFDKENE AHRRMVMETL IKAGDVSNVT
KPFETSRMWA MAVTEEFYRQ GDMEKEKGVE VLPMFDRSKN NELARGQIGF IDFVAGKFFR
DIVGNLFHGM QWCVDTVNSN RAKWQEILDG RRDSTRSSIV
//
