ID A0A1X0P936_9TRYP Unreviewed; 712 AA.
AC A0A1X0P936;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=TM35_000013210 {ECO:0000313|EMBL:ORC93444.1};
OS Trypanosoma theileri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC93444.1, ECO:0000313|Proteomes:UP000192257};
RN [1] {ECO:0000313|EMBL:ORC93444.1, ECO:0000313|Proteomes:UP000192257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edinburgh {ECO:0000313|EMBL:ORC93444.1};
RA Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA Matthews J., Matthews K., Carrington M.;
RT "An alternative strategy for trypanosome survival in the mammalian
RT bloodstream revealed through genome and transcriptome analysis of the
RT ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL Submitted (MAR-2017) 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 -!- 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:ORC93444.1}.
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; NBCO01000001; ORC93444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0P936; -.
DR STRING; 67003.A0A1X0P936; -.
DR VEuPathDB; TriTrypDB:TM35_000013210; -.
DR OrthoDB; 240889at2759; -.
DR Proteomes; UP000192257; 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; 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:SF223; PHOSPHODIESTERASE; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
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|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000192257}.
FT DOMAIN 365..705
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 455
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 455..459
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 498
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 609
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 662
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 712 AA; 80283 MW; C3D058CA0FCFF0C5 CRC64;
MGCGATKESS SSNTPPALAL YMGTSPKLDA TTIQAADATG VVAATAVISE NITAPTNCIT
SPATGLTKSS SGAQQMRMPG KEKYIMESGA VVMDDRPKGG WTSLGLLLLY CAPVTNELTI
SYRENSSGAV FAKRFTDKEL LASKEAAGIP FSWGPFFKSL ASDVLKGKAI VQSLTHQTKE
VRFTIVNSKE PNVTYLYLCT LEEVSGPGHS AKPTAVLEYF VAPLTRMLQI RHHSAEMSNR
MTQVEKIESD FTVKSASARH YKKKVQQLLT IIRPLREESS ITAQRTMKLA LEVKAVERRL
RLIRDTRIKK HPLDELYENG GAQYFEHVPQ AEKHFPLKEV VDPNILACIR SVFPLSPGMK
LENVVELLDR PALQPYLTES SSQSIRDVFK IFQGIDRWDY DAIQLEIITN GNALFYTTYL
LMYKLDLVAH FNLDDEILQR FLLEVQSGYH PNPYHNAMHA ADVTQINYYI IMIAGLKEKC
ELSKEEILAA VIAGAIHDFD HPGLNNNFHS KTNAYLSTLY NDRSILENHH VASVYELLKN
PAYNVFAPLN DEQLRVVRET MIEMVLATDM GNHGRIFKSF QLRMGETTDW HTNKTDVRLA
LSMSIKMADI SNCARPHYIY AEWARNIARE FYNQGDAEVA CNLPISPFMD RTKEIVDFPK
GQISFMMYIV IPMVEVISEF LPSLRFALQY CNENKQIWQK YQEEHSSVNP QE
//
