ID A0A0S4JK37_BODSA Unreviewed; 1083 AA.
AC A0A0S4JK37;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=3'5'-cyclic nucleotide phosphodiesterase, putative {ECO:0000313|EMBL:CUG91885.1};
GN ORFNames=BSAL_34625 {ECO:0000313|EMBL:CUG91885.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG91885.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; CYKH01001977; CUG91885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4JK37; -.
DR VEuPathDB; TriTrypDB:BSAL_34625; -.
DR OrthoDB; 125130at2759; -.
DR Proteomes; UP000051952; 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 PANTHER; PTHR11347:SF179; 3',5'-CYCLIC PHOSPHODIESTERASE PDE-3-RELATED; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF00233; PDEase_I; 2.
DR PRINTS; PR00387; PDIESTERASE1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT DOMAIN 518..888
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 611
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 611..615
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 652
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 796
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 796
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 847
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1083 AA; 116291 MW; C2961F5F22140D54 CRC64;
MSNTPSNASL PAVRIQQPST SHYQEQSYLG SDQDAILAAA GGAGGNGAGL VSLESTRPNS
SSINSNNQQQ QLHPTRPRRV SVNGGGPARS PSKGVRHQNE TNEILHQRLS TALQSLRQLQ
ANTEASTAPA TTGDTFAVKL CGSIEQQLLA ALETVDDTML ANSATAMSSA TPSKANGGVA
ASSSDDMPTM MMMPRGISVD AFGASQTHHD GSSHFMNNTT SHISGGVAGL FYMQTSFASG
VTPFGGELRN TRDNLQRSTS ISGSPAVSPH SSFHNFKNAA AMVTGGAGQS VASVANGAVT
VNRAQKGRVT SVRYDNVPDG NVADWLTDTF APTQRRRKSL GMSLASQSQI NVRSLSPALS
FTADRGSSEP PPSVSIDNLL PITQIQSSGQ ESTTHGSDTT RRYSNKDPLS ANTHPLMHGD
EESERHKARD PPIPIDESLS SRNTASTPGR FSPVEQQQHA PGSVPPPPSL LQTTSVKEPL
PSTLSATGGA VARALSPHSS SGATARVEAA TFVRFQRSMD RLIPAVASTL DTALVLKKCG
GGIPMIDDVD SEDFDIFDVV QERGVDDTFL VVATNVFARY SFMTSLSLHV PKFVSFLKCL
CQCYRKENLY HNAIHATDCL QTVHIFLCVN DMRENFSDVE LLSVLFAAIV HDLGQLGVNN
AFLNRLGHPI SQIFNAQSTL ESAHAASALY LVSLPQYNFF PIPFRQSPQN SGDAQASKAT
QSEPGDATNL SVFVPEAPMT PDMLDDFRSL VVECLLATDM KHHTDQIRIV KGMLDSGIIG
DGDFTNILRS IIHVADISNP MKMYPTYVKW MSRVVAEFWV QGDAEKKRGF PISMMCDKRN
TVIGKAQHGF IQFVVRPFAL EMAPIMPSVW LKRLEDNAAR MQGMSQEEEG AVLQSIHDLI
GDSEWADDDV GSSATASRLP DGTPTRLVDI FQQLLSQGGT WKCSADPQSE QAPAQLGALA
IVPRPPHVSA AGRPPSSPPR KVKTTRATST TPVQEQQHPQ QQQPTLPPIR GALAIRPYGS
ASPKRTLANA LTTPSPFVNQ QHAATTATSY SNDVVAALRP PYRQLRDVVP TPQWMATLSS
PRK
//
