ID A0A2C6KSU7_9APIC Unreviewed; 1441 AA.
AC A0A2C6KSU7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=CSUI_006791 {ECO:0000313|EMBL:PHJ19382.1};
OS Cystoisospora suis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Cystoisospora.
OX NCBI_TaxID=483139 {ECO:0000313|EMBL:PHJ19382.1, ECO:0000313|Proteomes:UP000221165};
RN [1] {ECO:0000313|EMBL:PHJ19382.1, ECO:0000313|Proteomes:UP000221165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wien I {ECO:0000313|EMBL:PHJ19382.1,
RC ECO:0000313|Proteomes:UP000221165};
RX PubMed=28161402; DOI=10.1016/j.ijpara.2016.11.007;
RA Palmieri N., Shrestha A., Ruttkowski B., Beck T., Vogl C., Tomley F.,
RA Blake D.P., Joachim A.;
RT "The genome of the protozoan parasite Cystoisospora suis and a reverse
RT vaccinology approach to identify vaccine candidates.";
RL Int. J. Parasitol. 47:189-202(2017).
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 -!- 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:PHJ19382.1}.
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DR EMBL; MIGC01003486; PHJ19382.1; -; Genomic_DNA.
DR VEuPathDB; ToxoDB:CSUI_006791; -.
DR OrthoDB; 213872at2759; -.
DR Proteomes; UP000221165; Unassembled WGS sequence.
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 Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000221165};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1089..1441
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 76..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1441 AA; 159652 MW; 4AB507C0CC156BC1 CRC64;
MPCDGDAARY TSRCLLTIQT EAVRGFHGYC PKADHAPSHV QQVRESHGTG VSLDRAKTRL
EKKLSAGLPA LACTLPKMPG QKATGARRRS PDGSSRQPGP TWERGMRSTS FGMASGADSR
QSYCAVKTTH QEKTYEMFRA YDKEIDKRSA LICRAHIVVF AALVVLSVAL FNVQMDLLAI
KTRAVVSEED VYTELMGMKN MSVTLRRVRA LSNLFGSSYQ RVLVQSTPLS SAYLDHDVYM
QLYEIAVQII TGFESVKSYD NSIRSATRCF QQSGSGRRNS TCPLREAINR LRTIDPHLSA
RLREAVLTIK VPLSLVLEQK ILQYYPAGWP DVYDPYKFVL NLITQGRFRE IFERADMYFE
ELNDIVNALR SIRIWPRLLQ GPSLALGLLT LTLLVFVGFV EYNSAQIARA FRICQDAVAF
SDEEVQTNVA DLSNVVLATL EHKILPRLHP LSGISALLLT SGKLTAYHLK LLKVMEKCTA
DMIAVCVNAL DYIAAEAELL HATTDLADLR SLVEDCLESF RPKATSKQLP LSCLFGAGCP
SLVMVDTAKL RKVLNREPRN ARLPAPGAPC LYFTDQTLSY VLDHTFDKGM GIEVFINANA
SRSGKEHDDP DQFKAYDIHV EVRQGSSVGT AAGGFNLDGR ESPRTHVKGL GVRMENQKAQ
LMVQTKGLVD RSGQGLRLLV SNKMLQSIGG GMKIQSSPLR GIFFSFAIRA KARFRLQDLH
EDFAVIAGRQ AVVITLGLSQ ETRRFFVFLC KDIGVQCVHC FSFKEMMDIL AQVSENPSEK
GSRALTPPEI FSRLQAATSR LNENSVKVFL ASIESEAAGT SSQGSPDKFP VDQHFIRLTL
PVHSSTLIEL IVRGSTGGAW QDGNSLQDWY TRRSSPAAKK SWMTSLPFPN SSLLSAADGL
ERQPPAKQLR KSLAVGMPSR SPKSERADPV KQVRRSQATT HPNKTEDLSM GDADDDESAD
GEPLYSSLNL LVLDGGDILD GSPELFPMSD EEMEKLFCRR ELIPECLYRD VNGVIHVLDQ
LGLSRRVGDI ALALAESPMR RDLAHDSTEH SLQSAIFQVV TPGQDCSSDV PTRGPKKLAP
SARFVVRGVT GSVAGLYAGP LPSQAYFNLV STSPTDCEPL TMHQLLDWDF NVLGLSPPVA
VRLTRDLLTQ FAQQANLDIP GETIMKFSVA VYENYRPNPY HNFYHALNVA QVRQFVTLLD
SSPAACNSRV LCLLLALPDV AAQFTPIDYL VLSVAALGHD LGHPGANNLF MTRFNCWPAR
IYQNVSVLEN LHAASLFQIL RDPAFNVFCS VAQTHFSQIR KRIISAILWT DMAKHFDVVA
KLQAKIQGEM VLTEGIIVTL TKPYLEGLLL HAADISNPMM NFDMCRDWAF RACDEFYQQN
KLEEEAGFPP FMPALGEFDD YNVAKCQVGF IDAICKPLFN SLALMFPAQL GDRATQLQKN
R
//
