ID U6GTC8_EIMAC Unreviewed; 1608 AA.
AC U6GTC8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=EAH_00037850 {ECO:0000313|EMBL:CDI83435.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI83435.1};
RN [1] {ECO:0000313|EMBL:CDI83435.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI83435.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI83435.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI83435.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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 -!- 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}.
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DR EMBL; HG673413; CDI83435.1; -; Genomic_DNA.
DR RefSeq; XP_013247443.1; XM_013391989.1.
DR EnsemblProtists; CDI83435; CDI83435; EAH_00037850.
DR GeneID; 25271855; -.
DR VEuPathDB; ToxoDB:EAH_00037850; -.
DR OrthoDB; 199847at2759; -.
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 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363067}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 651..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1115..1505
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1608 AA; 167615 MW; 06A3E43EBB01A1D8 CRC64;
MSGPVGRPPE GLMGSAPRSV FALRTAESGG SSSSSRSSSN NPRPQQAAAS QSTTSSSRLA
TAYRSFKLWV ENLLVTGLNP TVGHLSKSSV PSAVAPSTGA AAGAAAGAAA ASPANGSPTA
STKSKREGNQ ICSELSRSCC SSATPFSRDI SPDVGGPLRR HQATASVGGP AEGPLIPPLG
SLSENFLHRS VRSQTGPAYL PSRLPFSCVR TPEGRPQECS DLRGRYFVSK GSKEHDMRYV
DLCPGVCPPS SECTPREPVV SGVSPCAADA DAAAATAAAA ARLRSCCLSG PAVACPSHNP
EGAPLIHKAS LRGPCPWEPQ TATAGAEGPT PVRKPTFTPF GSSRVRWEDV KADVSLGAPL
GPPCGVPRVG GVAGHLVLDD GGADGAGRWQ QQGPGKEEAG GALGAPTCRR AGDGAAVAVA
EDASAGGGWN MLHFSCSLEH SANSAAASGA ARSGIYKEEG FVHGLNSVLS VRFSNTNSRT
NTNTHTHTNI HTNSTNNCNS NNSSSSTNHL KNSPRHNFSL VFKDPEVETA YGEFLRKARA
KRLVVVGILT IVLNTLYDLP EWTAIFTSPL MEQSPSDATD SLSAAAAAKA QQPHASSLST
GLLLALDVVE TLLLPVQAIM TSTFLRSIVG SVLIDAVCLV RRRMLMHYHK LMLLLLLLLL
TACTVGGVKM GFPFSFLVFT WTVGLASCIV IGASYAGAYM GELMHRRAFL SVAAVSAKLQ
MLQQESSNQK ATGKNMLEQL VGLVKQMGVS LSAVDPTPLD KTAKETFLYV CAVQAKCLDV
LTSGRNMYAV NWLAPDVPPD VQQLYRQFIE PYIRQDSAPL HTQDNQSAVN ASTPHNLPSQ
TKTLTHAVST PLAAAPLTTA PAAAASAAAA APAAAGTATP TLSLAQSSQA ISQPQAPQAS
ASPADAPSTT APSAAAPAPA QPAAAAPSVA AAATATTAAA AFRPIPLPLR EGVRLPEVES
EAFIPPMHYC EAKKNPLPNA QPDEPKAPSP PQAAAETPAE TTAPDVAAAA DPAVGTPAVA
GNTAGLHKRE EQSGAKPLHN LEDPIPQKDH QAGNVATGAA PAAPAPSEAT AAAVAESAEP
PAPAPAADTG AQQLQCPAGE APPWEGAFAG SEGVVEAAFQ NPTLSTVAAA TGVEWTIDMF
AVDQSTNGNC MLFVGLQLLL PHLQQHRGLS CSFAALCAFL KALQAQYLPN LYHNRMHAAL
VAHFSVLLAR SSNLYPTFPR RLGTPAEALL ASAPSLHTGP GGGVLGGPPP AGPSSMTCKD
GYSREESLLL PSCSLGTQAD VHAGGVQRRA AVDDEVVICI AALGHDVGHP GLNNAFLVST
NQSLALVYND NAVLENFHAY KTFKTLADTA DVDGGVLKLR RQVIELILST DMAQHFPILS
SFRARIASQT FSVASNEEDK WMLAKLFIKA GDIGHSMLAW EQHYVWACRV NEEFYAQGDV
EENLGLGISP LCDRRKAAEM PAAQCGFLEY IVLPLVGEIR SCFEQQLTQH HQQQQQQQQH
QQQQHQQQQQ QQALSTAWSL VEPACAGLHV IEGIIGHANY NLRCWKSLAN APTPPPAATP
TASSEPLSAA TERVGSLTDT GRHASAAFTV STVANAAQAQ QQQQQQSK
//
