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Database: UniProt
Entry: G0QTW0_ICHMG
LinkDB: G0QTW0_ICHMG
Original site: G0QTW0_ICHMG 
ID   G0QTW0_ICHMG            Unreviewed;       598 AA.
AC   G0QTW0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-SEP-2017, entry version 35.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE   Flags: Fragment;
GN   ORFNames=IMG5_112180 {ECO:0000313|EMBL:EGR31348.1};
OS   Ichthyophthirius multifiliis (strain G5) (White spot disease agent)
OS   (Ich).
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Ophryoglenina; Ichthyophthirius.
OX   NCBI_TaxID=857967 {ECO:0000313|Proteomes:UP000008983};
RN   [1] {ECO:0000313|EMBL:EGR31348.1, ECO:0000313|Proteomes:UP000008983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G5 {ECO:0000313|EMBL:EGR31348.1,
RC   ECO:0000313|Proteomes:UP000008983};
RA   Coyne R., Brami D., Johnson J., Hostetler J., Hannick L., Clark T.,
RA   Cassidy-Hanley D., Inman J.;
RL   Submitted (JUL-2011) 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
CC       family. {ECO:0000256|RuleBase:RU363067}.
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DR   EMBL; GL983880; EGR31348.1; -; Genomic_DNA.
DR   RefSeq; XP_004034834.1; XM_004034786.1.
DR   ProteinModelPortal; G0QTW0; -.
DR   EnsemblProtists; EGR31348; EGR31348; IMG5_112180.
DR   GeneID; 14907487; -.
DR   InParanoid; G0QTW0; -.
DR   Proteomes; UP000008983; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.1300.10; -; 1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008983};
KW   Hydrolase {ECO:0000256|RuleBase:RU363067};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU363067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008983};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     20     38       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     58     79       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     91    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    118    138       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    184    206       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    212    229       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    250    275       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       20    141       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      347    580       PDEase_I. {ECO:0000259|Pfam:PF00233}.
FT   NON_TER     598    598       {ECO:0000313|EMBL:EGR31348.1}.
SQ   SEQUENCE   598 AA;  71500 MW;  2DF428CFB6B30A89 CRC64;
     MQSVISAKRR KLKNILRSKF TQFFVILLII TYTALIFTNI AVEDLEEDKN KSDQVQEYLL
     NVEICILAIF LIEILLNSYS SGFVHYFTDK WLLLDFTIII VSIILVVIDL STDSSSQFSS
     IASIVRGIFR FLRIFLLIRK VYIKIYNFQI NINNKQIKKI QSFKKQKFLV QQKHQQKEYQ
     KFQLSLKIIL TLLILFRIFN GLWILLPLIN YMIHYYFLIK IKKVRYLIYN NKIFYKHNKI
     KAQEWHKKQF YFIIFIIHIQ KFLNIKSFLY IYIYILQNYF YLIYNFKVDE LNFDCFKLEL
     ITKGDETSLL LIYLFNKYNL IEELRIDQNV FKQFTKGIQN GYKNNPYHNK LHSFDVLQTI
     HFFMKKCKFT YIAKLSKLEQ AAMYIAAAAH DYDHQGYNNV FLINTSNILA LKYNDISVLE
     NHHVSSLFQL VLNEKVNIFQ HFKNEEFKQF REIVIGMILA TDMSKHFSDI AMLKSRLSQD
     FEIDGKDKKI CMESLLHSAD VSNPIKEWKI CFQWTNKVMT EFWNQGDEER LLGLPIAYLC
     DRYTTNVSKS QTGFIDFIVK PLFEVVAIAL PDLQQYLKNF ETNKQNWIEL QPKYEEEL
//
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