ID A0A0G4ETL0_VITBC Unreviewed; 1435 AA.
AC A0A0G4ETL0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=Vbra_13207 {ECO:0000313|EMBL:CEM01577.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM01577.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM01577.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) 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; CDMY01000305; CEM01577.1; -; Genomic_DNA.
DR STRING; 1169540.A0A0G4ETL0; -.
DR VEuPathDB; CryptoDB:Vbra_13207; -.
DR InParanoid; A0A0G4ETL0; -.
DR OrthoDB; 199847at2759; -.
DR Proteomes; UP000041254; 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; 3.30.450.40; -; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
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:SF198; CAMP-SPECIFIC 3',5'-CAMP PHOSPHODIESTERASE 4; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000041254}.
FT DOMAIN 863..1188
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 123..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..489
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1171..1198
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 150..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 939
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 939..943
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 943
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 979
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 980
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 980
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 980
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1093
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1093
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1145
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1435 AA; 160121 MW; 103EC2F2357FF115 CRC64;
MSASREHVRV RKGSSISADD IQHFRAHLEE LFPSQGSPHS SQDIPSLPLK AAYVKQAHVI
HMHMEAKCTH MTTFEFCQHF SFCCSTLFGS PVVLCLARDL DDELIGFYPL EGTWIDLPRL
AQEHAKQRGK APKSPSAATP KEGDGGSPGQ RKRTTISQPD HAQSHGQTYD IPHEILHFSS
SKGLAGSILN DSAGARFVEF LLPWTTPPTG QPTPPSTATK HRWTEVLNDP PSVQEEELPD
VLLSHFLIEK LSAAHRADES RSPAMGPVPS SVTSSSSASL MADFTAASPA RATSATTSHV
PLQVYDAASG RFEYHSRRMS CVSATPSQMK TVPEEDSQSD LTTAKERQSV PDFSTMPPAG
VVTPSRDRRN TSPTVHASRV RWDEGGNREY ASEREEEAEG EGEGEGEALE REVSRDHPRV
YVLAGRLVDP RHGKPLGVVL CFAPALADVV LMDRLTEAVQ GLLIRALELE RLQRELRESQ
VMIHMHRRVF LESNDAEHTV FKLLVLLVNL TKAQEVAFYA IDYPNDSLIC YFGPKGAIGM
TLPFSTHPLL AAAVKSRKII RRADTEVRMQ NKQFDDAVGI STRASMVAPL HDHRGNVKAI
VHLINKMSSE VEYNRHLKGS TFLSKSLGTP ATTQSSPGPR RGTSAAKKGV RQFGFGEMSP
DAKSPTMGST GLSSSMKTSV VSESFWKELY KFNREEWEPL QSFSKDDERV VSRVVDEVAD
QFGGKLTKLT LEVIIAANPN SVISWIAPDK GQVRRLGVSL LDENLLSPMA SSRDTRRSTT
VFSKSHHPPP TQRRNTMRPR RFQTTDVGAV KVPASPALSD GDGVVGHRRS RDKADRVVDR
ERGLSVPCAE KRDGLEAFAE EAEYEEQEEE EDEALNSRLQ PWMSWSLDIW DYSTSAMAQF
FADGLVRLGL VTYFSLRTVS LKEFFHRVDS SYHLTNPFHN MYHAVHVFQS CFLVLYKYGC
REHLTELDQF TLLIAALCHD IDHRGVNNTF LIAAQDDLAL TYNDQSVLEN HHCAHTFKLL
TANPTCDFRI SLTEEQRLDF RKTFIAAVLA TDMAYHIKKL TKLKDRASSD DPISVQNNSD
RLLLVESILH SADVNNPVMP EPFYMKWAGL IVEEFNGQVD RERAENIPIT TFMDARDELA
RTKMQIGFVE YVALPQWRSL AALLPALREL QVQGEANYEQ WKKEKETLER AIQIKEEGGA
VVLPLPSNFN FTLKTVLELR RRAHPQEPSS RVKPLTYDTD DEEDAMQTRP PMHQSVTITP
EQVARATKKM TIMESAESIS ATESPTEPSH KHGVHFSADS ASSSRRATAF AGSAREAARR
SRELVDRPQS APNGPQPIPL KETVDEDDEV PQGRRRSQPR TSKTATVSRL GYSESPGDET
DEDEGSPTMR GVDVRRRSVS GNYVSHFQMP AQISTQGHEV IDALRRDTHP HYYSP
//
