ID A0A250WWX9_9CHLO Unreviewed; 1662 AA.
AC A0A250WWX9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=CEUSTIGMA_g2766.t1 {ECO:0000313|EMBL:GAX75321.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX75321.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX75321.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX75321.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-2017) 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 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:GAX75321.1}.
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DR EMBL; BEGY01000011; GAX75321.1; -; Genomic_DNA.
DR STRING; 1157962.A0A250WWX9; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000232323; Unassembled WGS sequence.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
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; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR InterPro; IPR011645; HNOB_dom_associated.
DR InterPro; IPR042463; HNOB_dom_associated_sf.
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; PF07701; HNOBA; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
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:UP000232323}.
FT DOMAIN 1224..1601
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 672..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 303..337
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 716..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1299
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 1299..1303
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1342
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1506
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1558
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1662 AA; 180667 MW; E0585A4EAC479AE3 CRC64;
MGINEKFNAF VNTSGISIAQ ALEKDWSDVQ RCRLMSTMTS GPKVSDFSTY PFLQPFLLCV
KNENGADFQV TVRSSESDTS LTCSRQSPES VVQSIQNLSK ILHGECMDVT IREGLTDGEL
NMEHCDNTDV KMYHLKFTPA AKTAVREYLQ QKSWSSSTSE DLRFSPKPTL FGELFPFHFL
INQQCCLLQA GPKMKKLIPS WIIGSHPSNS ALQVSAPTVG WDYERLSARS TSCVFLSAEA
GSGEGLVIRG QFHVTDMDGA PALLFVGSPC LTTVSKLKGW DLNWLDLPAH DLGRELAMLG
EKYTCVQEEM QNLKMDLDAL EKEAKWMEQE AAWLEKEKTK TDAMCERLKD SLKEALSLQD
SGFLNTPSPM LMDVGTPALM ALGIIEKFLN GEKVSVKEAM EAHNAITLGG HDLHKPLKLK
EMLGVSGMDA DVNEALDLML GASKTDSGWA DYAEEAEAHT EQLTPYELAR ALTAVWPQES
RALRNSQIQA AVDAAEASNQ AEDEVVRAKA YVAHNYRAMD SRPSTPQRLG EVTASDASIL
KCRGGSEDVS GAPTSFSESL SDSASLLVNT SSLLMGPGPV DSFHQDAMSE AVSKTVSGMR
IPPGNSSSQP LSPELLIGHM SGDKGFQRSS SMLSLRSSQG TIAYRPFAPL KTSDSVGSET
YCLTSEKASL HQQLPGGIKK ATMSRATLSS RENRGTGISV GRDPLYPKLV QHPDKVDAHS
QQQSPSKTSS RVSPGVTPSA NNTSLVVVSS RKLSDEQGKV GGNALIGTAQ RYPLDLMYSS
LYSNSGRLSP RSSILMVGGS GGMADSMVVK GSTLRASSPS LLRHRQPSPP AHSPVHGSCG
KVRSVSLPSV PGMGPVGMPP GQRGGPNQPL IMRGSSPHGK GRILFRPQSQ TSPGSIIEPD
SLSAATTLRS SRDEQQDISF GADSRNSSPS ASRRVLFTQL PAAPKPPKSS LRSASSSDTA
PTNLMKGPGS QRLMINSSIP LGKFSEEEEN TSLEGWAKGS LATGLKVLSE TIGSFDDGLN
NGSSSSMSGL LLSRLSSRPK VQLHQKPSSS SEEGGPMVPQ LRARFSEQLS SHVPVPELNL
PAGEPHSSRS QHNSDLHQAI AAHRLRSARS SYAGSLAASD ETDDDIDTLL RDREDAEADQ
LMRRTKRRVR RSYSFGGNRG LGGNTVMSAL AWNNVMRRTD SLRVGSLGSF RRNGASMEVE
GGGVPSSSTA MVTASGSGHG HEHPVKEPHD KLAHLLANIE EWQYDIFALE EATQSHALSV
LGFALITRTE AFRRFNMDAD KLARFLMEVE SGYTEKNYHC ASHGADVLRT MHVLGTRGGV
WKETRCSEIG IIAMYLSALI HDYEHVGYNN DFLIKTHNEL SIRYNDRSPM ENHHVASAWA
LLREDRHNFV ENMPAKAQEF LRKLVIECVL STDMKQHFSL TSTFSSKAAS LAPQAGPNSK
PNSRAGSRNN SRPSSAHSSA GDKVEDAPPP RPPAQNMESS SKQSSFKAWD DDSRVLAMQM
LLKTSDLGHL AGPLTAHLAW VQKLEKEMYK QGDEERTLGL PISPLMDRES GKGVTKSQTG
FLNFVALPLY KAMALAFPDC GPILSALMSN HKYWSEQEKL QMMRYIMEKA ETLPAVHAGS
TCWPEKKRLK MAQAMSDKWN NWVFGLAEAA GNLLFIKCLD CI
//
