ID A0A250XQA2_9CHLO Unreviewed; 1360 AA.
AC A0A250XQA2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=CEUSTIGMA_g12646.t1 {ECO:0000313|EMBL:GAX85226.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX85226.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX85226.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX85226.1,
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:GAX85226.1}.
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DR EMBL; BEGY01000156; GAX85226.1; -; Genomic_DNA.
DR OrthoDB; 297509at2759; -.
DR Proteomes; UP000232323; 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 Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000232323}.
FT DOMAIN 942..1348
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 186..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1360 AA; 146858 MW; 0600057939480A0E CRC64;
MEPLDAHFAS NGSDILRVDI ATEILASKGI DVLDRLIMGQ QVSIEDIART RALLMHFCGS
RRPPSPPQAV REALRLALEN SIDLSVPSMG HRYGEVESGL KGQIVSGGNL MGEEDEDVQA
SLLQMVGETP TFEHQFWRED EPIIQVGQAH VCFSPVPPPP LDQQEGRHIP STQSLSCTIM
AGSHVSGNRR SLSSTRKSMS GPSLAVRRPG GESFPISFKA TSVGRRCPQA NLPCQQFIVG
SVGNQSMHAA GSLGYPTTTA LSDAFHASFQ ASSLGCTGPH QRTSLAYEAD VLSPLSQAHQ
PPASNLQPPA PLTTSSCLLR GGSPGLALNQ GITMRGLSGK DHSATRRKSR RCAIELNENS
FSRRSAFDSS SAQEVHKCTV TDSYVAESIA ADMEEYDMVG DALEEVAIPS NKIQLAPDRI
QPHAAHHGHP QQRRRWSMLS HGTHISEMLS RRLGLKGQDQ VIHSLLPEIS SASADRRRTG
SDLMRPFASS GEVLVQGMIS HMWYDHARAP RRPSSASINE EEALVVFSGG PGIVPGPMKN
NSLKEARYMG LPTQQEETSE QVPEPHSSER PEGLETLQNV PKSIKNHSPK SGFLVRLLGA
CLSPPAADLT CKVSTPNTQQ QPGSLNTKNV AETEAASTSN KSLTGSTGMR SAKNAAEKLV
ESPSKKLSRE TDYFTTFRTT SSTSSPYFSA LPTMVVSPVP TSVHTLAASP APSPACPNMV
ESEYSAVIPH GVEAAASPAM PPFTKEATSP APAASPAMPP LTKDATAPVN DQVVSIPVMS
SPRLSPASQG VKSNTSPLEE EKDYSDEAIV SCVRQNPEEA EPEDVTEQLV TKTDTEEVEE
VAQLELQDIP LRGHDKVEII TGDGLCKEAS SVMTVTGRPS GTGQAMHEDG VDVECAIVGS
GTAAAKLVSG HAVSAGILHG GEDLKLHEEG VKGDVSNEKL EADVELQSIM ARPLQDRVTR
ALFGVDEWAF DSYELCEATA DRPLSTLGFF LLKRSGVIEI LQLPEGRLTR FLHTIEDGYL
QNPYHGRTHA ADVLRNFHVI ATRGGLLRIM SDQRVMAGGK RIPAGGLGAP VPPATALSSP
ALAEHRQQQK QQDALLLLSV YLSAIIHDFD HRGLTNAFLI TDQHPLALLY NDQSPMENHH
VAAAFSVMLD EKQNFLAHLS RKAQVMLRNQ MIQLVLGTDM KQHFPTCGLF ASNVKAKALA
AAASASVACR TSSDRADCHA ERPLALEHVE PLSRLQLDEE AQLLVWKMAL KCSDLGHLAS
PEDVHRRWVL ALEEEMFRQG DLEKERGHVV SPLMDRAKAG ITKSQPGFFN LIALPLFSSF
VSVLPSAEPL LNQVKKNHTM WVSDMTAGFI FAKPTMNVHK
//
