ID A0A150GD57_GONPE Unreviewed; 2208 AA.
AC A0A150GD57;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=GPECTOR_33g595 {ECO:0000313|EMBL:KXZ47713.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ47713.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
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}.
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:KXZ47713.1}.
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DR EMBL; LSYV01000034; KXZ47713.1; -; Genomic_DNA.
DR STRING; 33097.A0A150GD57; -.
DR OrthoDB; 297509at2759; -.
DR Proteomes; UP000075714; 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; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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 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:UP000075714}.
FT DOMAIN 1831..2197
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 319..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2047..2069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..453
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1526..1581
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 319..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1909
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 1909..1913
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1913
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1950
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1951
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1951
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1951
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 2103
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 2103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 2154
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 2208 AA; 233062 MW; 88FDB3D7580572E0 CRC64;
MRPQHPRLST TASPWTGSVA TEERLREQLQ TLQRKLLHTI TENEALSTRL AGLRSVCLEL
QEQLHLADVA SNLDPAVQSH LVHLCTTAAS YCEVEPQIDT LGRISSSGKL PDHDLACYAT
DAAFVASACG GMSGGVLLAN PASGATDSLA AVGLACNGGL GVSPGQPGAG IGTGMSPCMS
PALGARMGAG VRISAGLGSG FGEGGSARLA AGGRGGMAVA ANAAREGGCD RNYTALMDSF
VALKASYDLL IQQQQDPTLM EQQLLPLPHS AALSTAAGSV GESSPQLTAK MGMFIGARCS
GSGDRDLRSR MMSGNGVASI TSEQSAGGGN SGSSGAPQVP RMSLTGLMSA LHTMPADADD
GEDPEAAGSC ALSADWRASS LGDVGSERTA DREVERLAAH ARALKASYDV LMLQRDHALS
AAVAQKAAFD RTLAEAQEEA VQAAETAAVT KAQFDKFILD KAEEKAAFDL VLEKTAAEAA
QQKAIADKAL VDMGELQECA AATKAQFDKF VLDKTEEKAA FDAVLEKTAA EVAQQKAIAD
KALLDMGELQ DTATATKAQF DKFVLDKTEE KAAFDAVLER TAAEASAQKA IADKALLDMG
ELQESAAATK AQFDKFVLDK TEEKAAFDAV LEKTAAEAAA QKAIADKALL DMSELQDTAT
ATKAQFDKFV LDKTEEKAAF DAVLEKTAAE AAQQKAIADK ALLDMSELQD TATATKAQFD
KFVLDKTEEK AAFDAVLEKT AAEAAQQKAI ADKALLDMSE LQDTAAATKA QFDKFVLDKT
EEKVAFDAVL EKTAAEAAAQ KAIADKALLD MGELQESAAA TKAQFDKFVL DKTEEKAAFD
AVLEKTAAEA AAQKAIADKA LLDMSELQDT ATATKAQFDK FVLDKTEEKA AFDAVLEKTA
AEAAQQKAIA DKALLDMGEL QDTAAATKAQ FDKFVLDKTE EKAAFDAVLE KTAAEAAQQK
AIADKALLDM GELQETATAT KAQFDKFILD KTEEKAAFDN VLERTAAAAA AQKAIADKAL
LDMSELQECA AATKAQFDKF VLDKTEEKAA FDAVLEQTAA AAAQQKAIAD KALLDMGELQ
ASAEADKAEH DKALLDLAEL QARTGPAGPR SAAATTKAQF DKFVLDKAEE KAAFDAVLEK
TAAAAAQQKA IADKALLDMG ELQESAAATK AQFDKFVLDK TEEKASFDAV LEKTAAEAAQ
QKAIADKALL DMGELQDTAA ATKAQFDKFV LDKTEEKAAF DAVLEKTAAA AAQQKAIADK
ALLDMGELQE SAATTKAQFD KFVLDKAEEK AAFDLVLEKT AADAAQQKAI ADKALVDMGE
LQAAAEADKA EHDKALLDLD TAAATKAQFD KFVLDKTEEK AAFDAVLEKT AAAAAQQKAI
ADKALLDMGE LQESAAATKA QFDKFVVDKT EEKATFDKMY TDVQVAASQQ KAIADKALMD
FSELKAAADV TKSQFDKFVL DKTEEKATFD ATLEKVAAEA AQNKAVADKA LVDMGELQET
AAATKAQFDK YMNDKAEEKA VFDAALEKAA AEAVAQKAVA DALRAEAETV AAQLAAERQT
LDDLQAQNER LLKQQEVLQA ELQMALSSYT PKAIIDAGTP ADKILSMMTD LLDGSPPSIQ
DILLVQSAIL EAHDIYQPVN LGKQLLQSST LDNDVGMALL AQLGNGDEAR MLTRASGSES
SLTLRDFGTR ENGAAASRGG VVRGHGGGSS SSSLEDAVAG AAAKWASLEG AIMAILAADA
PFSDVRDNGG TGGAAAAADR AAAEGPAAAV MSRAASTVSR GLHARVRRRA SVLSFGTPHA
QSPHGISTGP GGMAGGLNSS GVGSVASGAS GGPAAGSAAA SMLEVCAPGL LAANPPAALE
RSNTMCTDAT TDADEFPEQP VFTEFDIKPQ MLARFLRRLE EGYRPNPYHS KTHAADVLQT
FNVVIHRGGL SPGYVDPLSL MACYLAALVH DYEHGGLTND YLINSGDLLA VRYNDRAPLE
NHHLAAAFTL LKKPEYAFLA HLPKADMDRL RKMVIELVLA TDMKQHFAIM SHFTTVHRLG
SANSVTPSLL SGTERRRSSS NASSINSLAH GGSGTNIEMD KIVIPLDENE RMLSLQMALK
CSDLGHVSAA LPVHCRWVAL LEEEFFRQGD MEKLHHLPVS PLFDRSKPGV TKSQVGFFDI
VVIPLLNAFS RVFSNTKPLL TYTMRNYKYW SEIQKREQQA AAAAAGRK
//
