ID A0A0M9A3F7_9HYME Unreviewed; 1521 AA.
AC A0A0M9A3F7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=WN51_13376 {ECO:0000313|EMBL:KOX75069.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX75069.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX75069.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX75069.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX75069.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; KQ435774; KOX75069.1; -; Genomic_DNA.
DR STRING; 166423.A0A0M9A3F7; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000053105; 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; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF209; 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:UP000053105}.
FT DOMAIN 554..814
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 817..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 318..404
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 850..865
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 719
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
SQ SEQUENCE 1521 AA; 172658 MW; 61F05BAC6D48E9E3 CRC64;
MRNDCITPSY DVGMLEQRNK EETRLNRTDT TVENCTPCSP TLTKDSRDWR KEHVERQRFN
EAKSDVCWTC RMDHEGAQRE LVVDERSFSL LVPRRPSTGS CNAESFTLQV LRTAARSNRK
ASPCKLSQGR AQRSGRRFKA DISCLAMDLE ARNGTGGNDD EEYTNIYFIV GDRRETVTYK
ADQVTDMELK GNSFNSGTIA IILCRLGNRV ILHGEWFVES PSVSNALWNT LYHNTVRVKS
ARVNWNAEHG LFEKCCSLEK LFRNAAEAGP LDIVKLCKGD KLLNISTNLP ANTPDSPYVL
QIVGAHPASS GVIEAEVLWA LERRVAALER QLREHQEALY ASPSFALREL KRQVDSFKNK
LEHNDQLSWL SNRYEIDQKL KLNITKQQQQ QQQQQKEQQQ QQQRIALFVF RILPNKSNFN
FFGPSILAVL SGTDCIQEDL ESMNSAFRKH VETKALLNFA VGREEGEDTF QRELYHEFNQ
QRAFQGKAWQ IGFCHNFSVT KISIMTELFN KLYADALFDC KINDVSVSSS VREWLRSPAF
DARQWEDEEL LLMLQTMFVE LDLPQKFNIP LPILRNFLYE MYAIAWAVDL PSRIGDLEVF
ILIVSCICHD LDHPGYNNIY QINARTELAL RYNDISPLEN HHCSVAFRVL EAPECNILAS
LDNATYRVVR EGIIRCILAT DMARHNEILG QFTDIIPEFD YSSKAHINLL SMILIKVADI
SNEARPMEVA EPWLDRLLQE FFKQSDAEKL EGLPVTPFMD RDKVTKPSSQ VSFIGLVLLP
LFEALGELLP ELQSLIVQPV REALEYYRRL NEAAKDERVV KSTSSHSMRS KRSAGTVHSR
SRSTDDDITE NLTGEEAENL ESSDPETATE VEVSEKTLKF KISTEGTLAG PATGRKSYPG
SRKGSREKSS LDYHNHDLAR AVREHERERK RSKGESLGSD LSSPMSAWSA EGTTRILEEL
EKDETQALLD AKLNERRTME GNGNVVVESQ QRNNLKKTSS LAIENEQETR SSRKEVQRES
VVGGLRCCCE DKTGSNNHKS IFSRLRNFTD RLSISFDSKE PPAPKPTKHV TKTLNKSNSV
TAATTSARHN NTLAICKRCN LAKVTMKESK AIATVVELSS VDKRAMTLPK VRKSTDYKNK
SWRMVFAKEK RSSASLEALP GAMSESSLAK HRRNSSNPEG KSHSMKDAKD QVIESSASME
DISKMAKQAE SAMLCGTLEP KKAEERPHAG SLDSMLYKDS AKSRKKPTYE ASPTTTSKKP
SSGLLSRFKS GMSIDSTRSN SNSDSLHDQS TQSPSGWISS LTASFRPKRQ VPETPQVLSS
HPPRSPSREE IKHFYVVTPK KRYRAIDCTV EHGFPVVFRL IEERVSSRGA SDVSQREPAK
GLNKNIRPMQ EFTRTQQILP IERLTLKPEL LESEPTEGIK SFLKWKYPKL LFIFWVALKR
RKVSNLKTFE RIRTEVNQSL VVLVFLLHLD QHIDEIAPLL SGIDPLVNHV PENGSKELCR
FLSEELGFNI LDHFREEEYE V
//
