ID A0A383ZFU2_BALAS Unreviewed; 934 AA.
AC A0A383ZFU2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE2A {ECO:0000313|RefSeq:XP_007173739.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007173739.1};
RN [1] {ECO:0000313|RefSeq:XP_007173739.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007173739.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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 RefSeq; XP_007173739.1; XM_007173677.2.
DR AlphaFoldDB; A0A383ZFU2; -.
DR STRING; 310752.A0A383ZFU2; -.
DR GeneID; 103000616; -.
DR KEGG; bacu:103000616; -.
DR CTD; 5138; -.
DR InParanoid; A0A383ZFU2; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000261681; Unplaced.
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; -; 2.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003018; GAF.
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; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF102; PHOSPHODIESTERASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 3.
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 cGMP {ECO:0000256|ARBA:ARBA00022535};
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:UP000261681};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..934
FT /note="Phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016979803"
FT DOMAIN 571..895
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 190..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 649
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 649..653
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 653
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 690
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 801
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 852
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 934 AA; 104826 MW; 6137981867A51A83 CRC64;
MVLVLHHILI AVVQFLRRGQ QVFLKPDEPP PPQPCADSLQ DALLSLGSII DIAGLQRAVR
EALSAVLPRV ETVYTYLLDG ESRLVCEEPP HELPQEGKVR EAVISRKRLG CNGLGPSDMP
GKPLARLVAP LAPDTQVLVI PLVDKEAGAV AAVILVHCGQ LSDSEEWSLQ AVEKHTLVAL
KRVQALQQRG PSAAPEAVQN TPEGAAGDQK GGVPYTDQDR KILQLCGELY DLDASSLQLK
VLQYLQQEIQ ASRCCLLLVS EDNLQLSCKV IGDKVLEEEI SFPLTMGRLG QVVEDKKSIQ
LKDLTSEDVQ QLQSMLGFEV QAMLCVPVIS RATDQVVALA CTFNKLGGDL FTDQDERVIQ
HCFHYTSTVL TSTLAFQKEQ KLKCECQALL QVAKNLFTHL DDVSVLLQEI ITEARNLSNA
EICSVFLLDQ NELVAKVFDG GVVDDESYEI RIPADQGIAG HVATTGQILN IPDAYAHPLF
YRGVDDSTGF RTRNILCFPI KNENQEVIGV AELVNKINGP WFSKFDEDLA TAFSIYCGIS
IAHSLLYKKV NEAQYRSHLA NEMMMYHMKV SDDEYTKLLH DGIQPVAAID SSFACFTYTP
RSLPEDDTSM AILSMLQDMN FINNYKIDCP TLARFCLMVK KGYRDPPYHN WMHAFSVSHF
CYLLYKNLEL ANYLEDMEIF ALFISCMCHD LDHRGTNNSF QVASKSVLAA LYSSEGSVME
RHHFAQAIAI LNTHGCNIFD HFSRKDYQRM LDLMRDIILA TDLAHHLRIF KDLQKMAEVG
YDRTNKQHHS LLLCLLMTSC DLSDQTKGWK TTRKIAELIY KEFFSQGDLE KAMGNRPMEM
MDREKAYIPE LQISFMEHIA MPIYKLLQDL FPKAAELYER VASNREHWTK VSHKFTIRGL
PSNNSLDFLD EEYEVPDLDG AGAPINGCCS LDAE
//
