ID H3BF12_LATCH Unreviewed; 785 AA.
AC H3BF12;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE8A {ECO:0000313|Ensembl:ENSLACP00000020483.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000020483.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000020483.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004703}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE8 subfamily. {ECO:0000256|ARBA:ARBA00006437}.
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DR EMBL; AFYH01020552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01020553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01020554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01020555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01020556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BF12; -.
DR Ensembl; ENSLACT00000020623.1; ENSLACP00000020483.1; ENSLACG00000018003.2.
DR GeneTree; ENSGT00940000156422; -.
DR HOGENOM; CLU_005940_4_2_1; -.
DR UniPathway; UPA00762; UER00747.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000018003; Expressed in chordate pharynx and 2 other cell types or tissues.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF85; HIGH AFFINITY CAMP-SPECIFIC AND IBMX-INSENSITIVE 3',5'-CYCLIC PHOSPHODIESTERASE 8A; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|ARBA:ARBA00023149};
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:UP000008672}.
FT DOMAIN 169..240
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 436..776
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 290..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 512
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 512..516
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 553
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 682
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 734
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 785 AA; 89021 MW; 6731C2740680243F CRC64;
LEPNSQRTVE TSQMKAAVTE VQFGPMRVHQ DQLQVLLVFA KEDSQSNGFC WACEKAGFRC
NVARTPESAL ESFLDKHHEI IIIDHRHSRY FDAEALCSLR SIRATNPSEN SVIVAVARKP
GDREEASVMP LISAGFTRRY IENPNIMACY NELIQLEFGE VRSQFKLRAC NSLFTALEQS
QEVIEITSED HVIQYVNPAF ESITGYRQRE VIGKDLTEMP KSDKNKPDLL DTINYYIKKG
KEWQGIYYAK KKNGDSVQQS VKITPVIGQG GKIRHYVSIK RLCNENNKAE KANERVQAEP
QIDTQSSKHK DRRKGSLDVR STTSRASDGS SQRRHSSMAR IHSMTIEAPI TKVINIINAA
QESSPIPVVE ALDRVLEILR TTELYSPQLG TKDEDPHTSD LVGGLMTDGL RRLSGNEYIF
ATKQSHHVPS HLTPISLSDI PPRVAEAMKN EESWDFSILE LETATHKRPL TFLGLKIFAQ
FRVCGFLNCS ESTLRSWLQV IEANYHSSNS YHNSTHSADV LHATAYFLSK ERVKQSLDQI
DEVAALIAAT IHDVDHPGRT NSFLCNAGSE LAVLYNDIAV LESHHAALAF QLTIRDDKCN
IFKNMERTEY RTLRQAIIDM VLATEMTKHF EHVNKFVNSI NKPLAALEEN GSGNGEEESV
NNILNTPENR ILVKRMLIKC ADVSNPCRPL EQCIEWAGRI SEEYFAQTDE EKKQGLPVVM
PVFDRNTCSI PKSQISFIDY FITDMFDAWD VFADLPNLMQ HLDNNFKYWK GLDDRNLRTL
RPPPE
//
