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Database: UniProt
Entry: M7AJC0_CHEMY
LinkDB: M7AJC0_CHEMY
Original site: M7AJC0_CHEMY 
ID   M7AJC0_CHEMY            Unreviewed;       681 AA.
AC   M7AJC0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE   Flags: Fragment;
GN   ORFNames=UY3_17857 {ECO:0000313|EMBL:EMP25176.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP25176.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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; KB594214; EMP25176.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7AJC0; -.
DR   STRING; 8469.M7AJC0; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   Proteomes; UP000031443; 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; 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:SF111; CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE 10A; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF01590; GAF; 2.
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; 2.
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:UP000031443}.
FT   DOMAIN          377..681
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   ACT_SITE        450
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         450..454
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         454
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         488
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         489
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         489
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         489
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         599
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         599
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         651
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMP25176.1"
FT   NON_TER         681
FT                   /evidence="ECO:0000313|EMBL:EMP25176.1"
SQ   SEQUENCE   681 AA;  77153 MW;  87FEF5BFD02A3D3D CRC64;
     YQDTNMQGVV YELNSYIEQR LDTGGDNQLL LYELSSIIKI ATKADGFALY FLGECNNSLC
     VFTPPGAKEG QPQLIPAGPI ALGTTISAYV AKYRKTLLVE DILGDERFPK GTGLESGTRI
     QSVLCLPIVT AIGDLIGILE LYRHWGKEAF HLSHQEVATA NLAWASVAIH QVQVCRGLAK
     QTELNDFLLD VSKTYFDNIV AIDSLLEHIM IYAKNLVNAD RCALFQVDHK NKELYSDLFD
     IGEEKEGKPV FKKTKEIRFS IEKGIAGQVA RTGEVLNIPD AYADPRFNRE VDLYTGYTTR
     NILCMPIVSR GSVIGVVQMV NKISGSAFSK TDENNFKMFA VFCALALHCA NMYHRIRHSE
     CIYRVTMEKL SYHSICTAEE WQNLMNCTLP THICKEIELY HFDIGPYEDV WPAIFVYMVH
     QSCGATCFEL EKLCRFTMSV KKNYRRVPYH NWKHAITVAH CMYAILQNNQ GLFTDLERKG
     LLVACLCHDL DHRGYSNSYL QKFDHPLAAL YSTSTMEQHH FSQTVAILQL EGHNIFSKLS
     SSEYEQVLEI IRKAIIATDL ALYFGNRKQL EELHQTGALN LKNQAHRDRM IGLMMTACDL
     CSVTKLWPVT RLTANDIYAE FWAEGDEMRK IGIQPIPMMD RDKKDEVPQG QIGFYNAVAI
     PCYTTLTQIF PPAGPLLRAC R
//
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