ID   A0A091UHC4_PHALP        Unreviewed;       913 AA.
AC   A0A091UHC4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE   Flags: Fragment;
GN   ORFNames=N335_02814 {ECO:0000313|EMBL:KFQ74115.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC   Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ74115.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ74115.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ74115.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KK451989; KFQ74115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091UHC4; -.
DR   PhylomeDB; A0A091UHC4; -.
DR   Proteomes; UP000053638; 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; 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:SF29; PHOSPHODIESTERASE; 1.
DR   Pfam; PF00233; PDEase_I; 1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU363067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053638}.
FT   DOMAIN          461..870
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          239..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ74115.1"
FT   NON_TER         913
FT                   /evidence="ECO:0000313|EMBL:KFQ74115.1"
SQ   SEQUENCE   913 AA;  101819 MW;  7CAA5995D546157A CRC64;
     PQMVLGRFLT VLGSVAALTL LQSSLKLRQS LLVLVFSSLV WLGSLTSLHS LPSALRPLLA
     GSVGVAGGLL ALCGGQHGIF AAQSRGAHHQ HHHHPRLPSV EEKVPVIKPR RRSSCVSLGE
     TSASYYGSCK MFRRPSLPCI SREQMILWDW DLKQWYKPYY QNAGSGNGVD LSVLNEARSM
     LTDLLTDPSL PPQMISSLRS ISSLIGTFSG TCRPKASPFT PFPGFFPYAE IEDPSEKGDR
     KLLKGLNSRN SLPTPQLRRT SGVSGIPPIE STSPRWERSN SKRSHQEYNT PSQGSHSNGS
     FGANLLTIPK QRSSSMTLSH IGPRRAGASP GLSPVGSPSH GSVSSGAFSN WSPVEFPDTA
     DFLTKPSINI HKPPGYTLSS PDFQQQVKTP VGYICSSCGH QILKPVSTPE PDFAEYKDRK
     SGEIGIASVP KESFHHAEKK KDERKEMIDQ TQNNLLVEQS PTLETMLLDH DSLMEKMTNW
     NFQIFDLVQE MGDQSGRILS QVTYTLFQDT GLFEIFKIPT QEFINYFRAL ENGYRDIPYH
     NRIHATDVLH AVWYLTTRPI PGFQQTHNEH IIESDMDEAS GIASVQVSYI SSKSCSIADD
     SYGCLASNIP AAMHDYDHPG RTNAFLVATN APQAVLYNDR SVLENHHAAS AWNLFLSRPE
     YNFLSNLDHV EFKRFRFLVI EAILATDLKK HFDFLAEFNA KVNDIDSHGI EWSNENDRLL
     ACQICIKLAD INGPAKVRDL HLKWTEGIVN EFYEQGDEEA SLGLPISPFM DRSSPQLAKL
     QESFITHIVG PLCNSYNAAG LLPGQWVDEE EEDAESTEDD DGAQLESDDE EMEDDLILKA
     QRKKGRRIFC QLIHHLSENH KIWKKVIEEE EKNKAEGAKL LTEISSLPQA DEIQVIEEAD
     EEDERQLGEE KTC
//