ID A0A0A0A799_CHAVO Unreviewed; 814 AA.
AC A0A0A0A799;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE Flags: Fragment;
GN ORFNames=N301_16207 {ECO:0000313|EMBL:KGL88865.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL88865.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL88865.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL88865.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL870627; KGL88865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0A799; -.
DR STRING; 50402.A0A0A0A799; -.
DR Proteomes; UP000053858; 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; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
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:SF104; PHOSPHODIESTERASE; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR SMART; SM00471; HDc; 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:UP000053858}.
FT DOMAIN 361..774
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..735
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL88865.1"
FT NON_TER 814
FT /evidence="ECO:0000313|EMBL:KGL88865.1"
SQ SEQUENCE 814 AA; 90690 MW; 609BD60BD01306ED CRC64;
QLMGHSEWDH KRGPRGSQSS GTSITVDIAV MGEAHGLITD LLADPSLPPN VCTSLRTVSN
LLNTQLTFQA IHKPRVNPLV SFSENYTCSD SEECPEKGEK LAIPKRLRRS LPPGLLRRVS
STWTTTTSAT GLPTLEPAPV RRDRSASIKP HESSSSSADS WNSSILMTIT KSRSFSTSYA
MSSTNHLNAK RQSRQGIPPN ISPLTSPCHS PIQGTPATSP TGKTSSVSFP DSTDTDTKQG
LKPHKVLTST QSAPTLSEPV ISPSVICSSC GRPYNQIEAG DGTLDRNDGT THTLNRTDDP
AQATSDYETN NSDSSDIVQN DDETDCSKEQ TRKGSVCRTY TPETIILHPL IPPEDKPVLA
PEPLVMDNLD PLMEQLNSWN FPIFDLVEKI GKKCGRILSQ VSYRLFEDMG LFETFKIPVR
EFMNYFHALE CGYREIPYHN RIHATDVLHA VWYLTTQPIP GLPTVINDHG SASDSDSDSG
ITHGHMGYVF SKTYTPTDDS YGCLAGNIPA LELMALYVAA AMHDYDHPGR TNAFLVATSA
PQAVLYNDRS VLENHHAAAA WNLFMSRPEY NFLVNLDHVE FKHFRFLVIE AILATDLKKH
FDFVAKFNAK VNDDVGIDWT NENDRLLVCQ MCIKLADING PAKCKDLHLQ WTEGIVNEFY
EQGDEEASLG LPISPFMDRS APQLAHLQES FITHIVGPLC NSYDSAGLMP GKWIEDSDES
GDTDEHEEEE TAEMETCENA ESRKKKFKRR KIYCQITQHL LQNHKMWKKV IEDEERLAGT
EKQGVEQSTL HQSSEQIQAI REEEEEKGKP KRDE
//
