ID A0A093RGV8_PHACA Unreviewed; 676 AA.
AC A0A093RGV8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE Flags: Fragment;
GN ORFNames=N336_08799 {ECO:0000313|EMBL:KFW95212.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW95212.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW95212.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW95212.1};
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; KL445040; KFW95212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093RGV8; -.
DR Proteomes; UP000053238; 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:SF23; CONE CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT ALPHA; 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 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:UP000053238}.
FT DOMAIN 483..676
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 559
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
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 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW95212.1"
FT NON_TER 676
FT /evidence="ECO:0000313|EMBL:KFW95212.1"
SQ SEQUENCE 676 AA; 78414 MW; 4B341C65AB3E124F CRC64;
VNKDAVEKYL ENNPQFAKEY FDRKMRAEVL GSIFKVSPGE VKEGVSFKDM SRLEECNILF
ELITEIQDEG GVMEKIVHKA LQRLAQLLTA DRCSMFICRS RNGIPEVATR LLNVTPTSSF
EENLVNPDNE TVFPLDIGIA GWVAHTKKFF NIPDVKKNNH FSDFLDKKTG YTTISMLATP
IMQGKEVLAV VMALNKLNAT EFSKEDEEVF KKYLNFIALA LRSHHTSYLY NIESRRSQML
LWSANKIFEE LTDIERQFHK ALYTIRMYLN CERYSVGLLD MTKEKEFYDE WPIRLGEAEP
YKGPKTPDGR EVNFYKIIDY ILHGKEEIKV IPSPPADHWC LASGLPTYVA ENGFICNMMN
APADEYFTFQ KGPVDETGWV IKNVLSLPIV NKKEEIVGVA TFYNRKDGKP FDEYDEQIIE
TLTQFLGWSV LNTDTYDKMN KLENRKDIAQ EMLMYQTKAT PSEVQSILKY KEKLNVNSTE
DCDEKDLIRI LKEELPDPKD LELYEFRFSD FPVTEHGLIT CGIRLFFEIN VVEKFKVPAE
VLTRWMYTVR KGYRDITYHN WRHGFNVGQT MFTLLMTGKI KKYYTDLEAF AMVAAAFCHD
IDHRGTNNLY QMKSAAPLAK LHGSSILERH HLEYSKTLLQ DESLNIFQNL NKRQFETVLH
LFEVAIIATD LALYFK
//