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Database: UniProt
Entry: A0A1Y2AIE9_9FUNG
LinkDB: A0A1Y2AIE9_9FUNG
Original site: A0A1Y2AIE9_9FUNG 
ID   A0A1Y2AIE9_9FUNG        Unreviewed;      1135 AA.
AC   A0A1Y2AIE9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   ORFNames=LY90DRAFT_675945 {ECO:0000313|EMBL:ORY22296.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY22296.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY22296.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY22296.1,
RC   ECO:0000313|Proteomes:UP000193920};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORY22296.1}.
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DR   EMBL; MCOG01000250; ORY22296.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2AIE9; -.
DR   STRING; 1754190.A0A1Y2AIE9; -.
DR   OrthoDB; 5479253at2759; -.
DR   Proteomes; UP000193920; 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; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF221; DUAL 3',5'-CYCLIC-AMP AND -GMP PHOSPHODIESTERASE 11; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00065; GAF; 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:UP000193920}.
FT   DOMAIN          789..1123
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          465..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        869
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         869..873
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         873
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         910
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         911
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         911
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         911
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         1026
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         1026
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         1080
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   1135 AA;  131528 MW;  C88F6E39E048E49E CRC64;
     MSSHSLHKKK NRIGVNENIG LKKRHFYPLN HNELSKEFEG KVYSSPNLSF KFNRSNEIHY
     QLNKLSKKLS HTIFDEDESF SVLNDSYTQI NSSLERIVSK MLNIANAEAA SLSLIKPIET
     SSLNNFSTSN LSLSNNIYGE VNSKIDHPIN KAFKLELTTF INRNEHNKKE RRKSENKTYK
     MYRNVKVKKI EKDISVDLSE IQYFCCEVVQ RNKVIIENNS EIINKRSWLD LNGNVRSIEN
     NNKRYISSIN LFQDLDPNNY DEKNSLFKSG YSIENVENGE SSYEDPELTY KKKYSYKSDY
     SLDNLKEIES GTDSHIRNFI GIPISCCVDR KLVPWMQNKC YNNNVIGVVC LYNKYNPIHN
     IDNCINDSNE NMSSLNTLSD SNSSINKKKG NIKVFTNNDY EKLKVYLKLL GSAIQNNYLY
     SSYNLCKNEI NNRYKKFIQY EKEIEEEVKD DSDLVSIIDN MGKETTKIND SDETNEQPKN
     SITKDEILDD DGKAIMNGDS IECLIQKTQK NVTSSILKNE IENKLIDLKK ENLYYREAQK
     ELIEKMKEMS NKNDVLTDQV SRHSIILQLV NILQSLFGEL DYYTLLRKIV SSAQELVGSD
     QASLYMVQDN DTFRYVNFDS EDDNKYEDIP ISKGGLIGHV IQTGELLNIG DAYLDKNYNG
     TIDTDHKYRT KSIIVVPIFR STQIVNGGNE TNFFSNYNGG FYIPDPTEND KEDAKKVISV
     LKLVNKLGED GEVIEFSDYD VMVIQFFAAY CAISMERAIL LERNQKQKML MDVNVEMIAY
     HMTTSVEDVD HFYEKYLKDE SKTFINPEIY QNWDFDTHSL KDQNEELILT IYSMFQEFNF
     TETFQIPEKM LVHFLMTVHK NYRTNVQYHN FSHASAVTHT LYLLLKFGGL RELINDQFDI
     LVMLVSCICH DIDHRGTNNQ FQVSAKTMLA VESSDSTMER HHFNHTINIL SLPDHNIFKN
     LSKENYKRAL NIMESCIIST DLSIFFKNLK SINELGDRYI NGENLDLENN KRNLELLHGI
     VMTSCDLGSM FKPFEETRLI AEDVLIESFE QGKKEKELGL QFTSALVDRA STEKEIPKVQ
     YEFFSNVIEP AAKALVKFLP KAKYILEGVQ RNKECWRQLM EKKIEYAIGS YTHTS
//
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