ID A0A0F0IDC9_ASPPU Unreviewed; 1026 AA.
AC A0A0F0IDC9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=P875_00010607 {ECO:0000313|EMBL:KJK65126.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK65126.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK65126.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) 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:KJK65126.1}.
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DR EMBL; JZEE01000374; KJK65126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IDC9; -.
DR STRING; 1403190.A0A0F0IDC9; -.
DR Proteomes; UP000033540; 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; 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:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
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|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT DOMAIN 290..636
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 32..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 366
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 366..370
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 424
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 538
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 593
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1026 AA; 112683 MW; FD4C428AED6B4203 CRC64;
MGVPNPVDSM DGVECSAVYI DRRVVQERWV YQSPTDSSNT SSSDASTFPD EPDSLRSDVE
VLLGVCKRIY LCNVGPSLAS KLAELSDDAI TTCRPIFAFF DVDLSGEDAG LSRRKSGRGS
WPEVSPPSPA SLRRGFTFSS QSEGAHDLKL LSGLSADIQV QESPNLIVPV AVLRSSTQPP
SSVPVDPQRN GAIPEFQQIS KCLDAGAVDV LASPLSKARM QGLVVHAFRA RKSALKEQSR
FMSRKKLRKY SWVGVHDEQP YAYLREAMVS KLMKGICNPE EVIEEFQDQS ELDVSPEREE
LIKEQIGNWN FTAHDFSDDE LVLGASEILH HAFTMPNLEQ WQLTPAELRT FLLACRASYN
SFVLYHNFRH AIDVLQSVFC FLLHIGALPP YGSVTRDTDS KSPIASLLTP FDTLTLLISA
IGHDVGHPGV NNFFLVKLNA PLAQLYNDNS VLEAFHCAAF SQILRRYWPS AFKDKQIRKL
LISSILATDM GVHQKFMERL GSLQEKFYEN GQTVDGWKPQ DLDMYKTLLC GLLIKCADIS
NVARPWDVAE KWTKILQEEF ANQGEMEKEV GMETALFGGP PELGNVYKLA IGQIGFMSIF
ALPLFEGVAD ILPDMRFTVE HIRNNQSRWH HLADLEKRKQ TLLDESGPED VVSPCTQSPA
VSLKGFKGLR APLTTSGPDT PAKQSFPLNE NSSRRETDYF GAAHSSVDSG TSRGSLNENT
ISPVVSPDTA GPSMDITGSP LPSQTPSRKS SNAVPDLTMV SIAGASPDRN RIRTDSGVSN
GAADGHSSLD TNHSSRDPAV LAAVIFSNSR KEDDSQDHSS VRGSMGDVTG ERPSSSRNGP
QNYRRHHANT NSSGRTSGPS NSQRNSCTRT HSISNYSNNM TPISPATNAT SFLTVDDSED
KGFSQESSSR SDRESDRGDA RPGSSNIDRE SEGRPPQSSH TSHSQSDEMN KNHLMAPVKG
NGNGYSKQSA HPPGSPKQDG NGQQWDGSSG GEQPSRKLLK RRSRLRLAFW KRKTHHSHHH
ELSGES
//
