ID N1RMZ2_FUSC4 Unreviewed; 862 AA.
AC N1RMZ2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=FOC4_g10011468 {ECO:0000313|EMBL:EMT65482.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT65482.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB726990; EMT65482.1; -; Genomic_DNA.
DR AlphaFoldDB; N1RMZ2; -.
DR STRING; 1229665.N1RMZ2; -.
DR HOGENOM; CLU_010668_1_0_1; -.
DR Proteomes; UP000016929; 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:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 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:UP000016929}.
FT DOMAIN 252..605
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 87..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 94478 MW; D7435FA62FEB1673 CRC64;
MSTMDRAACH VIYVNRNASE DGLIHSTSGD STSDWAADEA RHVVQPLLDA FGDVHVCASG
GACLTKLFEL QEGSMLDLKP TLVLLDTPND DPVPEARRRA SSPSPSCSSS NENVDIHTPD
EALYGLGLLQ KIITEAHLRG HPTTNGQMTD GTAEQKPLPL GSLDTNRQLI RRCLDLGAVD
VIICPMSTKC ITSLEICAYR AHRDAAKEQS TLLEIRQGRK RSWVGVNEEK PFAYLREAMV
SGLMKGICRL GTSDDQINNA HVAVSSERQS AIAEAIGSWR FCAHSFTDDE LLVAAMDMFR
HALAMPELER WRIHADQLIS FLVACRAAYN SFVPYHNFRH VVDVLQATFN FLVHIGALSP
YPSGTESRST PEKSPMASLI TPFEALTLLI TAIGHDVGHP GVNNGFLVTL NAPLAQLYND
RSVLESFHCA AYSQILRRYW PSAFEDTKMR NLMISSILAT DMGLHFDYMK KLGDVQERLQ
ANNSADGWNG RQIEENKSLA CSLLIKCADI SNVARNHEIA LKWTYILSEE FSRQASMESE
LSIPSSLMTP PKQDMTSLAK GQLGFMNLFA TPLFQGVADI MPAMQYTVDE LEMNKSLFEL
KLQQEKEKQP LDDPIRRRLL KEGTFSPRTM SFAVPQEEEK EEKRDMTTLF EALDRGSDTT
PVGNGELPMP RPERDDLSPA DSQRTMGPSA ANGVVGDHRG SNGSASTFDA VRELANSDPF
QTQTRRDSAK QRSSETTDGS VSGACSGDWA SQATSATTGK MPMSPSTRGT SIVSGDSTEH
AVGIPKINVD SASLKDSSGT LRQDGSPIDD ETRSDASTTG GSIGRAEGKS LRKKTSRFRI
KDLPFFRRHK GTNSPSTADM TG
//
