ID M2T938_COCSN Unreviewed; 966 AA.
AC M2T938;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=COCSADRAFT_305722 {ECO:0000313|EMBL:EMD65447.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD65447.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD65447.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445641; EMD65447.1; -; Genomic_DNA.
DR RefSeq; XP_007698591.1; XM_007700401.1.
DR AlphaFoldDB; M2T938; -.
DR STRING; 665912.M2T938; -.
DR GeneID; 19136268; -.
DR KEGG; bsc:COCSADRAFT_305722; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_010668_1_0_1; -.
DR OMA; GFMNMFA; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000016934; 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:UP000016934}.
FT DOMAIN 272..631
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 108..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 107045 MW; 73F2329727E02FCD CRC64;
MDHGACNVVY IDRRANDEHV RKENLSKSLV ARTSTGNVGQ SYFAMGKTSP REVHDNVEAM
LSISTEVHIC STGRACLQKI NQLIDDTKTA IPTFVIIDIP FDEEQRMKRL SREPRTPSPT
SSRMNRMDTT EPDDIYAMHL LTHIASEISS RNFSKLVVPV VMLSGVTLDE PSTSGPLPSP
GLHMSFPLGD TVRLTRYLDA GAVDVLTSPM SRERMLGLAV HAYRLQKEFN REEASFLTTK
RNRKLSWVGV DDAKPYAYLR EAMVSNLMTG ICNPETVGDS LDSMDFHLDY DRKILVENAV
GVWAFSAHDF TDDELLYGAL VMLKHALQMP ELERWAITED EMIVFLLASR TAYNEFVKYH
NFRHVVDVLQ ALFHFLVRIG TLPMYPPDAR NVSAPKSPIA SLLKPFDALT LLISAIGHDV
GHPGVNNAFL VALNAPLAQL YNDRSVLESF HCAAYSQILR RYWPSAFSDT AMRKLMINNI
LATDMGLHFK YMSDLGNLQQ KVAHDQGAVD GWSAKVQEEQ KDLTCGLLIK CADICNVARK
FPTAAKWANI LTDEFSNQGL MEAELEMPSC LFGGPPVRED IVKLAESQIG FMNIFARPLF
EAVTDILPAM QFVVDEILTN KAIWENRIDE ERRKKRKNKN MNLGLLTSGF SVDPTPSPLS
GGPNKSPLKI PLSAIKTISP EEAARRGSTG SIQAVAAASD SRRSSIIDRS SRRSSTTPVP
GQRPMGSSEN VTSSRRGSRD PSLTAILVTQ TPNASDQATK GQGTGPDDRS RTDRKDTLTR
PSSMIKDRDS PRPVTAPSHA RRSQALDPYP IKQPSPQSHS QVDLSHSENG NLDGSKLQPW
DTNNKLSADG NAARSDVSRD SSWWRQMGSR RRTRDGRNGE MEARTHVKES TPESLVPPNA
DSPTVSPTCS SPGRKTTTTG KIMSFFKRKP NSQREQAEKQ LSSFGSSSQL RTPQTSDPGR
SLNSDD
//
