ID G4TNS6_SERID Unreviewed; 1276 AA.
AC G4TNS6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 22-FEB-2023, entry version 47.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=PIIN_06919 {ECO:0000313|EMBL:CCA72964.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA72964.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA72964.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA72964.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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:CCA72964.1}.
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DR EMBL; CAFZ01000193; CCA72964.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TNS6; -.
DR STRING; 1109443.G4TNS6; -.
DR eggNOG; KOG3688; Eukaryota.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_263501_0_0_1; -.
DR InParanoid; G4TNS6; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000007148; 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:SF219; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE, ISOFORM I; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 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:UP000007148}.
FT DOMAIN 529..1013
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 42..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..527
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 137987 MW; A08C2ABF0FE2C048 CRC64;
MSSESSRNND SLTLRDRWGA VTVLIEQKDV LSTAAARRTS LTPSLVAPSS DGTAPEQPWN
SRASTTSNSS PSLHHSTSVA AAATNRRQRT STTMHASLDV PHSLVLGLSS QAIVQIQPQL
LPLPAARPLV LLVQLEDYIP QELSTTPSSV CFPPNATPTP QSIQRALAPL YTVIARLQAA
KANEGVDLKQ EVAIMLYSEN VHLPDEIAIA AFKSGAHGLL CPPFTPDSVK RAVSSALERH
AYMHSTRPPH SLSELAPDHH SDNAEQELHE TPQPAFQAPF TSSAPVDHHL RASRRQAPEI
QSHEREGFSP MDTSHPILDS APHLSLADSL GARGFPHLAG VTERRASVDL GGLALSINSF
TRSSDSMAFD SAPRELDWRA TTGSGWAGWD TAPQGSSPFG EQRDTITATT SKRRKSVPAF
DEGGELEHAN LVLSMHLHSI AALENATLAS FAPNGNSMRH QQTLSNSSAF TSSPSASPLS
QHYPEGVPFS VTNAGYQLQP LSAKVDPGRA PSPSPPSHSP NGPLQLVPPS PRNATRLLNL
LSSWHFEPFL LSPNDAANCV ILMFSTLLSA FKVSPLTTSP ISESAASGNT RIPLASLGSI
RVKEDIAPFV QSLQRLYRKE NRYHSFVHAL DVLQAVWTFL KNEGRVPLLE EQDVQAQADW
EVSVDGAWRV RAASRFNAGY DGAESKKKRG PSALSLLNDA ELFVLCLAAI GHDVGHPGNG
NAFLKNAQTP LSKLYEDKSA LEKMHCTLLL RLLKKYGMEH LITTQTPEGR EGRRLVVGTV
LATDMSWHFQ WLEGFQRAMK ERKTRTRYAL QMQQAATSAA RGNTTSTTAQ TLDGGGDDAS
SETHTDEAPE LVLNPSGNGT WTVEPDTEEN RRRASLVPPP QGDVGGENED GGEGLFRSPE
IADREDRMFL CQAIMKCADI SNPCRPHHIS RHWSTVLLEE WAAQALLERH LGLPVSVAAD
ANEKVQCVGQ ISFIKLFTQP LFDAVSAVLD GLSPIAKDCA ENRVLWERRL ATFDPPPDSA
PADDTAPNSP TTHVSQMIRP IPLALPILPP MARYAKTVFP LSFPRRKKAP LETRRLASMS
PWHAVAVPMA SGSKVAAGGG RRFHTANGST ANTSTSTATN ASSGTSRMWS RSRPESVSST
STLSSLPGSN SSRGGGDMKG DLPRTPTNAN SMMQPGQMRS PISPLLSPFS TSNMGLPFSF
GGYSVGDTNI GETQAFVPSS VWDVDREVKQ RCRSTLHHAW EHRDGRKAQN SLLLEMLGLD
GSDPPNGFRA RRSSFG
//
