ID I3TVY3_TISMK Unreviewed; 884 AA.
AC I3TVY3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Diguanylate cyclase/phosphodiesterase {ECO:0000313|EMBL:AFK56921.1};
GN OrderedLocusNames=TMO_c0311 {ECO:0000313|EMBL:AFK56921.1};
OS Tistrella mobilis (strain KA081020-065).
OG Plasmid pTM3 {ECO:0000313|EMBL:AFK56921.1,
OG ECO:0000313|Proteomes:UP000005258}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK56921.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK56921.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC PLASMID=Plasmid pTM3 {ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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DR EMBL; CP003239; AFK56921.1; -; Genomic_DNA.
DR RefSeq; WP_014747910.1; NC_017958.1.
DR AlphaFoldDB; I3TVY3; -.
DR KEGG; tmo:TMO_c0311; -.
DR PATRIC; fig|1110502.3.peg.5178; -.
DR HOGENOM; CLU_000445_70_49_5; -.
DR Proteomes; UP000005258; Plasmid pTM3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF71; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:AFK56921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..884
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003680380"
FT TRANSMEM 203..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 464..595
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 604..857
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 884 AA; 96456 MW; 3E83A74E01E7032F CRC64;
MPPGSVRCRL CLALIGMLFL ASLMAGGGAV RAAIAAEAPA VMTEGIGAGV DLAPYTRLLP
DPGGGMDLEA ARRATGWTAT PNRVLRFGYA PDMAWWARVT LTNPSARTAR VVLDLGTSQQ
DYVDWYVTDP DGRVLLANQS GDRRPFDSRL MPYRDLALPY HLPPDASVTV YLRFDTHDGL
FAMMPFRLYD YTGFFTASGR ESLLLSMFHG GLAALASFNL LVFLATRQGP VGLYVLHLLA
VLAGSASYRG YGFQYVWPDL PAFGNAMTAG SIILAFVTGS LFVVRYVRLH RHVSVITRRA
VSLLMIAALS GLVPLAFGQY VLAVAFSLIG LLLVVVVYLL NVHLLFKGVR EARFTVPAFF
ALIVAVALHY LELSELLPAS GFRIWPLIVG SSIEVMLLAF GLADSMNQQR ERRFAAERRE
EAARLHMAEI EREASHKARH DELTGLLNRR AAEDWLEAAV ERGQPVAVLH LGLSDFGAVN
EAIGHAGGDA VLRQLGRRLE TTLAPGEIAA RLLADEFLVL MPGTDQARAM IAADRIQRLF
AVPQQVGGTD MSIACRVGIV IHPDDARTAE DLLRRAAIAM QDAARLPRRI QLYQAGRDDD
HRRRIALIRD LRHAAEHGEF RLLYQPKIHV ATGRLVAAEA LIRWQHPTYG MISPAEFIPL
AEQSGATRGV TRWVIREAVR RMRSWRLAGL DIGLSVNISA LDLDDPDLVG FVGRSLEAEG
IEGGRLTLEV TESAIMTDPD RSRAVLEGLR RSGVTISVDD FGTGYSSLAH LKRLPVQELK
IDQSFIRDLS AASEDAVIVR STIGMSHNLG LSVVAEGVES EEILTLLGSW GCDVAQGYAI
ARPMDAADFE RWAGHRMAAA REQAAAADLT RVRTVPGDQA PQPG
//
