ID A0A160FHN6_9BURK Unreviewed; 788 AA.
AC A0A160FHN6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=dGTP triphosphohydrolase {ECO:0000313|EMBL:ANB71690.1};
GN ORFNames=AYM40_04360 {ECO:0000313|EMBL:ANB71690.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB71690.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB71690.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB71690.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP014578; ANB71690.1; -; Genomic_DNA.
DR RefSeq; WP_063495153.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FHN6; -.
DR STRING; 1804984.AYM40_04360; -.
DR KEGG; buz:AYM40_04360; -.
DR Proteomes; UP000076852; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12915; PDC2_DGC_like; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR033479; dCache_1.
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; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF02743; dCache_1; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:ANB71690.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 364..497
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 506..760
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 788 AA; 86750 MW; 597435610F7194E6 CRC64;
MSQSRFSDQH EAKPRRDPAV SRRRALLVIP ALGVLVLILL WTVIFARLSV EKEATNREAM
ASAAILSAAL EQHTVKAIHQ VDQITRFVKY EFEKTPNHFD LSSTVEKGVV QSETLVQVSL
IDEHGRLIAN TAELNPKHID LSDREHFKVH EHENDDQLYI SKPVLGRISG HWTLQMTRRL
NHPDGSFAGV VVVSEDPSYF TSDFYNNAAI GREGVIAVIS DNGTVLARRT GSAESANGAF
SASGSYPTSE HVSGTYVDSI DNVTRIVSYR HIDGYPLGVL VGLSQAEEFA DYNHTRNVYL
LMASFVSLAM LSFFAVATGL IGKLLGRERE MTHLVEYDLL TGLRNRYATL QTLRHDVVQP
ANLGRLAILF IDLDNFKTVN DTLGHNAGDI VLQMTASRLA AAVGDCGTLS RIGGDEFVVV
IKGDDVEKRA VTLAEAAAEV FAQPFEVRGS SFVLHASIGI ALYSVANENE IDLLKKADLA
MYSAKDAGKN CYQFYSPQLS HRADHLMKWE QQLRVALAEG QLFLAYQPKI DLTRRCITGF
EALVRWNHPQ HGLIPANEFI PVAESTGLIV PIGDFVIETA CRQLALWQQQ GYDTLSLAVN
ISAVQFWRGD LYETIAHAIE ESGISARRLE LEITETAMME YPELVSEKIF ALKRLGVRIA
LDDFGTGYSS LSYLNRFSVD TLKVDRSFVQ AIPGDRSVCV MVTAIVNLAR SLGLTVVVEG
TETEEQIAWL AGLGHIEAQG FLFSRPVPVD AIPALLERFG VCGMKGHRAA HETDSTNSVS
STSASTNS
//