ID L0DJU7_SINAD Unreviewed; 1261 AA.
AC L0DJU7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=PAS domain S-box/diguanylate cyclase (GGDEF) domain-containing protein {ECO:0000313|EMBL:AGA28906.1};
GN OrderedLocusNames=Sinac_4735 {ECO:0000313|EMBL:AGA28906.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA28906.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA28906.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003364; AGA28906.1; -; Genomic_DNA.
DR RefSeq; WP_015248020.1; NZ_JH621483.1.
DR AlphaFoldDB; L0DJU7; -.
DR STRING; 886293.Sinac_4735; -.
DR KEGG; saci:Sinac_4735; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR HOGENOM; CLU_264824_0_0_0; -.
DR OrthoDB; 9798833at2; -.
DR Proteomes; UP000010798; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00077; HDc; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13487; HD_5; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS51832; HD_GYP; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..317
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 372..444
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 447..499
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 680..875
FT /note="HD-GYP"
FT /evidence="ECO:0000259|PROSITE:PS51832"
FT DOMAIN 939..1055
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1119..1248
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT MOD_RES 988
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1261 AA; 141095 MW; E18EF13113C5F0A6 CRC64;
MATEKPDPVH DAVSSPGEHT PGLLRSLLIQ VIVLPLVLTA ILAVIFLTST VSLLNTSKRI
EHTNRVIDQA HLVQMLLVGM ENGLRGYLIT GLTSFLEPYK SASGAIDTSL NELARLVADE
PIQTKRVTQL QELTRRWTRD ADEMIVLKQE GVGVLPNHDL NPAGNSLIDG IRNLLSKCIA
DEKAQSNRYG YSTRALATAG LISTGIAALI LGAVLFIITR RQLFAVSSAY EIALATLRER
SSSLARSEAR FQAFMDYNPA VTFIKDDRGR YIYGNKAWVK LFGKPIEALL GRTDEELRGQ
ETAELLTKSD REVLRTQAFV KAATETCDQV DQPHHWISLK YPIDDGSGQI LIGGIAVDVT
ELRRAERDLR ISEERYTLAM RGSSAGLWDW NCDNDVLYLS PRFKELIGYE DHEVENTLKS
FVSLLHDHDC ERVMFAFSEH LTRQAPYDVE YRLRNKAGVY RWFHARGQAI WDQNGKATRM
SGSITDITAR KLAEEEVLAL NARLERRLQR LASLRRIDSA ITAGLDLPTI LNLVLDQVKA
QLHVDACDLL LLDPRTQTLE TAASWGFRTE AIGNAHVPLC RHGGGRVALE HRSMHIADLN
RSDETFVRAA EFAQEGFVTY HAVPLLAKGE VKGILEVFHR SPFEIDQEWS DLLELLASQA
AIAVENVSLY EGLRRANTEL TLAYDATIEG WSHALDLRDK ETEGHCRRVT EMTVRLARAM
GVGQDEIIQI RRGALLHDIG KMGIPDRILL KPGPLNEEEW QIMRQHPEYA RDLLSRIQFL
RPAIDIPFCH HEKWDGSGYP QGLAGEEIPL AARIFTVADI WDALSNDRPY RKAWPLGRVM
EYIASLAGTA LDPLVVETFL RLHASGPHSG LDQSATELLR TFPTKSSLVE NASIDQNHEG
ALQHSRKTTA VKPLPHTNPS ITVPVPFRFS ESPPQPGLTV LIADENQAAA HVLQQGLEAM
GHHAIVALDG HKAWQTIRQD RVQAVLADWH LPLIDGRELC RRIRGEANLA ATYVILTGER
NEDQQELGEL PADADDFLAK PIDPRDLTAR LTVALRFLRA EEMILDRTAQ AKRMYVELRD
QNERLAELVA TDPLTGLSNR RHLLEVLETQ AALTLRQKQP LSLAILDVDL FKQYNDDYGH
RAGDEVLCRI ADILRTNVRA CDLVARYGGE EFIVVMPMTA VDGSREVAER LRSAVADWAW
PLRPITSSVG VATMTPSYLD ISKLMEAADQ ALYRSKQRGR DRVTHRDELY PADDGKLLQP
A
//
