ID A0A0U5N5H3_9PROT Unreviewed; 642 AA.
AC A0A0U5N5H3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative diguanylate cyclase with PAS/PAC sensor {ECO:0000313|EMBL:CUW40129.1};
DE EC=2.7.7.65 {ECO:0000313|EMBL:CUW40129.1};
GN ORFNames=XM1_3068 {ECO:0000313|EMBL:CUW40129.1};
OS Magnetospirillum sp. XM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW40129.1, ECO:0000313|Proteomes:UP000063191};
RN [1] {ECO:0000313|Proteomes:UP000063191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang Y.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; LN997848; CUW40129.1; -; Genomic_DNA.
DR RefSeq; WP_068434456.1; NZ_LN997848.1.
DR AlphaFoldDB; A0A0U5N5H3; -.
DR STRING; 1663591.XM1_3068; -.
DR KEGG; magx:XM1_3068; -.
DR PATRIC; fig|1663591.3.peg.3028; -.
DR OrthoDB; 7333362at2; -.
DR Proteomes; UP000063191; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052621; F:diguanylate cyclase activity; IEA:UniProtKB-EC.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029095; NarX-like_N.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR46663; DIGUANYLATE CYCLASE DGCT-RELATED; 1.
DR PANTHER; PTHR46663:SF3; DIGUANYLATE CYCLASE DGCT-RELATED; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF13675; PilJ; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotidyltransferase {ECO:0000313|EMBL:CUW40129.1};
KW Transferase {ECO:0000313|EMBL:CUW40129.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..273
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 300..350
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 353..393
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 420..472
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 504..637
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
SQ SEQUENCE 642 AA; 71498 MW; D867EB792D50751C CRC64;
MSDLGERITR ELTTRYVAVL VVLGALALMS FVALTRMIVD AEGSAELVNL AGRQRMLVQR
VAFAANRLVI VDDAERAATA RLLGETLDQI EERHDRLMRG DKSPPPASVM EVFSGPPWNL
DRDLQGFIAR GRAILAEEGR PSATNPDLAA ISAGAVGSLL RSLDELTIRF QRDSESQMEE
LMKLQAVTVA VAVGLLVLSA LGVFRPMVER LQADIAERSA NAARLKESEE RLWRILEESP
VGVSVSRRRD GRVVFANSRF TDIIGMSKEE FLGSKARDHY VDDAQRQVVL ALLRRDGHLD
DVEVEFRRKN GAPFWSLLTI RSLGFADEPV NLAWIYDITE RKAAEQQIML ASKVLETVTE
AVVITDADNR IIFVNPAFTT ITEYSKDEVR GQNPSFLRSG RHEPEFYAEL WRRLSETGHW
EGEIWNRRKS GAFYAEWLSI NALRDVGGAI THFVAVFSDI THRKEDEERI WRQANYDALT
GLPNRSLFLD RLNQTVRQSK REKKRFALLF LDLDGFKAVN DTLGHAAGDV LLQQTASRMS
ECVRAADTLA RLAGDEFVLI LDGVHGRDDP ALVAGKILRL LAEPYALEAG TAHVRGSIGV
ALYPDDAEDG ASLIRRADAA MYAVKRMGKN NFLFSADLPS GD
//
