ID   A4TUL5_9PROT            Unreviewed;       685 AA.
AC   A4TUL5;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Adenylate/guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:CAM74322.1};
GN   ORFNames=MGR_0207 {ECO:0000313|EMBL:CAM74322.1};
OS   Magnetospirillum gryphiswaldense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM74322.1};
RN   [1] {ECO:0000313|EMBL:CAM74322.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MSR-1 {ECO:0000313|EMBL:CAM74322.1};
RX   PubMed=17449609; DOI=10.1128/JB.00119-07;
RA   Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA   Reinhardt R., Schueler D.;
RT   "Comparative genome analysis of four magnetotactic bacteria reveals a
RT   complex set of group-specific genes implicated in magnetosome
RT   biomineralization and function.";
RL   J. Bacteriol. 189:4899-4910(2007).
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DR   EMBL; CU459003; CAM74322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TUL5; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR007890; CHASE2.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   Pfam; PF05226; CHASE2; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM01080; CHASE2; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        315..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        368..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          430..562
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   685 AA;  75360 MW;  9D6C78344FE6703F CRC64;
     MGFLARRDVL LTVLLFLLAL PAQHFEWFAL LEDQANSFRH QMRIAYGDQK DLSISKDVVL
     VNVDEPFFKA YGSYPLRRTD IGAIISNIKE LGAKVVAVDM LMDFPSSYNE DPTLAAALKD
     AGNTILVAQG QFEHGKFVKL NYPTKLLDEA SVSGYTNISS NSALLTVLSR LKIHPDITKE
     RHGWPFAVQA VAMYLGQQPK LENNVLSFGD LKVPLDHGNH LYIDFPPLPS GTRFLSQSAG
     ISALEFLDIS QLDEAEKEEL GYWVKDKIVV VGDTSEVSHD WFDTPVGMVY GVEIIADTIS
     SILKGAPLRA AGTPLAAAVT SVLMMLMILL AVAFSRPVFR AVGAVLILGG FVVAVTAVYV
     HAGLVLPLSY ALAAGILSYV LIEYRAYMVE RNQKKQISKT FGQYIPAELV KEMNESGQEV
     SVGGESREMT VLFSDVRGFT TISEGLSPQD LTTLMNAFLS PMTRVIQANR GTIDKYMGDA
     IMAFWGAPLR DENHAEHAVR AALAMGKTMD ELSESFIARG WKPLKIGVGL NTGVMSVGNM
     GSDFRLAYTV MGDAVNLGSR LESLTKQYGI FTQISEYTLA QVPGLIAREV DLVKVKGKDQ
     PVRTFEPLGF DGDVDQQTLD ILARYTAALA LYRAARFSEA KAEFQALSEL EPNRMLYKIY
     IDRIAHYEAE PPPADWDGSY TAKEK
//