ID B9NMH5_9RHOB Unreviewed; 561 AA.
AC B9NMH5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Adenylate/guanylate cyclase {ECO:0000313|EMBL:EEE36369.1};
GN ORFNames=RKLH11_202 {ECO:0000313|EMBL:EEE36369.1};
OS Rhodobacteraceae bacterium KLH11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE36369.1, ECO:0000313|Proteomes:UP000005135};
RN [1] {ECO:0000313|Proteomes:UP000005135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX PubMed=21742885; DOI=10.1128/jb.05556-11;
RA Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL J. Bacteriol. 193:5011-5012(2011).
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DR EMBL; DS999531; EEE36369.1; -; Genomic_DNA.
DR AlphaFoldDB; B9NMH5; -.
DR STRING; 467661.RKLH11_202; -.
DR eggNOG; COG0633; Bacteria.
DR eggNOG; COG2114; Bacteria.
DR HOGENOM; CLU_492377_0_0_5; -.
DR OrthoDB; 341967at2; -.
DR Proteomes; UP000005135; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
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 CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF17; BLL5647 PROTEIN; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005135};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..350
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 367..498
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 561 AA; 61658 MW; D56A585C61DC6B74 CRC64;
MDNALWRGGW MSQLRIASGL VLFVFAFFHF INIGLGLFHT DLLHNVQDGR QAISRHGIGS
FILYAALLIH AGLALISIAQ RRTLRMPFSV ALQVVLGLLI PLQLIAHLVH TRYAHEIFGV
NDEMGYIIIL MWPSTAIWMQ SLLLLLVWIH GCIGLHLWLR LTRWWRRFEP YLIGIAVFVP
GFALAGLLSE GRRIWADFAD PGLRDQYIEH YNWPSPEAFQ TLLTVEDYTL MVFWAALATT
ALIYIGRKLW RRRHSVRVRY VDGPEIVSEK GMTLLEMSRA NGIPHTALCG GKGRCTTCRV
VVENGADQLH PPSEVEARSL KAVGAAPGTR LACQIRPTDP LSVVRVFRPD GTRDRGHASQ
GQERQLAVLF LDMRGFTART AGQLPYDIVF LLNRFFDAIV PAITAQGGVV DKYMGDGLLA
MFETADAGSS ARAGLNAAIG VGRALEQFNQ QLETEGSAPV RIGMGLHLGD LVLGEIGAAK
HAPRTIIGDA VNVASRLESE TKALGVELLV SETVLGASGL QCQPDALREF KLRGVSEPVP
ALPVKHASEL EAQMTPLGQI A
//
