ID W6K8P2_MAGSQ Unreviewed; 317 AA.
AC W6K8P2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Adenylate cyclase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGMAQ_1682 {ECO:0000313|EMBL:CCQ73590.1};
OS Magnetospira sp. (strain QH-2) (Marine magnetic spirillum (strain QH-2)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Magnetospira.
OX NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ73590.1, ECO:0000313|Proteomes:UP000032733};
RN [1] {ECO:0000313|EMBL:CCQ73590.1, ECO:0000313|Proteomes:UP000032733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-2 {ECO:0000313|EMBL:CCQ73590.1,
RC ECO:0000313|Proteomes:UP000032733};
RX PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., Murat D.,
RA Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., Pradel N.,
RA Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., Coutinho P.M.,
RA Li Y., Xiao T., Medigue C., Barbe V., Pignol D., Talla E., Wu L.F.;
RT "Comparative genomic analysis provides insights into the evolution and
RT niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL Environ. Microbiol. 16:525-544(2014).
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DR EMBL; FO538765; CCQ73590.1; -; Genomic_DNA.
DR RefSeq; WP_052716237.1; NZ_FO538765.1.
DR AlphaFoldDB; W6K8P2; -.
DR STRING; 1288970.MGMAQ_1682; -.
DR KEGG; magq:MGMAQ_1682; -.
DR HOGENOM; CLU_071498_0_0_5; -.
DR OrthoDB; 9762462at2; -.
DR Proteomes; UP000032733; Chromosome.
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 PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 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; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000032733}.
FT DOMAIN 1..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 120..255
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 317 AA; 33891 MW; FDB8AE11E0C9CCDF CRC64;
MDLYIDGQAI PLLESEGDTL LRLSLAAGIP HQHACGGEAR CSTCRVRVLE GADLLAPPTA
AERKLAKSLA FPPEIRLACQ CRPRVKGKGR VSVQRLIRDT LDAENLLAID EAGVREMNLV
ILFSDLRGFT SFAEPLLPYD TVHILNRYFR VMGDAVLNHH GVIDKYMGDG LMALFGVEGE
ACEQAAENGL RAGLAMLEAL ESFNGYLVDN GYRGEPLAMG VGIHAGTVVY GDMGHPGQVS
RTAIGDPVNV ASRLESATKE AGHPILVSED FKRLLNGRLH SAGELEVALK GKSEPTLASK
AIGLAGSPRC QPDQVSS
//
