ID   Q92SD3_RHIME            Unreviewed;       623 AA.
AC   Q92SD3;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   SubName: Full=Adenylate cyclase transmembrane protein {ECO:0000313|EMBL:CAC41908.1};
DE            EC=4.6.1.1 {ECO:0000313|EMBL:CAC41908.1};
GN   Name=cyaD1 {ECO:0000313|EMBL:CAC41908.1};
GN   ORFNames=SMc02176 {ECO:0000313|EMBL:CAC41908.1};
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834 {ECO:0000313|EMBL:CAC41908.1, ECO:0000313|Proteomes:UP000001976};
RN   [1] {ECO:0000313|EMBL:CAC41908.1, ECO:0000313|Proteomes:UP000001976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000313|EMBL:CAC41908.1,
RC   ECO:0000313|Proteomes:UP000001976};
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2] {ECO:0000313|Proteomes:UP000001976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000313|Proteomes:UP000001976};
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|PROSITE-ProRule:PRU00099}.
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DR   EMBL; AL591688; CAC41908.1; -; Genomic_DNA.
DR   RefSeq; WP_010968600.1; NC_003047.1.
DR   AlphaFoldDB; Q92SD3; -.
DR   SMR; Q92SD3; -.
DR   EnsemblBacteria; CAC41908; CAC41908; SMc02176.
DR   KEGG; sme:SMc02176; -.
DR   PATRIC; fig|266834.11.peg.1847; -.
DR   eggNOG; COG2114; Bacteria.
DR   eggNOG; COG4252; Bacteria.
DR   HOGENOM; CLU_000445_85_1_5; -.
DR   OrthoDB; 9789782at2; -.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
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; IPR050697; Adenylyl/Guanylyl_Cyclase_3/4.
DR   InterPro; IPR007890; CHASE2.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR43081:SF1; 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   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CAC41908.1};
KW   Magnesium {ECO:0000256|PROSITE-ProRule:PRU00099};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001976};
KW   Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:CAC41908.1};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        319..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          436..568
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   BINDING         441
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         441
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         485
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         485
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
SQ   SEQUENCE   623 AA;  65215 MW;  8BC3D7011DD2300D CRC64;
     MHHRITPLSG GIIASLAAAL LLYLYAGTIL DTQRELFFDS LTQWVPSPRS PDIIVVDVDR
     KAYEAHGGSW DRAATADLIT RLAAAGPKTI AVDFVFSSAC DPASPANAAL AAAIGRAPVA
     LGFLAADRVL ARPRPVPPLA LRRQLAVPAQ WFIEGAETSC PAFMDRAKAA TAAFLVGDED
     ARVRRVQAYA ILGNDAYPAL GIEAGRLAAD SSTPVLGGEP AWLRLDHAII PLDESGNLRF
     PASSGEAIAA RTISAADILA GRLEKSRLAG RLVLIGSSMP SLGGLRPTAS MPLQPSVQIH
     ADIANAIMTG FVPYRGSNLP LIEAVFAFAA GVAAAYAATR LRPMASLMLG AAAVLATIAF
     AGAIYASTGW LFDAVGTSLA LAAVLIVTSA LQLARTRRAE AIARRKFSQY LPQSVVARYI
     DEPDRGRMAG EERPVTALFT DIEGFSTVSQ KLGPRELVAL LDIYFAEVNA LVSGHGGMVD
     KVVGDAVHAL FNAPEDLPGH VDKAIGCAAA IHALTEEMRR RPQFAEHGFG RTRIGIETGP
     AVLGEVGAGG KLDYTAHGDA VNLAARLQEA NKFLGTAICI GPAAAAQSKA ALRSLGRHDI
     RGFGSMELFT VAGDGLNKHL GAE
//