ID Q92WN9_RHIME Unreviewed; 637 AA. AC Q92WN9; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 02-SEP-2026, entry version 121. DE SubName: Full=Adenylate cyclase protein {ECO:0000313|EMBL:CAC48690.1}; DE EC=4.6.1.1 {ECO:0000313|EMBL:CAC48690.1}; GN Name=cyaF7 {ECO:0000313|EMBL:CAC48690.1}; GN ORFNames=SM_b20300 {ECO:0000313|EMBL:CAC48690.1}; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OG Plasmid pSymB {ECO:0000313|EMBL:CAC48690.1, OG ECO:0000313|Proteomes:UP000001976}. OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834 {ECO:0000313|EMBL:CAC48690.1, ECO:0000313|Proteomes:UP000001976}; RN [1] {ECO:0000313|EMBL:CAC48690.1, ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|EMBL:CAC48690.1, RC ECO:0000313|Proteomes:UP000001976}; RC PLASMID=Plasmid pSymB {ECO:0000313|Proteomes:UP000001976}; RX PubMed=11481431; DOI=10.1073/pnas.161294698; RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorholter F.J., RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puhler A.; RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing RT endosymbiont Sinorhizobium meliloti."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001). RN [2] {ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976}; RC PLASMID=Plasmid pSymB {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL591985; CAC48690.1; -; Genomic_DNA. DR PIR; B95878; B95878. DR RefSeq; WP_010975187.1; NC_003078.1. DR AlphaFoldDB; Q92WN9; -. DR SMR; Q92WN9; -. DR EnsemblBacteria; CAC48690; CAC48690; SM_b20300. DR KEGG; sme:SM_b20300; -. DR PATRIC; fig|266834.11.peg.5216; -. DR eggNOG; COG0457; Bacteria. DR eggNOG; COG2114; Bacteria. DR eggNOG; COG5616; Bacteria. DR HOGENOM; CLU_019981_0_0_5; -. DR OrthoDB; 9807521at2; -. DR Proteomes; UP000001976; Plasmid pSymB. DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC. DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:TreeGrafter. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR CDD; cd07302; CHD; 1. DR Gene3D; 3.40.50.10610; ABC-type transport auxiliary lipoprotein component; 1. DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR050697; Adenylyl/Guanylyl_Cyclase_3/4. DR InterPro; IPR063595; HilA-like_2nd. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1. DR PANTHER; PTHR43081:SF19; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1. DR Pfam; PF12895; ANAPC3; 1. DR Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF30449; HilA_2nd; 1. DR SMART; SM00044; CYCc; 1. DR SUPFAM; SSF55073; Nucleotide cyclase; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1. DR PROSITE; PS50005; TPR; 2. PE 3: Inferred from homology; KW Lyase {ECO:0000313|EMBL:CAC48690.1}; KW Magnesium {ECO:0000256|PROSITE-ProRule:PRU00099}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00099}; KW Plasmid {ECO:0000313|EMBL:CAC48690.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001976}; KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE- KW ProRule:PRU00339}. FT DOMAIN 7..114 FT /note="Guanylate cyclase" FT /evidence="ECO:0000259|PROSITE:PS50125" FT REPEAT 456..489 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT REPEAT 490..523 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT BINDING 12 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 12 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 13 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 56 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 56 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 637 AA; 69139 MW; B31B264170873AB0 CRC64; MERKLAAIVA GDIVGYTRLM SEDESSTYAA LRATFSGLII PSVEKHGGRT FKTTGDGFLA TFPSVNEALD AAIEIQNGFS EQPFDMRLGI NLGDVIEADG DMFGDGVNVA SRLEAMAEPG GIFVSEAVVR SADRNRSKLF YSIGRRQAKN IPEPFVVYAV RLDADEKNRR GWLGRIARGR RAALPYAIGA AALVLAAAAA QAPEVRAVGA DLAGRLARLA GGELADARPT VAVLPFDNMS GDAEQSYFAD GLTEDIIANL ARNPELQVIA RNSTFALRGQ AEDIRLIGER LGAGYVVEGS ARRAGDQLRV VAQLIDARSG AHLWSRSYDR RVEDIFAVQT ELTAEIVSHL VSYVRESEVS NAAERPTENL QAYDLVLKAR DRYKHGSKDA EALIAARALL HRALELDPGY AAARANLGMT YIVDFVQNLS GRATTTDVET GLSEARQAVR LDPNLAAGFQ VLSFGLSATG DYPGAMQAAQ RAVELNPNDP DSLMALAKAQ VRFGSYDEAV QNAERARRLH PMAPEYYTYV YGQALYAAGR LDEADEVLRE CLIRAPQEAD CLLIRTAVLS QRGDVEGAQR TMARLTEVDP EFSLASERSM RRFGDSALME QFLSRLAEAN APDVTSGFLH PRTQSRT //