ID Q92ZZ5_RHIME Unreviewed; 819 AA. AC Q92ZZ5; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 2. DT 27-MAR-2024, entry version 100. DE SubName: Full=Adenylate/guanylate cyclase {ECO:0000313|EMBL:AAK64961.2}; GN Name=cyaN {ECO:0000313|EMBL:AAK64961.2}; GN ORFNames=SMa0579 {ECO:0000313|EMBL:AAK64961.2}; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OG Plasmid pSymA {ECO:0000313|EMBL:AAK64961.2, OG ECO:0000313|Proteomes:UP000001976}. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834 {ECO:0000313|EMBL:AAK64961.2, ECO:0000313|Proteomes:UP000001976}; RN [1] {ECO:0000313|EMBL:AAK64961.2, ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|EMBL:AAK64961.2, RC ECO:0000313|Proteomes:UP000001976}; RC PLASMID=Plasmid pSymA {ECO:0000313|Proteomes:UP000001976}; RX PubMed=11481432; DOI=10.1073/pnas.161294798; RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C., RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., RA Long S.R.; RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium RT meliloti pSymA megaplasmid."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001). RN [2] {ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976}; RC PLASMID=Plasmid pSymA {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-3 family. CC {ECO:0000256|ARBA:ARBA00005381}. 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; AE006469; AAK64961.2; -; Genomic_DNA. DR RefSeq; NP_435549.2; NC_003037.1. DR RefSeq; WP_010967298.1; NC_003037.1. DR AlphaFoldDB; Q92ZZ5; -. DR EnsemblBacteria; AAK64961; AAK64961; SMa0579. DR GeneID; 61599136; -. DR KEGG; sme:SMa0579; -. DR PATRIC; fig|266834.11.peg.319; -. DR HOGENOM; CLU_340939_0_0_5; -. DR OrthoDB; 9789782at2; -. DR Proteomes; UP000001976; Plasmid pSymA. 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 CDD; cd06225; HAMP; 1. DR Gene3D; 1.20.58.920; -; 1. DR Gene3D; 6.10.340.10; -; 1. DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR038188; TorS_sensor_sf. DR PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1. DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1. DR Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF12860; PAS_7; 1. DR SMART; SM00044; CYCc; 1. DR SMART; SM00304; HAMP; 1. DR SUPFAM; SSF158472; HAMP domain-like; 1. DR SUPFAM; SSF55073; Nucleotide cyclase; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1. DR PROSITE; PS50885; HAMP; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:AAK64961.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001976}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12..34 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 359..411 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 589..724 FT /note="Guanylate cyclase" FT /evidence="ECO:0000259|PROSITE:PS50125" SQ SEQUENCE 819 AA; 90120 MW; F515B79F8C76DE6A CRC64; MFDRLGVRGR LLFAFFGISA FAVLATVGAL YAFLELSQVL ERVTERRAPS ALASLELSRH AERVAATAPA FLASTSRARH SEVSAAIGSE MARLEELLAA LKGATLSSGV VSEIEDAVVG LRRNLHALDD LVTVRLAAVA RKEELLRRLS ATTNASQRLV APGILVMNSK VPRWRAATAD AVTTPEAEAA ATRDLARAIA AYIPQQTAQR EIAAINDTLL QAAVAPTPGD LSLISFPLRR SIETLESVTP EFDEQLRKRF QQLVDQFEAL IDGQRSIPNA RNEELAVVAE GEKLVVENDK LSRKLTLAVD RLVAAAKGDI AEAGSEAATV RRYGTGVVLG SALLSLLSSV LIVWLYVDRN LLARLTGLSH SMLAIAAGDL RVPLPQTRGD EIGRMAKALR VFRDTAIEVE EKNLRTVAEA RQRLIDAIES ISEGFAFYDS EDRLLVCNSR YRDILYPGMD DTVVSGTHFE AIIRAAAERG LIEDAIGREQ EWLAERLEAH RNPTGTLLQQ RGPDRWIQIS ERRISGGGTV AVYSDITELK RREQDLSEKS VALEALSAKL AKYLAPQVYN SIFSGKQDVR IESRRKKLTI CFSDIAAFTE TTDKMESEEL TQLLNQYLTE MSKIALSFGA TIDKYVGDAI LMFFGDPETR GIREDAIACV SMALAMQERM GELGETWRSV GIEMPLRCRI GIHTDYCTVG NFGSEDRMDY TIIGGAVNLA ARLEEEAAPG SVLISYETFA QVKDLIHCEE TGRVQIRGIA YPVATYRVVD FKANLTKSCN AIRTELPHLR LEAEPELMST GEREVAITAL RETLDRLRR //