ID Q6FCE8_ACIAD Unreviewed; 485 AA. AC Q6FCE8; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 104. DE SubName: Full=Putative adenylate or guanylate cyclase {ECO:0000313|EMBL:CAG68263.1}; DE EC=4.6.1.- {ECO:0000313|EMBL:CAG68263.1}; GN OrderedLocusNames=ACIAD1397 {ECO:0000313|EMBL:CAG68263.1}; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter. OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68263.1, ECO:0000313|Proteomes:UP000000430}; RN [1] {ECO:0000313|EMBL:CAG68263.1, ECO:0000313|Proteomes:UP000000430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430}; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, RT a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). 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; CR543861; CAG68263.1; -; Genomic_DNA. DR AlphaFoldDB; Q6FCE8; -. DR STRING; 202950.GCA_001485005_01154; -. DR KEGG; aci:ACIAD1397; -. DR eggNOG; COG2114; Bacteria. DR HOGENOM; CLU_047397_0_0_6; -. DR OrthoDB; 9806704at2; -. DR BioCyc; ASP62977:ACIAD_RS06450-MONOMER; -. DR Proteomes; UP000000430; Chromosome. 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 Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1. DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1. DR InterPro; IPR001054; A/G_cyclase. 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; PF00211; Guanylate_cyc; 1. DR SMART; SM00044; CYCc; 1. DR SUPFAM; SSF55073; Nucleotide cyclase; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1. PE 4: Predicted; KW Lyase {ECO:0000313|EMBL:CAG68263.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000430}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20..37 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 75..108 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 114..139 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 151..169 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 227..361 FT /note="Guanylate cyclase" FT /evidence="ECO:0000259|PROSITE:PS50125" SQ SEQUENCE 485 AA; 56409 MW; 6A634F92AD492FAB CRC64; MLTRFIERGP QQFIYFHRMM GYFILSLLIV IYSFTSAHSQ YQIYVPIFIV ILVLLIPRLN RVFEAKFDKK ITRSIFFLID TFVVSIVLAG VHLSLVLTFI ILFAWIYSAI NSRIPFVVMS LAVLSGIACF YFHTFFVFGF QGYLANTSQE LTVISLICLI IFISMGNYYQ HIYIERIKQL RQDYYNQMTR YMTFANQLSR YAPLQLWQSI MRGEAEAKIE YKRKKLTVFF SDIQGFTELS ESLIPDDLAF LLNDYLSHMT EIANQYEATI DKFMGDAILI FFGDPNSQGV QQDAASCVEM AIAMRQQMKL LRERWKKMGY PALNIRMGVS TGYCHVGNYG ATYRMAYTIV GRDVNLAARL QYAAEVDEIL ISDETYQLIK DQFLCAPKAP IYLKGIQGAV KTWQVLEKYT GNQEDLQQWF DYEYKGFHLL LNLEEVQRFE YSELVEVMEK MIHRIQAQQA MTNDKGIVKL SMKDEVKLAQ GNLKS //