ID A4QAW4_CORGB Unreviewed; 501 AA.
AC A4QAW4;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Adenylate cyclase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=cgR_0397 {ECO:0000313|EMBL:BAF53361.1};
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=340322 {ECO:0000313|EMBL:BAF53361.1, ECO:0000313|Proteomes:UP000006698};
RN [1] {ECO:0000313|Proteomes:UP000006698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R {ECO:0000313|Proteomes:UP000006698};
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; AP009044; BAF53361.1; -; Genomic_DNA.
DR AlphaFoldDB; A4QAW4; -.
DR KEGG; cgt:cgR_0397; -.
DR HOGENOM; CLU_025433_2_0_11; -.
DR PhylomeDB; A4QAW4; -.
DR Proteomes; UP000006698; 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 CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF17; BLL5647 PROTEIN; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00672; HAMP; 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};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 238..290
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 322..444
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 501 AA; 54625 MW; 5D17CBEA7A420ACE CRC64;
MKWLWGTSWP LYAATVLGTN VFGALAVMLF VRFLIPQPDA SNFNAEISYL PAVGFAYLAF
AIVAGMLVTF LMFRPVLDWQ RSPEDHDRNM VRNLVMRIPI YQAILCAVVW LIGIAIATLI
SASVSTSLAL VVAFSTLMAA AIVVLLTFLE AERLVRPVAA SALARRFEDS TLEPPVSQRL
RMTWLLTLGI PVMGILLLIW GYSQGIFGSD ASGIMPAIAA LAFASLVTGY LGNRLVVSSV
VDPIRELQEA INRVRRGEND VQVDIYDGSE IGVLQAGFNE MMRGLRERQR VRDLFGRYVG
AEVAKRALEE RPTLGGEDRK VAVLFVDVIG STTFAVNHTP EEVVEALNEF FEHVVEVVHR
NKGVINKFQG DAALAIFGAP LPLSDATGHA LAAARELRAE LKDLQLKAGI GVAAGHVVAG
HIGGHARFEY TVIGDAVNQA ARLTEIAKTT PGRTVTNAST LREANEAEQA RWTLMKSVEL
RGRGQMTQIA RPIRPTLADR S
//
