ID A0A378I3D7_9GAMM Unreviewed; 1084 AA.
AC A0A378I3D7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:STX29280.1};
DE EC=4.6.1.1 {ECO:0000313|EMBL:STX29280.1};
GN Name=cyaB {ECO:0000313|EMBL:STX29280.1};
GN ORFNames=NCTC13315_01819 {ECO:0000313|EMBL:STX29280.1};
OS Legionella beliardensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=91822 {ECO:0000313|EMBL:STX29280.1, ECO:0000313|Proteomes:UP000254968};
RN [1] {ECO:0000313|EMBL:STX29280.1, ECO:0000313|Proteomes:UP000254968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13315 {ECO:0000313|EMBL:STX29280.1,
RC ECO:0000313|Proteomes:UP000254968};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UGNV01000001; STX29280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378I3D7; -.
DR OrthoDB; 9806704at2; -.
DR Proteomes; UP000254968; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR025874; DZR.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR16305:SF28; ADENYLATE CYCLASE 10; 1.
DR PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF12773; DZR; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:STX29280.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000254968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 911..936
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..199
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1084 AA; 122152 MW; B42E4417E09154B2 CRC64;
MYCNQCHFIL QEQKFCPQCG TPTRVTKTCP NCHKECSLDS NFCGECGTSL VTQPKPIQPM
ANRKDSEAIK KHVSILFADI KESTSAISNL DPEEARNLLS PAIEKMLNAV YQYSGTIIHT
AGDGIVAIFG APQALEDHAF RACLAANFMQ TQLNALPLGL KIRVGLNSGE ILMDVVGRSE
QHLEYDITGA AVNLAARMEQ TATPGNIQIT KHTLILVKDA VEVESIGRIT IKGFSEPVEV
FKLKGIKDES NLISLKYRPT FTPFVGRNDT IKKLNELLDL AEAGQGSMVC LEAEAGQGKS
RVIYELLNNN TSLQIIYSGG FSHLCNVTLF PIVQLFRKLL DIHQDDLTEN IYDKVCPYTK
DLTVPYATDA ALSLLNSSGY SKAWEKLAPQ LKHKYLFLIG IAILTKACTN KTLVLIIEDL
HWIDNETENF ISLLLNEIHK LKILLIGTYR PSFNDTWLKN PNYHLIKLGP IPQKHLKTLA
DIILGTHPSI NSLKKDILHA CSGNPFFIQE IIDSLIADNL LTGRLGNYQL DTVNFAKRSK
LPESIFALLQ TKIDKLPAHQ KELLEIASVI GERFPYTLIA QLSTTENKVT RKNLNQLTAL
NYIYEAQLYP DLEFSFSHAL IQEVLYNTLL KKVRHQIHLK ILEFFECLPE DQKKEKIQIL
ANHAYLGQHW EKAFYYCAQA AEKTFIINAL KLTIQYSKQA IEAAAYIKDQ SSIIDSLIMV
HIDMMHAYLH LGLPEEQGPI LEKILKLSVE AKRPAVKCAV YGAYATFIMG ISCPQHAEPF
LEKANQYAKE SKRQDLMKFV DFAFLLRYTL GGDYIKGQKI GRTFLAQQAS QDFFCPEFRL
NFRYVGIIIL MINQLTSGAF LDFDRQIEFY STCFNLTEPS IYSAGITTAL GTALVQKGDF
SSTAERYLHL AIYYLIEVNF FLILPLAQAA LALLYLNTKR LKEGKEQLEK AQNSIELVGY
YLSSNYSVGF IAEGLLLSGQ LTKADKFIQN ALALSEKRNL KGNMAWLKRL SAEIALKKSK
LNPLKIKNLL EEALILTKET HMKIQEGKCH LTLAKYYQIS KHNEMAVKEE KLAYAIFKQI
GYKL
//