ID A0A0W0ZUA7_9GAMM Unreviewed; 431 AA.
AC A0A0W0ZUA7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Guanylate/adenylate cyclase {ECO:0000313|EMBL:KTD72518.1};
GN ORFNames=Ltuc_0365 {ECO:0000313|EMBL:KTD72518.1};
OS Legionella tucsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD72518.1, ECO:0000313|Proteomes:UP000054693};
RN [1] {ECO:0000313|EMBL:KTD72518.1, ECO:0000313|Proteomes:UP000054693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD72518.1,
RC ECO:0000313|Proteomes:UP000054693};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD72518.1}.
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; LNZA01000001; KTD72518.1; -; Genomic_DNA.
DR RefSeq; WP_058519658.1; NZ_LNZA01000001.1.
DR AlphaFoldDB; A0A0W0ZUA7; -.
DR STRING; 40335.Ltuc_0365; -.
DR PATRIC; fig|40335.7.peg.381; -.
DR OrthoDB; 9806704at2; -.
DR Proteomes; UP000054693; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00072; Response_reg; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000054693}.
FT DOMAIN 7..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 191..316
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 125..156
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 431 AA; 48391 MW; BF5936ECEBBDA19F CRC64;
MEKENPVIMI VDDSATMRLI TCDALTKVGF NVIQAENGEV ALSLLKTTKP DAILLDVEMP
GLNGFEVCAE IRKLPDLHYL PIMMVTGLDD YESVNKAFQV GATDFTTKPI NPTLLGYRVR
YMVRTNSYFQ DLQIAEQRVR ALNEELINKL VEIQQNAIAV ARFVPQDFLK VLNRKNISDI
KLGDCVEKVM TVLFLDIKSF TTMAERLSPV DIFNLFNTLM SYLDPAIFKN SGLIDKYIGD
AIMALFNNAD DAVIAALDML EALKDFNATR MRDNLSPINV GIGINTGNLI VGTVGFEKRM
DCSVISDAVN TASRLETLTR TFNIELIIGE ETYEQLKQKD GYDMRFLGLT TVKGKSLPIK
IYEVFNHNPP IEVQLKKDSA SIFATALDHY EAKQLDEASS LFEQIIISNP NDLPAQYFLQ
QCKEKKIRKP G
//
