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Database: UniProt
Entry: A0A1Q6W966_9GAMM
LinkDB: A0A1Q6W966_9GAMM
Original site: A0A1Q6W966_9GAMM 
ID   A0A1Q6W966_9GAMM        Unreviewed;       292 AA.
AC   A0A1Q6W966;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Adenylate/guanylate cyclase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUH10_14010 {ECO:0000313|EMBL:OLB09649.1};
OS   Gammaproteobacteria bacterium 13_2_20CM_66_19.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1805166 {ECO:0000313|EMBL:OLB09649.1, ECO:0000313|Proteomes:UP000186999};
RN   [1] {ECO:0000313|EMBL:OLB09649.1, ECO:0000313|Proteomes:UP000186999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLB09649.1}.
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DR   EMBL; MNCZ01000133; OLB09649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q6W966; -.
DR   STRING; 1805166.AUH10_14010; -.
DR   Proteomes; UP000186999; 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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
FT   DOMAIN          1..115
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          205..249
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
SQ   SEQUENCE   292 AA;  32009 MW;  8DD6CA39D6CD1FD5 CRC64;
     MLFADVVGST RLYDTMGDLR ARDMVAICID VMRGATEQRQ GTVIKTMGDE VMATFPTADA
     ALNAAAQMQQ QISTHAQLNV DGQPVAIRIG CHYGPVMLEN RDVFGAAVHT ANRMTSQAKA
     GQIVTTAATV EKLSPEWRAS CRQIDVATLK GQGSEVALYE VLWQTEDVTS MVPGIATEPR
     SGHHLRLRLQ WQDRELLVDE RHSSVTIGRA EDNDMVVKGN LISRLHARIE ISRNKFVLID
     QSTNGTFVQS ADGEESFVRR DSLQIKGQGM IGLGRLPERG SPQTIGYACE EA
//
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