ID A0A1Q3H4A5_9BACT Unreviewed; 559 AA.
AC A0A1Q3H4A5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Guanylate cyclase domain-containing protein {ECO:0000259|PROSITE:PS50125};
GN ORFNames=BKI52_05160 {ECO:0000313|EMBL:OJJ23740.1};
OS marine bacterium AO1-C.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae.
OX NCBI_TaxID=1905359 {ECO:0000313|EMBL:OJJ23740.1, ECO:0000313|Proteomes:UP000186474};
RN [1] {ECO:0000313|EMBL:OJJ23740.1, ECO:0000313|Proteomes:UP000186474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-C {ECO:0000313|EMBL:OJJ23740.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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:OJJ23740.1}.
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; MLAY01000001; OJJ23740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3H4A5; -.
DR STRING; 1905359.BKI52_05160; -.
DR Proteomes; UP000186474; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 6.10.250.780; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186474};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 354..485
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 178..268
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 559 AA; 63348 MW; 5AFE71245B835C21 CRC64;
MRRLIAIILF YFGCVGFSWG QNVDSLKRLL NPNQNTVKQV NALNALSKIL KTKNTKASIN
YANQALTTAI KIKFKEGMAD SYANIGYAQA FLADDQDDPT SGYEKAASSF REAFDIYDAL
YKSNRMNQSK MLQFLDGGVI TVYRDLADIY YSEKKNYQKA SDIYKVLFEK FGEYSSEVKE
ANLVVSRTKL QNQQLRQKLL LQQRQALENE LQVEKIQGEK DSLALLDQRR KTEQAEREKA
YQALQNRVAQ SKKEKELTAN KLKLAEQNAE LDRSKLLTNA FIVGFALVFV IIGVLFYSYR
RQKRVNQIIS RQQAEIVKEK ERSETLLLNI LPSQVANELK EKGKASIQQY DKVSVLFTDF
KGFTSIAEKI SPVELVRELE SCFLKFDEII EKYNIEKIKT IGDAYMAAGG IPTANHTNPL
DVILAGLEMQ YFMNDLKATK AAAGEPYWEL RLGINTGKLI AGVIGKKKFA YDVWGDTVNT
ASRMESSGEV GKVNISGKTY SLIKDFFECE HRGKVSAKGK GEIDMYFVHR IKPELSADDR
GLQPNEQFKS LRNGVTITS
//
