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Database: UniProt
Entry: A0A1Y2K7P1_9PROT
LinkDB: A0A1Y2K7P1_9PROT
Original site: A0A1Y2K7P1_9PROT 
ID   A0A1Y2K7P1_9PROT        Unreviewed;       694 AA.
AC   A0A1Y2K7P1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Putative adenylate/guanylate cyclase {ECO:0000313|EMBL:OSM06205.1};
GN   ORFNames=MAIT1_01184 {ECO:0000313|EMBL:OSM06205.1};
OS   Magnetofaba australis IT-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetofaba.
OX   NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM06205.1, ECO:0000313|Proteomes:UP000194003};
RN   [1] {ECO:0000313|EMBL:OSM06205.1, ECO:0000313|Proteomes:UP000194003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT-1 {ECO:0000313|EMBL:OSM06205.1,
RC   ECO:0000313|Proteomes:UP000194003};
RX   PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA   Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA   Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT   "Combined genomic and structural analyses of a cultured magnetotactic
RT   bacterium reveals its niche adaptation to a dynamic environment.";
RL   BMC Genomics 17:726-726(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:OSM06205.1}.
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DR   EMBL; LVJN01000016; OSM06205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2K7P1; -.
DR   STRING; 1434232.MAIT1_01184; -.
DR   Proteomes; UP000194003; Unassembled WGS sequence.
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   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR007890; CHASE2.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   PANTHER; PTHR43081:SF17; BLL5647 PROTEIN; 1.
DR   Pfam; PF05226; CHASE2; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM01080; CHASE2; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194003};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        324..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          438..570
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   694 AA;  77227 MW;  8899E31A03BE3EA7 CRC64;
     MQWTLEDVID PRIVIVNIDD ASLREEGRWP WSRSRIGELT TTLFDHYGVA AIGFDIIFAE
     PDPNAAGGAR ILRQLGNPTL EQAPWLNAFR SLLDANDPDR QFADALRDRP VALGFYFKGN
     DDGGARSMGV LPEPIIDAGL LRSAGITLPP MLSPNHFGGI VPTLLVDGVE AGFLDNPLVD
     DDGVFRKTPL LQRSGDKIYP TLALSLARML IGSGYPLSLD EQGRWIKIGP LSIPLLENAA
     TYIPFLGPVG SFRYVSAADV LNQRTSHEIL QGTVVLVGAT AAGLMDMRST PVASVYPGVE
     THANLLSGIL DGRNPYVPEE YKKSEVWALL VIGVFLGLLI PHAQPWKIVV MAIVVLGLWE
     GLALAFWQWD RAIIPMAAPL AMVLMLVISH LLFGLIVESR QRRQITKWFG QYIPPELVAE
     MSENEANYTL DGENREMTVL FADVRRFTDI AESMGPSELT QLMNAYLTPM SAIIYQNRGA
     IDKYMGDAIM AFWGAPLENA QHAATAIKTG LEMLEQIEQL HEPFAQRGWP QLKVGIGLGT
     GRMHVGNMGS EYRMAYTVMG DAVNLGSRLE GLTSVYKIPF IVSQTTRDAA PEYLYRKIDR
     VRVKGRTEPV TIYQPIGLTE ECDEQTRHLI TRHEQALSAY QSRQFEAAEE LWRALKQDDE
     RLSAFYQIFL TRIEMLRLEP PPADWSGVQN FSHK
//
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