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Database: UniProt
Entry: D2W1A6_NAEGR
LinkDB: D2W1A6_NAEGR
Original site: D2W1A6_NAEGR 
ID   D2W1A6_NAEGR            Unreviewed;      1060 AA.
AC   D2W1A6;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN   ORFNames=NAEGRDRAFT_82012 {ECO:0000313|EMBL:EFC37151.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC37151.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC37151.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; GG738921; EFC37151.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2W1A6; -.
DR   STRING; 5762.D2W1A6; -.
DR   EnsemblProtists; EFC37151; EFC37151; NAEGRDRAFT_82012.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_82012; -.
DR   eggNOG; KOG0618; Eukaryota.
DR   InParanoid; D2W1A6; -.
DR   OrthoDB; 5483094at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR43081:SF1; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF04069; OpuAC; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        681..710
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          729..866
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  121137 MW;  C4D2832DE477A291 CRC64;
     MESYCSLDED KMMMYSKKPD NSNDNDNSTG TQTSSNCGCI ENNNNDEEVE QQHADQQQQQ
     QKIDNDELLM EMILNNILPI NDSSDDSITA ISSSSAKLLS NNYYNTESNN NLSTEEEPSS
     STMEEEQATL LADEESANYN IISDSCSTTS SNNSNNTTCS TSTNYNHHKQ QHDDKDDNMQ
     CKYNERQRRA LALLMAIRDK YEKNLEKSSK ITTTSGGSLY SSKRMSSTRI TTNTSTTAAC
     SSFKTMLKLA LVLIVGVWCV LSFMSDVIIL DDYAASGFHH RYEYLEDDFY EFNHNNIMFV
     MAEPPGISPQ ALKEILSRES EIMRQEPIYN DFSFSSLFSM NGLHSLASKA TDFLQRGGFE
     SSADVATQCL INSPRKCDNS RKLQLIQFNW LGPTVNANVA KIVLEEMLGI CAEIVTMNVT
     HALEEMAEYG TRRSYAMLEF WSESRKFQYD KYVVNDKTIM DVGELGINAK LGWYILGFMK
     DEYDLIDEYR EYRTEKAAHY LATNDTYPLG RFIGGAKSWI TFDQQIITNL KLNLQIQYTQ
     EENAEDFLIS KIQEANDRKE PVLFYLWYPH QIFKKLSIKN VYLPPSSESC WTSYNQENQL
     IDCDYPTELL RKLVSPKLTE DMVLNSFFSK FAYESTDQID ILADIVFQEM SVVDASCKWL
     RNNTKRVAYW VSDHNDTSSS VIGIVIASLF VISLFFCTIF ITGLVLYFMY RKNLRKRSLK
     YAPRTTPFTL VFTDIQNSTL LWATASETMK SVLSIHNIIM RSNIQKYKGY EAKTAGDSFT
     VAFVDPLCAL AFCISVQKDL LLANWPSDSL LLPDMKEVRW NESLIYRGPR IRMGIHAGSD
     CNIQIDKKTQ RMEYVGNMVH IANKIEASSV GGRIYVSGAF VQAIKSRLML FDSASNSSNP
     KTSKEDVTTS ANTQYYDDSS DKGISKYVQE LNNNLIEFED LGPKQEIEIG GTKIPLFMVK
     DFSFARTSWI QQFERVLEES PVEEQKVIGQ KLDLIEEVEK FITDPGSFPA ERKSKLIYDF
     INHTSDAELN LPSWNSKYFI DLFDNVFRYI TTQHVNIKEE
//
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