ID D2V4C8_NAEGR Unreviewed; 766 AA.
AC D2V4C8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN ORFNames=NAEGRDRAFT_63679 {ECO:0000313|EMBL:EFC48361.1};
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:EFC48361.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC48361.1,
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 -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; GG738851; EFC48361.1; -; Genomic_DNA.
DR RefSeq; XP_002681105.1; XM_002681059.1.
DR AlphaFoldDB; D2V4C8; -.
DR EnsemblProtists; EFC48361; EFC48361; NAEGRDRAFT_63679.
DR GeneID; 8849827; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_63679; -.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; D2V4C8; -.
DR OrthoDB; 3076794at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 502..624
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 85736 MW; E173EC26E73CA5E2 CRC64;
MSRTTSRTSS KGNMVTPFSI DTIEEPESTP NSSDKKSRCW MCSPKKVLSL RNIIITLISS
SIIIIAFIVW IIGFTASNSS TKILSDKLKD SSTERIVVMI EGMFTQAQEL ALSYRYFYDK
QTNHMRNFLE DRSLYEYSVK NLLFSSLITR QGLINSVNFV FESGHVVGWE CNLNACDYFI
SKQDDLRLMA YNYDFELETL ANSTTYEVPN FNASIIIPTY SIVTNAAKVD KSLRKTGMFF
PISRHVLVSS MYVTSVAIPY YGLDGNMLGT SNVVFYVDTL NAKVRSANPS IGGYILVLED
SGVIVAHSFA NLTANMEKPC YLGGNLLVQT LCSYLLPDQN SSSISDRFGN TPSSKFSLEG
FSVQRKELKF PGITWHVLIA IPDEEILGDI LIQSYNTVWI SALVLVAAII FSVITTFSLF
RTLSMLARCF TDIQNLDLDA PTIVKATSIL TAVYELRELQ NNFKSMIVTL KSIRKFVPVQ
IIRKILITGR EASLGIEDAD ATIFFLDIAG FTTMSEKMEP KALVDLASSV FESCSQSINK
HNGVIDKFIG DAVMALWNVP TRTKDHEYHA LQSAIEIQLE MEMKNVPVRI GIHSGRVKAG
NIGSVDRFSF SVLGDCPNVA SRFEGANKVY MSKIICGSST IEVALLSEER LAIKDPSLKR
IVNRRLDKLK LIGKEHPVLA YQIFLSENPK HTNGLDSRDL KMYEKGYDYL VEKQYKEALS
IFYTLGDKAP NDMVIRRKIN LCRSLVENAG IVDGKKFEGF VEITGK
//