ID D2W2L5_NAEGR Unreviewed; 735 AA.
AC D2W2L5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN ORFNames=NAEGRDRAFT_75632 {ECO:0000313|EMBL:EFC36669.1};
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:EFC36669.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC36669.1,
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; GG738927; EFC36669.1; -; Genomic_DNA.
DR RefSeq; XP_002669413.1; XM_002669367.1.
DR AlphaFoldDB; D2W2L5; -.
DR EnsemblProtists; EFC36669; EFC36669; NAEGRDRAFT_75632.
DR GeneID; 8859957; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_75632; -.
DR InParanoid; D2W2L5; -.
DR OrthoDB; 5490269at2759; -.
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; IPR013587; Nitrate/nitrite_sensing.
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 Pfam; PF08376; NIT; 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 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 487..611
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 735 AA; 82670 MW; 294893C3F51CE72D CRC64;
MPEPLYELKS PRQFSEGGSV HIPIVPIDNI VSYITNSMPP LQQQQPTIAT TTTTTVTTTT
TTPQQAHHQE DELETRKTLS SVVTSTSILN SSVFSTSIVG LLERIPLMVK LILIVVFAIL
SLFVFGSLLI VKSVQQIQSA YQIQSLSELS VLLADVTHRT QIERGSSSLY MGSGGKSFVL
ELPQYRNDTD NAIKAYQARK VTLLQILGDD STRIYKNSDD NLKGIDTYIA GLPVWREKIW
KLQFNVTKVA LDYYTNWNTL MIDTILMISG QSTDATFTNI QTVYNFLTAM KEFNGLKRAV
GSNGLAAGRL STANYNYFLQ IQTQSDLLQH YLDLKSNDQF HNEFINRVTS TPVYSQCKTM
ETYIVNNYQS LTLYKSTDWF NNMTLVINAM REVEDVLRNT SLDYANQLNN QAIGSLIGFV
VATFFVTCLS TTIAIVFSKT IVGPWKKILS LQEDTVHKFV PREFMTIVNK DKVTDLRHGD
FFEKELDIMF VDVRNYTGIS ESLTSQKVFK FINKYLKVVG PIIRRHNAYI DKYLGDGFAA
LFLEPGQSVH AAIAIQNALE VFNETLGPKY PSLAVGIGIV RGSVAVGLVG ESKRMDPTII
GDSVNLSARL ESLTKQYGAK ILVSRNILDT TPHTEDNFFR RIGKVAVVGK KESVELIEIL
PYEDCPKRST KDLFESATDL LYNPKMFNPE ASYAIWKQIT SIDPDDMLAH MRLDLSEQLM
EDSSGWDFCD RPTKK
//
