ID D2V1C3_NAEGR Unreviewed; 756 AA.
AC D2V1C3;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC49281.1};
GN ORFNames=NAEGRDRAFT_62835 {ECO:0000313|EMBL:EFC49281.1};
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:EFC49281.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC49281.1,
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; GG738848; EFC49281.1; -; Genomic_DNA.
DR RefSeq; XP_002682025.1; XM_002681979.1.
DR AlphaFoldDB; D2V1C3; -.
DR EnsemblProtists; EFC49281; EFC49281; NAEGRDRAFT_62835.
DR GeneID; 8855223; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_62835; -.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; D2V1C3; -.
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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 491..613
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 756 AA; 85065 MW; 969909516F0F3602 CRC64;
MTNMVTPMHH SMDQFAFDED PSLNDSQRKK RKISARKVLS LRNIIITLIA LFMVIIAFVV
WIIGFTASNS STRLLSERLK ESSSERVVVM IESMFYQAQD LALTFKNFYD QQSDYMSNFF
VNRTIYERAV KSMLFSSLIT RQSAMNSVNF VFNTGHIVGW ECYNLGCNYI ISRESDLTMM
AYNYDFKAGK LKDTTVYQVP GFNAATIIPT YKVVTDPIYK NSTVRGTGMF FPISRHVVFV
DTYVTSIALP YYDTDEKLVG AANVVFYTDT LNSKVREANP SQEGYIIVIE DSGVIVAHSF
ANQTAIMEKP CYLEGNAAVK SLCSYFFPPN VTTISSRFPS STQKFSLDGL SIQRTETSFP
GVKWHIFIAI PDKEILGDIV VQSYNTIWIS ALVLVLAIIV SVLTTFSLMR TLSQLARCFD
AIRNLDLDAS TIVKATSGRT YVYELGELQN NFKSMIVTLK SIRKFVPVQI IKKILITGKE
ASLGIQDADA TIFFLDIAGF TTLSEKMEPK ALVDMICSVF ETCSQAISRR DGVIDKFIGD
AVMALWNVPT KTPDHEYHAI QAAIEIQTEM EKKNIPIRIG IHSGRVKAGN IGSVDRFSFS
VVGDGANLAS RLEGANKAYS SKIICSSSTM EVALISEERL VLHDPNINRL MYRRLDKLKV
KGKEQPVLTY QVFLSSHPKH TNDLDARDVK LYEKAFDLLM KNQYKEALAI FYTLIDKAPK
DVVLEKKIEL CKSLVENGGF YDDGKKFDGS IEFTEK
//
