Reviewed, UniProtKB/Swiss-Prot Q9V3R6 (ADAT1_DROME)

Names and origin

Protein names

Recommended name:
    tRNA-specific adenosine deaminase 1
    EC=3.5.4.-
Alternative name(s):
    dADAT1
    tRNA-specific adenosine-37 deaminase

Gene names

Name:	adat
ORF Names:	CG16889

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Specifically deaminates adenosine-37 to inosine in tRNA-Ala. Ref.1
Cofactor	Binds 1 inositol hexakisphosphate (IP6) per subunit By similarity.
Tissue specificity	Widely expressed in early embryos, and later concentrates in the central nervous system. Ref.1
Developmental stage	Expressed both maternally and zygotically. Ref.1
Sequence similarities	Belongs to the ADAT1 family. Contains 1 A to I editase domain.

Ontologies

Keywords
Biological process	tRNA processing
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tRNA modification Ref.1 Inferred from direct assay. Source: FlyBase
Molecular function	RNA binding Ref.1 Inferred from mutant phenotype. Source: UniProtKB tRNA-specific adenosine deaminase activity Ref.1 Inferred from direct assay. Source: FlyBase zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	tRNA-specific adenosine deaminase 1		PRO_0000287651
Regions
	Domain	54 – 388	335	A to I editase
Sites
	Active site	80	1	Proton donor By similarity
	Metal binding	78	1	Zinc By similarity
	Metal binding	127	1	Zinc By similarity
	Metal binding	191	1	Zinc By similarity
	Binding site	84	1	Inositol hexakisphosphate By similarity
	Binding site	85	1	Inositol hexakisphosphate By similarity
	Binding site	194	1	Inositol hexakisphosphate By similarity
	Binding site	197	1	Inositol hexakisphosphate By similarity
	Binding site	320	1	Inositol hexakisphosphate By similarity
	Binding site	357	1	Inositol hexakisphosphate By similarity
	Binding site	381	1	Inositol hexakisphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9V3R6-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7EBB8124F1EF9828	FASTA	394	45,350
	10 20 30 40 50 60 MCDNKKPTVK EIAELCLKKF ESLPKTGKPT ANQWTILAGI VEFNRNTEAC QLVSLGCGTK 70 80 90 100 110 120 CIGESKLCPN GLILNDSHAE VLARRGFLRF LYQELKQDRI FHWNSTLSTY DMDEHVEFHF 130 140 150 160 170 180 LSTQTPCGDA CILEEEQPAA RAKRQRLDED SEMVYTGAKL ISDLSDDPML QTPGALRTKP 190 200 210 220 230 240 GRGERTLSMS CSDKIARWNV IGVQGALLDV LISKPIYFSS LNFCCDDAQL ESLERAIFKR 250 260 270 280 290 300 FDCRTFKHTR FQPQRPQINI DPGIRFEFSQ RSDWQPSPNG LIWSQVPEEL RPYEISVNGK 310 320 330 340 350 360 RQGVTKKKMK TSQAALAISK YKLFLTFLEL VKFNPKLSEM FDQQLSDPER IAYASCKDLA 370 380 390 RDYQFAWREI KEKYFLQWTK KPHELLDFNP MSNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The properties of a tRNA-specific adenosine deaminase from Drosophila melanogaster support an evolutionary link between pre-mRNA editing and tRNA modification." Keegan L.P., Gerber A.P., Brindle J., Leemans R., Gallo A., Keller W., O'Connell M.A. Mol. Cell. Biol. 20:825-833(2000) [PubMed: 10629039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Oregon-R.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF192530 mRNA. Translation: AAF06773.1. AE014134 Genomic DNA. Translation: AAF53333.1.
RefSeq	NP_609676.1.
UniGene	Dm.12524
3D structure databases
HSSP	HSSP built from PDB template 1ZY7 based on UniProtKB P78563.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9V3R6. 5 interactions.
STRING	Q9V3R6.
Proteomic databases
PRIDE	Q9V3R6.
Genome annotation databases
Ensembl	FBtr0080573; FBpp0080150; FBgn0028658; Drosophila melanogaster. [Genome view]
GeneID	34787.
KEGG	dme:Dmel_CG16889.
NMPDR	fig|7227.3.peg.2320.
UCSC	CG16889-RA. d. melanogaster.
Organism-specific databases
CTD	34787.
FlyBase	FBgn0028658. adat.
Phylogenomic databases
HOGENOM	Q9V3R6.
OMA	NQTHPVN
OrthoDB	EOG9HMJGR
Family and domain databases
InterPro	IPR002466. A_deamin. [Graphical view]
Pfam	PF02137. A_deamin. 1 hit. [Graphical view]
SMART	SM00552. ADEAMc. 1 hit. [Graphical view]
PROSITE	PS50141. A_DEAMIN_EDITASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	790221.

Entry information

Entry name

ADAT1_DROME

Accession

Primary (citable) accession number: Q9V3R6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	May 1, 2000
Last modified:	November 24, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project