Reviewed, UniProtKB/Swiss-Prot P49776 (APH1_SCHPO)

Names and origin

Protein names

Recommended name:
    Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
    EC=3.6.1.17
Alternative name(s):
    Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
      Short name=Diadenosine tetraphosphatase
      Short name=Ap4A hydrolase
      Short name=Ap4Aase

Gene names

Name:	aph1
ORF Names:	SPCC4G3.02

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Asymmetrically hydrolyzes Ap4A to yield AMP and ATP.
Catalytic activity	P1,P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP.
Sequence similarities	Contains 1 HIT domain.

Ontologies

Keywords
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	adenosine catabolic process Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 182	181	Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]		PRO_0000109788
Regions
	Domain	3 – 110	108	HIT
	Motif	95 – 99	5	Histidine triad motif By similarity
Sites
	Active site	97	1	Tele-AMP-histidine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49776-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F690D863F438757D	FASTA	182	20,686
	10 20 30 40 50 60 MPKQLYFSKF PVGSQVFYRT KLSAAFVNLK PILPGHVLVI PQRAVPRLKD LTPSELTDLF 70 80 90 100 110 120 TSVRKVQQVI EKVFSASASN IGIQDGVDAG QTVPHVHVHI IPRKKADFSE NDLVYSELEK 130 140 150 160 170 180 NEGNLASLYL TGNERYAGDE RPPTSMRQAI PKDEDRKPRT LEEMEKEAQW LKGYFSEEQE KE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the Schizosaccharomyces pombe gene encoding diadenosine 5',5''-P1,P4-tetraphosphate (Ap4A) asymmetrical hydrolase: sequence similarity with the histidine triad (HIT) protein family." Huang Y., Garrison P.N., Barnes L.D. Biochem. J. 312:925-932(1995) [PubMed: 8554540] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21. Strain: ATCC 38366 / 972.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U32615 Genomic DNA. Translation: AAC49143.1. CU329672 Genomic DNA. Translation: CAB09779.1.
PIR	S64700.
RefSeq	NP_587836.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P49776.
Genome annotation databases
GeneID	2539292.
GenomeReviews	Gene locus aph1 in contig CU329672_GR.
KEGG	spo:SPCC4G3.02.
NMPDR	fig|4896.1.peg.174.
Organism-specific databases
GeneDB_Spombe	SPCC4G3.02.
Phylogenomic databases
OMA	REMERME
OrthoDB	EOG9PVQFX
Enzyme and pathway databases
BRENDA	3.6.1.17. 653.
Gene expression databases
ArrayExpress	P49776.
Family and domain databases
InterPro	IPR011146. His_triad-like_motif. IPR011151. His_triad_motif. IPR019808. Histidine_triad_CS. IPR001310. Histidine_triad_HIT. [Graphical view]
Gene3D	G3DSA:3.30.428.10. His_triad_motif. 1 hit.
PANTHER	PTHR23089. HIT. 1 hit.
Pfam	PF01230. HIT. 1 hit. [Graphical view]
PRINTS	PR00332. HISTRIAD.
PROSITE	PS00892. HIT_1. 1 hit. PS51084. HIT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APH1_SCHPO

Accession

Primary (citable) accession number: P49776

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)