Q9P6N7 (ASPGX_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative L-asparaginase
EC=3.5.1.1

Alternative name(s):
L-asparagine amidohydrolase

Gene names

ORF Names:

SPAC823.09c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers By similarity.
Subcellular location	Cytoplasm Ref.2.
Sequence similarities	Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	asparagine catabolic process via L-aspartate Inferred from sequence or structural similarity. Source: RefGenome protein maturation Inferred from sequence or structural similarity. Source: RefGenome
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	asparaginase activity Inferred from electronic annotation. Source: EC threonine-type endopeptidase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 316	316	Putative L-asparaginase		PRO_0000316207

Sequences

	Sequence		Length	Mass (Da)
	Q9P6N7 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: BF5B2D6369ACC3D7	FASTA	316	33,482
	10 20 30 40 50 60 MSNGLVILHA GAGLYSGQRE IQAKKTCSDA CKAAIQALKV GQSALSAAIQ AAKIMEDSPV 70 80 90 100 110 120 TNAGVGSNLN IDGKVECEAG VMDSESGLTA SVACCNCCRH PSEACLYILN KRKVMSQHGL 130 140 150 160 170 180 VPPAMLVGNG IEKLLLHSNI KLVPESHLIT ERSMKTQIKW KEILYQNPIN LSSQDTIGVI 190 200 210 220 230 240 CVDKNGRIAV VSSSGGLLLK PAGRIGSSPI PGHGFWIESF DNKSHSSTCA VATSGTGEHI 250 260 270 280 290 300 SNTCFACRSS QLLVSEDNVV SSLNKLINDF HEHPSATLYS DLQVGIIFAK VETSNSHNKR 310 IIFGLAHSSP DMVSVS

References

[1]	"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: 972 / ATCC 24843.
[2]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB90154.2.
RefSeq	NP_593836.2. NM_001019265.2.
3D structure databases
HSSP	HSSP built from PDB template 2A8I based on UniProtKB Q9H6P5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2543542.
KEGG	spo:SPAC823.09c.
NMPDR	fig|4896.1.peg.3806.
Organism-specific databases
GeneDB_Spombe	SPAC823.09c.
Phylogenomic databases
eggNOG	fuNOG08851.
GeneTree	EFGT00050000004962.
OMA	THSHENY.
OrthoDB	EOG4578FT.
Gene expression databases
ArrayExpress	Q9P6N7.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
PANTHER	PTHR10188. Peptidase_T2. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASPGX_SCHPO

Accession

Primary (citable) accession number: Q9P6N7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 22, 2009
Last modified:	December 14, 2011
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program