O94510 (AGN2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucan endo-1,3-alpha-glucosidase agn2
EC=3.2.1.59

Alternative name(s):
Endo-1,3-alpha-glucanase agn2

Gene names

Name:	agn2
ORF Names:	SPBC646.06c

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	433 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Involved in the endolysis of the ascus wall. Ref.1
Catalytic activity	Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran.
Subcellular location	Cytoplasm Ref.1.
Sequence similarities	Belongs to the glycosyl hydrolase 71 family.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	alpha-glucan catabolic process involved in ascospore release from ascus Inferred from direct assay. Source: GeneDB_Spombe cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ascospore wall Inferred from direct assay. Source: GeneDB_Spombe cell surface Inferred from direct assay. Source: GeneDB_Spombe cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	glucan endo-1,3-alpha-glucosidase activity Inferred from direct assay. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 433	433	Glucan endo-1,3-alpha-glucosidase agn2		PRO_0000119035

Sequences

	Sequence		Length	Mass (Da)
	O94510 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 7FA86E53523BC675	FASTA	433	48,066
	10 20 30 40 50 60 MASLTTALPN KAVVAHFMMG LTYNYAQSDF QNDIQNAISL GLDGFVLNFG NDSWMMSKLT 70 80 90 100 110 120 LMYNAADALN LQFLLYLNLD MSEMSTVPAS TLVTYVQTFA NRGHQARINN NVVVGTFLGQ 130 140 150 160 170 180 DINFGQSSVN QGWQVAFKNA LASAGINIFF MPTWPLDAST IYQTYPVADG FCKWNCWPYY 190 200 210 220 230 240 TSSPTSDAED LVYIQNSKAT NKKYMATVSP IFYTHFTSKN YSFFSEGLWF TRWMQLIKDQ 250 260 270 280 290 300 PNYVQVLTWN DYGESTYIGP TNYAADFPVI GSNSHEWVDS FTHAPLSYSL PLFIQMYKQN 310 320 330 340 350 360 TTGLPSNFSG ISQLYVTYRV HSKNATASSD SIPRPDNYQN SSDVISVISF AKSSYTLRVS 370 380 390 400 410 420 VNGTVLGTTN VNAGVQSANV SFIVNNTAAA GLPLFQILNG TTVIAQGYGP LNILGNNSVV 430 LYNFNFCTTR ISW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Role of the alpha-glucanase Agn1p in fission-yeast cell separation." Dekker N., Speijer D., Grun C.H., Van Den Berg M., De Haan A., Hochstenbach F. Mol. Biol. Cell 15:3903-3914(2004) [PubMed: 15194814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION. Strain: ND080.
[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: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY626902 mRNA. Translation: AAT84065.1. CU329671 Genomic DNA. Translation: CAH58744.1.
PIR	T40582.
RefSeq	XP_001713124.1. XM_001713072.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O94510.
Protein family/group databases
CAZy	GH71. Glycoside Hydrolase Family 71.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC646.06c.1; SPBC646.06c.1:pep; SPBC646.06c.
GeneID	2541122.
GenomeReviews	Gene locus agn2 in contig CU329671_GR.
KEGG	spo:SPBC646.06c.
Organism-specific databases
GeneDB_Spombe	SPBC646.06c.
Phylogenomic databases
GeneTree	EFGT00050000001577.
HOGENOM	HBG332366.
OrthoDB	EOG4PP1RP.
Gene expression databases
ArrayExpress	O94510.
Family and domain databases
InterPro	IPR005197. Glyco_hydro_71. [Graphical view]
KO	K08254.
Pfam	PF03659. Glyco_hydro_71. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGN2_SCHPO

Accession

Primary (citable) accession number: O94510
Secondary accession number(s): Q5ZEQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	November 16, 2011
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program