P12904 (AAKG_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5'-AMP-activated protein kinase subunit gamma
Short name=AMPK gamma
Short name=AMPK subunit gamma

Alternative name(s):
Regulatory protein CAT3
Sucrose non-fermenting protein 4

Gene names

Name:	SNF4
Synonyms:	CAT3, SCI1
Ordered Locus Names:	YGL115W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.28 Ref.31
Subunit structure	AMPK is a heterotrimer of an alpha catalytic subunit (SNF1), a beta (SIP1, SIP2 or GAL83) and a gamma non-catalytic subunits (SNF4). Note=Interaction between SNF1 and SNF4 is inhibited by high levels of glucose. Ref.23 Ref.26
Subcellular location	Nucleus. Cytoplasm Ref.1 Ref.2 Ref.27.
Disruption phenotype	Leads to a decrease in the length of G1 with respect to the wild-type strain along with a smaller difference in the cell cycle length of parent and daughter cells. Ref.20
Miscellaneous	Present with 11700 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the 5'-AMP-activated protein kinase gamma subunit family. Contains 4 CBS domains.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	CBS domain Repeat
Ligand	ATP-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW peroxisome organization Inferred from mutant phenotype PubMed 1355328. Source: SGD positive regulation of gluconeogenesis Inferred from mutant phenotype Ref.2. Source: SGD protein phosphorylation Inferred from mutant phenotype Ref.22Ref.11PubMed 7913470. Source: SGD regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction Ref.11. Source: SGD replicative cell aging Inferred from mutant phenotype PubMed 10921902. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	AMP-activated protein kinase complex Inferred from direct assay Ref.23Ref.2. Source: SGD cytoplasm Inferred from direct assay Ref.27Ref.2. Source: SGD nuclear envelope lumen Inferred from direct assay Ref.27. Source: SGD plasma membrane Inferred from direct assay PubMed 12562756. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW catalytic activity Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activator activity Inferred from mutant phenotype Ref.22Ref.11. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GAL83	Q04739	4	EBI-17537,EBI-7244
SIP1	P32578	5	EBI-17537,EBI-17179
SIP2	P34164	7	EBI-17537,EBI-17187
SNF1	P06782	17	EBI-17537,EBI-17516
YCL046W	P25575	3	EBI-17537,EBI-21748

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 322

322

5'-AMP-activated protein kinase subunit gamma

PRO_0000204389

Regions

Domain

37 – 97

61

CBS 1

Domain

118 – 181

64

CBS 2

Domain

194 – 253

60

CBS 3

Domain

262 – 322

61

CBS 4

Experimental info

Mutagenesis

63

1

V → Q: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. Ref.28

Mutagenesis

136

1

C → Y: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. Ref.28

Mutagenesis

145

1

G → E: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. Ref.28

Mutagenesis

146

1

R → A or Q: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. Ref.28

Mutagenesis

166

1

T → N: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. Ref.28

Mutagenesis

177

1

N → A or Y: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. Ref.28

Mutagenesis

242

1

L → E: Decreases SNF1-activation efficiency; when associated with A-291 and E-293. Ref.29

Mutagenesis

251

1

N → I: Leads to resistance to 2-deoxyglucose. Ref.28

Mutagenesis

291

1

R → A: Decreases SNF1-activation efficiency; when associated with E-242 and E-293. Ref.29

Mutagenesis

293

1

H → A: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. Ref.28 Ref.29

Mutagenesis

293

1

H → E: Decreases SNF1-activation efficiency; when associated with E-242 and A-291. Ref.28 Ref.29

Secondary structure

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322

Helix Strand Turn

Details...

Helix

8 – 28

21

Helix

31 – 34

4

Beta strand

37 – 45

9

Helix

50 – 59

10

Beta strand

65 – 69

5

Turn

70 – 73

4

Beta strand

74 – 79

6

Helix

81 – 93

13

Helix

95 – 103

9

Helix

106 – 115

10

Helix

132 – 142

11

Beta strand

145 – 152

8

Turn

154 – 156

3

Beta strand

159 – 166

8

Helix

167 – 177

11

Helix

179 – 181

3

Helix

182 – 185

4

Helix

188 – 190

3

Helix

208 – 218

11

Beta strand

221 – 226

6

Beta strand

231 – 237

7

Helix

238 – 246

9

Helix

249 – 252

4

Helix

257 – 263

7

Beta strand

272 – 274

3

Helix

280 – 290

11

Beta strand

293 – 298

6

Beta strand

302 – 309

8

Helix

310 – 319

10

Sequences

	Sequence		Length	Mass (Da)
	P12904 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 51B387E346EE9561	FASTA	322	36,401
	10 20 30 40 50 60 MKPTQDSQEK VSIEQQLAVE SIRKFLNSKT SYDVLPVSYR LIVLDTSLLV KKSLNVLLQN 70 80 90 100 110 120 SIVSAPLWDS KTSRFAGLLT TTDFINVIQY YFSNPDKFEL VDKLQLDGLK DIERALGVDQ 130 140 150 160 170 180 LDTASIHPSR PLFEACLKML ESRSGRIPLI DQDEETHREI VVSVLTQYRI LKFVALNCRE 190 200 210 220 230 240 THFLKIPIGD LNIITQDNMK SCQMTTPVID VIQMLTQGRV SSVPIIDENG YLINVYEAYD 250 260 270 280 290 300 VLGLIKGGIY NDLSLSVGEA LMRRSDDFEG VYTCTKNDKL STIMDNIRKA RVHRFFVVDD 310 320 VGRLVGVLTL SDILKYILLG SN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of yeast regulatory gene CAT3 necessary for glucose derepression and nuclear localization of its product." Schueller H.-J., Entian K.-D. Gene 67:247-257(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[2]	"Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence for physical association of the SNF4 protein with the SNF1 protein kinase." Celenza J.L., Eng F.J., Carlson M. Mol. Cell. Biol. 9:5045-5054(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INTERACTION WITH SNF1.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Correct end of the ORF for the CDC20 gene of Saccharomyces cerevisiae." Doi A., Doi K. Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[6]	"Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase." Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., Katsis F., Witters L.A., Kemp B.E. J. Biol. Chem. 269:2361-2364(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-34 AND 316-322.
[7]	"New genes involved in carbon catabolite repression and derepression in the yeast Saccharomyces cerevisiae." Entian K.D., Zimmermann F.K. J. Bacteriol. 151:1123-1128(1982) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Genes affecting the regulation of SUC2 gene expression by glucose repression in Saccharomyces cerevisiae." Neigeborn L., Carlson M. Genetics 108:845-858(1984) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Upstream region of the SUC2 gene confers regulated expression to a heterologous gene in Saccharomyces cerevisiae." Sarokin L., Carlson M. Mol. Cell. Biol. 5:2521-2526(1985) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"High-affinity glucose transport in Saccharomyces cerevisiae is under general glucose repression control." Bisson L.F. J. Bacteriol. 170:4838-4845(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein." Celenza J.L., Carlson M. Mol. Cell. Biol. 9:5034-5044(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Absence of glucose-induced cAMP signaling in the Saccharomyces cerevisiae mutants cat1 and cat3 which are deficient in derepression of glucose-repressible proteins." Arguelles J.C., Mbonyi K., Van Aelst L., Vanhalewyn M., Jans A.W., Thevelein J.M. Arch. Microbiol. 154:199-205(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"N-terminal mutations modulate yeast SNF1 protein kinase function." Estruch F., Treitel M.A., Yang X., Carlson M. Genetics 132:639-650(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SNF1.
[14]	"Transcriptional regulation of the isocitrate lyase encoding gene in Saccharomyces cerevisiae." Fernandez E., Fernandez M., Moreno F., Rodicio R. FEBS Lett. 333:238-242(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE AMPK COMPLEX.
[15]	"Mode of action of the qcr9 and cat3 mutations in restoring the ability of Saccharomyces cerevisiae tps1 mutants to grow on glucose." Blazquez M.A., Gancedo C. Mol. Gen. Genet. 249:655-664(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Glucose regulates protein interactions within the yeast SNF1 protein kinase complex." Jiang R., Carlson M. Genes Dev. 10:3105-3115(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SNF1.
[17]	"The Snf1 protein kinase and its activating subunit, Snf4, interact with distinct domains of the Sip1/Sip2/Gal83 component in the kinase complex." Jiang R., Carlson M. Mol. Cell. Biol. 17:2099-2106(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SNF1; SIP1; SIP2 AND GAL83.
[18]	"Catabolite repression mutants of Saccharomyces cerevisiae show altered fermentative metabolism as well as cell cycle behavior in glucose-limited chemostat cultures." Aon M.A., Cortassa S. Biotechnol. Bioeng. 59:203-213(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Glucose-regulated interaction of a regulatory subunit of protein phosphatase 1 with the Snf1 protein kinase in Saccharomyces cerevisiae." Ludin K., Jiang R., Carlson M. Proc. Natl. Acad. Sci. U.S.A. 95:6245-6250(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SNF1.
[20]	"Quantitation of the effects of disruption of catabolite (de)repression genes on the cell cycle behavior of Saccharomyces cerevisiae." Aon M.A., Cortassa S. Curr. Microbiol. 38:57-60(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[21]	"Evidence for the involvement of the Glc7-Reg1 phosphatase and the Snf1-Snf4 kinase in the regulation of INO1 transcription in Saccharomyces cerevisiae." Shirra M.K., Arndt K.M. Genetics 152:73-87(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SNIF1, FUNCTION OF THE AMPK COMPLEX.
[22]	"Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit." McCartney R.R., Schmidt M.C. J. Biol. Chem. 276:36460-36466(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Purification and characterization of Snf1 kinase complexes containing a defined beta subunit composition." Nath N., McCartney R.R., Schmidt M.C. J. Biol. Chem. 277:50403-50408(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE AMPK COMPLEX, FUNCTION OF THE AMPK COMPLEX.
[24]	"The Snf1 protein kinase controls the induction of genes of the iron uptake pathway at the diauxic shift in Saccharomyces cerevisiae." Haurie V., Boucherie H., Sagliocco F. J. Biol. Chem. 278:45391-45396(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE AMPK COMPLEX.
[25]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[26]	"Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity." Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C. J. Biol. Chem. 281:26170-26180(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE AMPK COMPLEX.
[27]	"Glucose-responsive regulators of gene expression in Saccharomyces cerevisiae function at the nuclear periphery via a reverse recruitment mechanism." Sarma N.J., Haley T.M., Barbara K.E., Buford T.D., Willis K.A., Santangelo G.M. Genetics 175:1127-1135(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[28]	"Roles of the glycogen-binding domain and Snf4 in glucose inhibition of SNF1 protein kinase." Momcilovic M., Iram S.H., Liu Y., Carlson M. J. Biol. Chem. 283:19521-19529(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF VAL-63; CYS-136; GLY-145; ARG-146; THR-166; ASN-177; ASN-251 AND HIS-293.
[29]	"Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP binding." Rudolph M.J., Amodeo G.A., Iram S.H., Hong S.P., Pirino G., Carlson M., Tong L. Structure 15:65-74(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 179-322, MUTAGENESIS OF LEU-242; ARG-291 AND HIS-293.
[30]	"Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1." Amodeo G.A., Rudolph M.J., Tong L. Nature 449:492-495(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 7-321 IN COMPLEX WITH SNF1 AND SIP2.
[31]	"ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-activated protein kinase." Mayer F.V., Heath R., Underwood E., Sanders M.J., Carmena D., McCartney R.R., Leiper F.C., Xiao B., Jing C., Walker P.A., Haire L.F., Ogrodowicz R., Martin S.R., Schmidt M.C., Gamblin S.J., Carling D. Cell Metab. 14:707-714(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-322, ADP-BINDING, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M21760 Genomic DNA. Translation: AAA34472.1.
M30470 Genomic DNA. Translation: AAA35061.1.
Z72637 Genomic DNA. Translation: CAA96823.1.
D16506 Genomic DNA. Translation: BAA03958.1.
BK006941 Genomic DNA. Translation: DAA07993.1.

PIR

RGBYC3. A38906.

RefSeq

NP_011400.1. NM_001180980.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NYC	X-ray	1.90	A	179-322	[»]
2NYE	X-ray	2.50	A/B	179-322	[»]
2QLV	X-ray	2.60	C/F	7-321	[»]
3T4N	X-ray	2.30	C	2-322	[»]
3TDH	X-ray	2.30	C	2-322	[»]
3TE5	X-ray	2.50	C	2-322	[»]

ProteinModelPortal

P12904.

SMR

P12904. Positions 6-321.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-592N.

IntAct

P12904. 37 interactions.

MINT

MINT-364345.

STRING

4932.YGL115W.

Proteomic databases

PaxDb

P12904.

PeptideAtlas

P12904.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL115W; YGL115W; YGL115W.

GeneID

852763.

KEGG

sce:YGL115W.

Organism-specific databases

CYGD

YGL115w.

SGD

S000003083. SNF4.

Phylogenomic databases

eggNOG

COG0517.

GeneTree

ENSGT00390000009849.

HOGENOM

HOG000176880.

OMA

PVIDVIQ.

OrthoDB

EOG4SR15D.

Gene expression databases

ArrayExpress

P12904.

Genevestigator

P12904.

GermOnline

YGL115W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR000644. Cysta_beta_synth_core.
[Graphical view]

Pfam

PF00571. CBS. 2 hits.
[Graphical view]

SMART

SM00116. CBS. 4 hits.
[Graphical view]

PROSITE

PS51371. CBS. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12904.

NextBio

972215.

Entry information

Entry name

AAKG_YEAST

Accession

Primary (citable) accession number: P12904
Secondary accession number(s): D6VU32

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program