Reviewed, UniProtKB/Swiss-Prot Q4WID6 (ATG26_ASPFU)

Names and origin

Protein names

Recommended name:
    Sterol 3-beta-glucosyltransferase
    EC=2.4.1.173
Alternative name(s):
    Autophagy-related protein 26

Gene names

Name:	atg26
ORF Names:	AFUA_2G02220

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	1405 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside By similarity.
Catalytic activity	UDP-glucose + a sterol = UDP + a sterol 3-beta-D-glucoside.
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 28 family. Contains 2 GRAM domains. Contains 1 PH domain.
Sequence caution	The sequence EAL87319.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Autophagy Lipid synthesis Protein transport Steroid biosynthesis Sterol biosynthesis Transport
Cellular component	Cytoplasm Membrane
Domain	Repeat
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	autophagy Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro lipid glycosylation Inferred from electronic annotation. Source: InterPro protein transport Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	sterol 3-beta-glucosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1405	1405	Sterol 3-beta-glucosyltransferase		PRO_0000318040
Regions
	Domain	246 – 285	40	GRAM 1
	Domain	285 – 384	100	PH
	Domain	724 – 790	67	GRAM 2

Sequences

	Sequence		Length	Mass (Da)
	Q4WID6-1 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: EDF70E3002C995D4	FASTA	1,405	157,749
	10 20 30 40 50 60 MRPFLDDAKR RVDRKLSARR QSLSASRFLP SALPDRLKDN HDAQVDFTAP PGGSGSREGH 70 80 90 100 110 120 LQYMQQSIFG MIAAVGSRSD FHARFDESSD SDGETGQRPR KESSVRKGTS VSVNTSSLDP 130 140 150 160 170 180 SQRSSSQTDG NSEKDLGTRG RRHRRTISDH KLLRPFMSNS KHEPDPSTGD EMPTVSPPSR 190 200 210 220 230 240 PRSATPRAAP ILSRMVEAQA QFDLKASSTE RSQSSLNETG AKGPRDASVS PLSTRLMDMF 250 260 270 280 290 300 GFDKPEKVLV EYACSLLQSM LLQGYMYVTE GHICFYAYLP KKSTVAIKSG YLHKRGRKNP 310 320 330 340 350 360 KYSRYWFSLK GDVLSYYADP SNLYFPSGHV DLRYGISASL GDPKEKGREP RDFQVTTDQR 370 380 390 400 410 420 TYYFRADSAM SAKEWVKALQ KVIFRTHNEG ESVKISFPIE SIIDIEESPM VDFAETFKIR 430 440 450 460 470 480 VIEDDDSYAI DEYFFTFFNS GREAFEFLKI LINDQSLKIS SQHLSPQPDR SPRSDRTRKS 490 500 510 520 530 540 RNRWSLTSGT SRAETQRKRS ASTSHMSLAH DIVKSSPATR HQDSSDSILN SFEQATESSA 550 560 570 580 590 600 AWQSITDAAE SASQILNRSD VFQSPTIYGL DRRPSGRERR GRRNSDETAR SPSTRVNVGT 610 620 630 640 650 660 GQQIDELDRR TDGNTSGREA RDTTSESDQY TQDPTKSFSG APSLNELVKA GVYPLQRAAG 670 680 690 700 710 720 LAEYLRTRSK QMSNLLASES MGYIEKVSGM WTGGRKHYGE AEDVLPDDQD VDPEDKEDGC 730 740 750 760 770 780 NYGDRFRAHF ALPPTEKLQA TYFAYLHRVL PLYGKIYVSQ KKLCFRSLIP GTRTKMILPL 790 800 810 820 830 840 RDIENVEKEK GFRFGYHGLV IIIRGHEELF FEFRTSDARD DCAVTLHQHL EAVKFMAESG 850 860 870 880 890 900 LLAEQEQNES EAAMTEHRML QEARYYDYGE NDLRPLNESS ELHPIFDDPR ASIVNFKPAE 910 920 930 940 950 960 SLRITCLTIG SRGDVQPYIA LCKGLLAEGH RPKIATHAEF EPWVRKHGID FAPVEGDPAE 970 980 990 1000 1010 1020 LMRICVENGM FTYSFLKEAS QKFRGWIDDL LSSAWASCQD SDLLIESPSA MAGIHIAEAL 1030 1040 1050 1060 1070 1080 RIPYFRAFTM PWSRTRAYPH AFAVPEHRMG GAYNYITYVM FDNVFWKAIA GQVNRWRKNE 1090 1100 1110 1120 1130 1140 LGLKATTLDK MQPNKVPFLY NYSPSVVPPP LDYPDWIRIT GYWFLNEGSD WTPPTALSEF 1150 1160 1170 1180 1190 1200 IHRAREDGKK IVYIGFGSIV VSDPSALTKT VIESVLKADV RCILSKGWSD RLGDPASAKP 1210 1220 1230 1240 1250 1260 EVPLPSEIHQ IQAAPHDWLF SHIDAAVHHG GAGTTGASLR AGVPTIIKPF FGDQFFFGSR 1270 1280 1290 1300 1310 1320 VEDLGVGICM KKLNVSVFSR ALWEATHSER MIIRAQDLGA RIRSEDGVAT AIQAIYRDLE 1330 1340 1350 1360 1370 1380 YAKTLARQRS IASSTPFSPT PSAKTAAEQD ADDDVEDSEE WTFVGDDTDV EMSRRLRDRA 1390 1400 ISDADMLPDR LLANSVPGDS GPGRN

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000008 Genomic DNA. Translation: EAL87319.1. Sequence problems.
RefSeq	XP_749357.1.
3D structure databases
SMR	Q4WID6. Positions 283-394.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4WID6.
Genome annotation databases
GeneID	3507158.
KEGG	afm:AFUA_2G02220.
Phylogenomic databases
eggNOG	fuNOG07241.
HOGENOM	HBG332791.
OrthoDB	EOG9908S8.
PhylomeDB	Q4WID6.
Enzyme and pathway databases
BRENDA	2.4.1.173. 18841.
Family and domain databases
InterPro	IPR004276. Glyco_trans_28. IPR004182. GRAM. IPR011993. PH_type. IPR001849. Pleckstrin_homology. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF03033. Glyco_transf_28. 1 hit. PF02893. GRAM. 2 hits. PF00169. PH. 1 hit. [Graphical view]
SMART	SM00568. GRAM. 2 hits. SM00233. PH. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATG26_ASPFU

Accession

Primary (citable) accession number: Q4WID6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	February 9, 2010
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)