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Q4WVG2 (ALG3_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
EC=2.4.1.258
Alternative name(s):
Asparagine-linked glycosylation protein 6
Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Gene names
Name:alg3
ORF Names:AFUA_5G11990
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc(2)-PP-Dol By similarity.

Catalytic activity

Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the ALG3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
PRO_0000350921

Regions

Topological domain1 – 2424Lumenal Potential
Transmembrane25 – 4521Helical; Potential
Topological domain46 – 7732Cytoplasmic Potential
Transmembrane78 – 9821Helical; Potential
Topological domain99 – 1035Lumenal Potential
Transmembrane104 – 12421Helical; Potential
Topological domain125 – 14723Cytoplasmic Potential
Transmembrane148 – 17023Helical; Potential
Topological domain171 – 1788Lumenal Potential
Transmembrane179 – 20729Helical; Potential
Topological domain208 – 2125Cytoplasmic Potential
Transmembrane213 – 23119Helical; Potential
Topological domain232 – 26938Lumenal Potential
Transmembrane270 – 29021Helical; Potential
Topological domain291 – 31424Cytoplasmic Potential
Transmembrane315 – 33521Helical; Potential
Topological domain336 – 34813Lumenal Potential
Transmembrane349 – 36921Helical; Potential
Topological domain370 – 38314Cytoplasmic Potential
Transmembrane384 – 40421Helical; Potential
Topological domain405 – 41915Lumenal Potential
Compositional bias272 – 28413Poly-Leu

Sequences

Sequence LengthMass (Da)Tools
Q4WVG2 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 9EC4C705154B90C2

FASTA41947,317
        10         20         30         40         50         60 
MQLHRINTMD LKHSLRDLCM NPRHTSWAAP LLILGDAVLC ALIIWRVPYT EIDWTTYMQQ 

        70         80         90        100        110        120 
ISLYISGERD YTLIKGSTGP LVYPAAHVYI YNILYHLTDE GRDIFLGQIL FAILYLATLT 

       130        140        150        160        170        180 
VAMTCYRQAG APPYLLVPLV LSKRLHSVFM LRLFNDGIAA FAMWVSIFLF MNKKLAAGVI 

       190        200        210        220        230        240 
VWSTGVAIKM TLLLLAPAIA MVLVLSLSFG PSIRLGFLAV LIQVLFGIPF LRNNPAGYVS 

       250        260        270        280        290        300 
RAFELTRQFM FKWTVNWRFV GEELFLSRKF SLALLALHLL LLGLFVATVW LEPSGSNLPS 

       310        320        330        340        350        360 
FLQRLIQRRY RTASLSKSFV MTAMLSSLAI GLLCARSLHY QFFAYLACAT PFLLWQAGFH 

       370        380        390        400        410 
PILVYVVWAA QEWAWNAYPS TNASSLVVVL SLAAQVFGVL GNSFSRKHLD QSSQKEHMQ

« Hide

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. expand/collapse author list , 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: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAHF01000003 Genomic DNA. Translation: EAL91414.1.
RefSeqXP_753452.1. XM_748359.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ4WVG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00006300; CADAFUAP00006300; CADAFUAG00006300.
GeneID3511581.
GenomeReviewsGene locus alg3 in contig CM000173_GR.
KEGGafm:AFUA_5G11990.

Phylogenomic databases

eggNOGfuNOG07998.
GeneTreeEFGT00050000003598.
HOGENOMHBG525447.
OMAIHRVAYT.
OrthoDBEOG4MPN04.

Family and domain databases

InterProIPR007873. Glycosyltransferase_ALG3.
[Graphical view]
KOK03845.
PANTHERPTHR12646. ALG3. 1 hit.
PfamPF05208. ALG3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALG3_ASPFU
AccessionPrimary (citable) accession number: Q4WVG2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: July 5, 2005
Last modified: December 14, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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