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Protein

Endo-1,3(4)-beta-glucanase 1

Gene

eng1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Has a role in cell separation where it is required for the degradation of the primary septum after completion of cytokinesis.1 Publication

Catalytic activityi

Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: PomBase
  2. glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group Source: UniProtKB-EC
  3. glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group Source: UniProtKB-EC
  4. polysaccharide binding Source: PomBase

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. extracellular polysaccharide metabolic process Source: PomBase
  3. mitotic cytokinetic cell separation Source: PomBase
  4. oligosaccharide catabolic process Source: PomBase
  5. primary cell septum disassembly Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division

Protein family/group databases

CAZyiCBM52. Carbohydrate-Binding Module Family 52.
GH81. Glycoside Hydrolase Family 81.
mycoCLAPiLAM81A_SCHPO.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,3(4)-beta-glucanase 1 (EC:3.2.1.6)
Short name:
Endo-1,3-beta-glucanase 1
Short name:
Endo-1,4-beta-glucanase 1
Alternative name(s):
Laminarinase-1
Gene namesi
Name:eng1
ORF Names:SPAC821.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC821.09.

Subcellular locationi

Cell septum 2 Publications
Note: Localized in a ring-like structure around the septum.

GO - Cellular componenti

  1. cell septum surface Source: PomBase
  2. cell surface Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 1016996Endo-1,3(4)-beta-glucanase 1PRO_0000012132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9UT45.

Interactioni

Protein-protein interaction databases

BioGridi279801. 17 interactions.
STRINGi4896.SPAC821.09-1.

Structurei

3D structure databases

ProteinModelPortaliQ9UT45.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi752 – 956205Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 81 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5498.
InParanoidiQ9UT45.
OMAiDVEPHTE.
OrthoDBiEOG7MSMXB.
PhylomeDBiQ9UT45.

Family and domain databases

InterProiIPR018909. CBM_septum.
IPR005200. Endo-beta-glucanase.
[Graphical view]
PfamiPF10645. Carb_bind. 3 hits.
PF03639. Glyco_hydro_81. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UT45-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSYLRSFIF GLLTISLAQC SPILKDTKDT KFSTGSNISL KKRDTNVFDS
60 70 80 90 100
VVDTINPASY FGTVSHPVTP AGVSTDSLSS PIETNKFFDN NLLGSRTNFM
110 120 130 140 150
YADPFRYWWQ SSDTMGGICI AHTDDNQRVM DTDDTIPSYY YEPIGICSLG
160 170 180 190 200
FGASGITSNT DPIVDEIDQM SARFTFSWDS SSMQLTLTEG MAVTTAVYTN
210 220 230 240 250
AIPQIFSSTL YINDFVEVPG TSAVQKYRVT MSDNHVWLIY IYGDSLTLTE
260 270 280 290 300
STSQMLVGSN TFNGYIQIAK IPLGDGTAEA LYDTYAGVYI TGISISGYVE
310 320 330 340 350
DAVGYYSFDF TTAGDTSVEP LFFLLPHQVD TAVSGTKVTS IVLASLVSGD
360 370 380 390 400
MNAAAGNSIT FAEAIPQDIG FLPWSPTGGQ IGYSEEALEI IAEVAGTELG
410 420 430 440 450
EDFSANSNLN SMYYSGKVLA KYAMLCVTIN DILGDETSSE QCIQKLEAAF
460 470 480 490 500
ARFVDNQQIY PLTYDNTWKG VVSVAGLSGD SLADFGNSYY NDHHFHYGYF
510 520 530 540 550
VFTAAVIGHI DPDWINTGNN KEWVNFLVRD VANPSSNDPY FPKHRMIDIY
560 570 580 590 600
HGHGWASGLF ESNDGKDEES TSEDYNFFFG MKLWGQVIGD SDMEDRANII
610 620 630 640 650
LGIERNALNK YMLYADGNVQ PTSMQPNYVA GITFMNKITH TTYFGTNIEY
660 670 680 690 700
IQGIHMLPIT PISAFIRGPS FVLAEWNALL ASVIDYVDSG WRSLLYANLA
710 720 730 740 750
IAEPEESYEY FSSSDFNTDY LDDGASRAWY LAYAAGLWAN DAVYYPVSSS
760 770 780 790 800
STTTTSTSTG SVTTTSTTAT ASCTLPISYT STPTTTSISG TCNGATFDAS
810 820 830 840 850
LYVCDGTVLC PIVNGVSYQN CNGACYNPSQ YGCDNGALGP VQSSSTTSSI
860 870 880 890 900
TPTPTTTSSI TPTPTTTSTT TTAQSTGMQL CGSNYYDASS YYCDNDQLCP
910 920 930 940 950
IIDGVDYLSC NGACYNPSQY VCSDGSLSPN TVTTTKATTT FTPTPTTTTT
960 970 980 990 1000
PTPTTTSATS TNVIAQCGSA WYDSQSYICY GNILCPIING SPLLACGNAC
1010
YDSSIYGCSN GALVAA
Length:1,016
Mass (Da):109,743
Last modified:May 1, 2000 - v1
Checksum:i9240CA34D35786FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB57443.1.
AB027918 Genomic DNA. Translation: BAA87222.1. Sequence problems.
PIRiT41720.
RefSeqiNP_593162.1. NM_001018560.2.

Genome annotation databases

EnsemblFungiiSPAC821.09.1; SPAC821.09.1:pep; SPAC821.09.
GeneIDi2543379.
KEGGispo:SPAC821.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB57443.1.
AB027918 Genomic DNA. Translation: BAA87222.1. Sequence problems.
PIRiT41720.
RefSeqiNP_593162.1. NM_001018560.2.

3D structure databases

ProteinModelPortaliQ9UT45.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279801. 17 interactions.
STRINGi4896.SPAC821.09-1.

Protein family/group databases

CAZyiCBM52. Carbohydrate-Binding Module Family 52.
GH81. Glycoside Hydrolase Family 81.
mycoCLAPiLAM81A_SCHPO.

Proteomic databases

MaxQBiQ9UT45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC821.09.1; SPAC821.09.1:pep; SPAC821.09.
GeneIDi2543379.
KEGGispo:SPAC821.09.

Organism-specific databases

PomBaseiSPAC821.09.

Phylogenomic databases

eggNOGiCOG5498.
InParanoidiQ9UT45.
OMAiDVEPHTE.
OrthoDBiEOG7MSMXB.
PhylomeDBiQ9UT45.

Miscellaneous databases

NextBioi20804394.

Family and domain databases

InterProiIPR018909. CBM_septum.
IPR005200. Endo-beta-glucanase.
[Graphical view]
PfamiPF10645. Carb_bind. 3 hits.
PF03639. Glyco_hydro_81. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-168, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.
  3. "The endo-beta-1,3-glucanase eng1p is required for dissolution of the primary septum during cell separation in Schizosaccharomyces pombe."
    Martin-Cuadrado A.B., Duenas E., Sipiczki M., de Aldana C.R.V., del Rey F.
    J. Cell Sci. 116:1689-1698(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiENG1_SCHPO
AccessioniPrimary (citable) accession number: Q9UT45
Secondary accession number(s): Q9UTZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.