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Protein

Endo-1,6-beta-D-glucanase

Gene

neg-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Partially degrades N.crassa cell wall beta-D-glucan, liberating small amounts of oligosaccharides.

Catalytic activityi

Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei225 – 2251Proton donorSequence Analysis
Active sitei321 – 3211NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.75. 3627.

Protein family/group databases

CAZyiGH30. Glycoside Hydrolase Family 30.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,6-beta-D-glucanase (EC:3.2.1.75)
Alternative name(s):
Beta-1,6-glucanase Neg1
Glucan endo-1,6-beta-glucosidase
Gene namesi
Name:neg-1
ORF Names:29E8.200, NCU04395
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 4, Linkage Group IV

Organism-specific databases

EuPathDBiFungiDB:NCU04395.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 480463Endo-1,6-beta-D-glucanasePRO_0000012180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ7M4T0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 30 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5520.
HOGENOMiHOG000159183.
InParanoidiQ7M4T0.
KOiK01201.
OMAiGANDYAK.
OrthoDBiEOG7966S1.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013780. Glyco_hydro_13_b.
IPR001139. Glyco_hydro_30.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11069. PTHR11069. 1 hit.
PfamiPF02055. Glyco_hydro_30. 1 hit.
[Graphical view]
PRINTSiPR00843. GLHYDRLASE30.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q7M4T0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYPPALTLLL TPGLVAAAIQ PQAYASSADG RYKLSSYSAP VRGTGTPGSN
60 70 80 90 100
STWKLTIDDT PSGRKQTIKG FGAAVTDSTV SVFNALPSAQ RTALLNTLMT
110 120 130 140 150
TAGANFAMMR HTIASSDLSA NPAYSYDDSN GQTDLSLSNF NLGGRGNAMA
160 170 180 190 200
SLLAEMRRLQ PGLTILGSPW SPPGWMKLNR AIQGTTVNNN LDHAYASQFA
210 220 230 240 250
QYFVKYLQAY QAKGATIDAI TIQNEPLNSR AQMPTMYIYA DEAGDLIQNN
260 270 280 290 300
IGPALRNAGL DTKIWAYDHN TDQPSYPSTV LSRAGGYVPA VAWHCYASSL
310 320 330 340 350
DWSVLTTFHN AHPGVEQYMT ECWTSAKQPT PWNWAASFTM GPLQNWASGV
360 370 380 390 400
TAWVLGTDTN DGPHLTGSDA CDKCTGLVTV DAAAGTYNLR GDYYMMAQFS
410 420 430 440 450
KFMKKGAVVM SGTGSWTYGD GSGLESVAAT NADDGSRVVV IENKFGNEIY
460 470 480
VTVEAKSGEV WSGLVYRNSV VTWVLPAAGA
Length:480
Mass (Da):51,353
Last modified:February 1, 2005 - v2
Checksum:i9183B780A3B491F8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011T → P in BAB91213 (PubMed:12162562).Curated
Sequence conflicti131 – 1311G → D in BAB91213 (PubMed:12162562).Curated
Sequence conflicti144 – 1441G → D in BAB91213 (PubMed:12162562).Curated
Sequence conflicti181 – 1811A → V in BAB91213 (PubMed:12162562).Curated
Sequence conflicti216 – 2161T → K in BAB91213 (PubMed:12162562).Curated
Sequence conflicti278 – 2781S → A in BAB91213 (PubMed:12162562).Curated
Sequence conflicti303 – 3031S → T in BAB91213 (PubMed:12162562).Curated
Sequence conflicti327 – 3271K → R in BAB91213 (PubMed:12162562).Curated
Sequence conflicti379 – 3791T → M in BAB91213 (PubMed:12162562).Curated
Sequence conflicti382 – 3821A → T in BAB91213 (PubMed:12162562).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073820 mRNA. Translation: BAB91213.1.
BX908809 Genomic DNA. Translation: CAF06053.1.
CM002239 Genomic DNA. Translation: EAA28236.1.
PIRiJC7866.
RefSeqiXP_957472.1. XM_952379.2.

Genome annotation databases

EnsemblFungiiEFNCRT00000005204; EFNCRP00000005200; EFNCRG00000005197.
GeneIDi3873626.
KEGGincr:NCU04395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073820 mRNA. Translation: BAB91213.1.
BX908809 Genomic DNA. Translation: CAF06053.1.
CM002239 Genomic DNA. Translation: EAA28236.1.
PIRiJC7866.
RefSeqiXP_957472.1. XM_952379.2.

3D structure databases

ProteinModelPortaliQ7M4T0.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH30. Glycoside Hydrolase Family 30.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000005204; EFNCRP00000005200; EFNCRG00000005197.
GeneIDi3873626.
KEGGincr:NCU04395.

Organism-specific databases

EuPathDBiFungiDB:NCU04395.

Phylogenomic databases

eggNOGiCOG5520.
HOGENOMiHOG000159183.
InParanoidiQ7M4T0.
KOiK01201.
OMAiGANDYAK.
OrthoDBiEOG7966S1.

Enzyme and pathway databases

BRENDAi3.2.1.75. 3627.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013780. Glyco_hydro_13_b.
IPR001139. Glyco_hydro_30.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11069. PTHR11069. 1 hit.
PfamiPF02055. Glyco_hydro_30. 1 hit.
[Graphical view]
PRINTSiPR00843. GLHYDRLASE30.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of an endo-1,6-beta-D-glucanase gene (neg1) from Neurospora crassa."
    Oyama S., Yamagata Y., Abe K., Nakajima T.
    Biosci. Biotechnol. Biochem. 66:1378-1381(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-35; 243-257; 323-330 AND 426-435, CHARACTERIZATION.
    Strain: ATCC 10336 / CBS 304.59 / FGSC 1757 / NBRC 6068 / IMI 53238.
  2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  3. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiNEG1_NEUCR
AccessioniPrimary (citable) accession number: Q7M4T0
Secondary accession number(s): Q7RZ78, Q8NKJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: July 22, 2015
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.