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Protein
Submitted name:

Beta-mannase

Gene
N/A
Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Submitted name:
Beta-mannaseImported
OrganismiHypocrea jecorina (Trichoderma reesei)Imported
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 437418Sequence analysisPRO_5004322683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 56Combined sources
Glycosylationi157 – 1571N-linked (GlcNAc...)Combined sourcesCAR_5005390100
Glycosylationi184 – 1841N-linked (GlcNAc...)Combined sourcesCAR_5005390099
Disulfide bondi199 ↔ 202Combined sources
Glycosylationi277 – 2771N-linked (GlcNAc...)Combined sourcesCAR_5005390101
Disulfide bondi292 ↔ 299Combined sources
Disulfide bondi311 ↔ 361Combined sources
Glycosylationi355 – 3551N-linked (GlcNAc...)Combined sourcesCAR_5005390098

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI56996.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QNOX-ray2.00A28-371[»]
1QNPX-ray1.50A28-371[»]
1QNQX-ray1.65A28-371[»]
1QNRX-ray1.40A28-371[»]
1QNSX-ray1.50A28-371[»]
ProteinModelPortaliQ99036.
SMRiQ99036. Positions 28-371, 403-435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99036.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini400 – 43536CBM1 (fungal-type carbohydrate-binding)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 5 (cellulase A) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG410IIG3. Eukaryota.
COG3934. LUCA.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99036-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMMLSKSLLS AATAASALAA VLQPVPRASS FVTISGTQFN IDGKVGYFAG
60 70 80 90 100
TNCYWCSFLT NHADVDSTFS HISSSGLKVV RVWGFNDVNT QPSPGQIWFQ
110 120 130 140 150
KLSATGSTIN TGADGLQTLD YVVQSAEQHN LKLIIPFVNN WSDYGGINAY
160 170 180 190 200
VNAFGGNATT WYTNTAAQTQ YRKYVQAVVS RYANSTAIFA WELGNEPRCN
210 220 230 240 250
GCSTDVIVQW ATSVSQYVKS LDSNHLVTLG DEGLGLSTGD GAYPYTYGEG
260 270 280 290 300
TDFAKNVQIK SLDFGTFHLY PDSWGTNYTW GNGWIQTHAA ACLAAGKPCV
310 320 330 340 350
FEEYGAQQNP CTNEAPWQTT SLTTRGMGGD MFWQWGDTFA NGAQSNSDPY
360 370 380 390 400
TVWYNSSNWQ CLVKNHVDAI NGGTTTPPPV SSTTTTSSRT SSTPPPPGGS
410 420 430
CSPLYGQCGG SGYTGPTCCA QGTCIYSNYW YSQCLNT
Length:437
Mass (Da):47,053
Last modified:November 1, 1996 - v1
Checksum:i17513DADE12654A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25310 mRNA. Translation: AAA34208.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25310 mRNA. Translation: AAA34208.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QNOX-ray2.00A28-371[»]
1QNPX-ray1.50A28-371[»]
1QNQX-ray1.65A28-371[»]
1QNRX-ray1.40A28-371[»]
1QNSX-ray1.50A28-371[»]
ProteinModelPortaliQ99036.
SMRiQ99036. Positions 28-371, 403-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI56996.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IIG3. Eukaryota.
COG3934. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ99036.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA encoding Trichoderma reesei beta-mannanase."
    Stalbrand H., Saloheimo A., Vehmaanpera J., Penttila M.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: RutC30Imported.
  2. "The three-dimensional structure of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5."
    Sabini E., Schubert H., Murshudov G., Wilson K.S., Siika-Aho M., Penttila M.
    Acta Crystallogr. D 56:3-13(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 28-371, GLYCOSYLATION AT ASN-157; ASN-184; ASN-277 AND ASN-355, DISULFIDE BONDS.

Entry informationi

Entry nameiQ99036_HYPJE
AccessioniPrimary (citable) accession number: Q99036
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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 one 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.