Non-catalytic protein 1 - Piromyces equi

Preferred order of sections

Names and origin

Protein names

Submitted name:
Non-catalytic protein 1 EMBL AAK20910.1

Gene names

Name:

ncp1 EMBL AAK20910.1

Organism

Piromyces equi EMBL AAK20910.1

Taxonomic identifier

99929 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Neocallimastigomycota › Neocallimastigomycetes › Neocallimastigales › Neocallimastigaceae › Piromyces

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Technical term	3D-structure PDB 1GWL PDB 1W8U PDB 1GWM PDB 1OH3 PDB 1W8T PDB 1W8W PDB 1W9F PDB 1W90 PDB 1WCU PDB 1W8Z PDB 1GWK
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

357 – 359

3

Beta-D-mannose binding PDB 1GWL PDB 1W8U

Sites

Binding site

379

1

Beta-D-mannose PDB 1GWL PDB 1W8U

Binding site

379

1

Glucose PDB 1OH3

Binding site

407

1

Beta-D-mannose PDB 1GWL PDB 1W8U

Binding site

411

1

Beta-D-mannose PDB 1GWL PDB 1W8U

Binding site

445

1

Beta-D-mannose PDB 1GWL PDB 1W8U

Binding site

449

1

Beta-D-mannose PDB 1GWL PDB 1W8U

Binding site

451

1

Glucose; via carbonyl oxygen PDB 1GWM PDB 1W8T

Sequences

Sequence

Length

Mass (Da)

Tools

Q9C171 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A97AA97A0C417DC6
Show »

FASTA

478

53,108

        10         20         30         40         50         60 
MFKQIGITAL LVASASAACW SESQGFKCCS SKNTPVVYTD ASGDWGVENN DWCGIPKEEA 

        70         80         90        100        110        120 
VTCFSQKLCY GCCPKRTAVS YTDADGDWGY ANGDWCGIVA EEKPTCWSEA LGYKCCQTTS 

       130        140        150        160        170        180 
KIEFTDNDGN WGFENGDWCG LQKVSGRTTT TRRTTTTRRT TTTTRRTTTT TRKVSATYSV 

       190        200        210        220        230        240 
VYETGKKLNS GFDNWGWDSK MSFKDNSLVL TADPDEYGAI SLKNLNSNYY GKGGCIYLQV 

       250        260        270        280        290        300 
KTETEGLVKV QGVRGYDETE AFNVGSFRSS SDFTEYKFEV DDEYQFDRII VQDGPASNIP 

       310        320        330        340        350        360 
IYMRYIIYST GSCDDFNPPV DTTKVPVTTT TKKSNVRATY TVIFKNASGL PNGYDNWGWG 

       370        380        390        400        410        420 
CTLSYYGGAM IINPQEGKYG AVSLKRNSGS FRGGSLRFDM KNEGKVKILV ENSEADEKFE 

       430        440        450        460        470 
VETISPSDEY VTYILDVDFD LPFDRIDFQD APGNGDRIWI KNLVHSTGSA DDFVDPIN

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References

[1]	"A novel carbohydrate-binding protein is a component of the plant cell wall-degrading complex of Piromyces equi." Freelove A.C., Bolam D.N., White P., Hazlewood G.P., Gilbert H.J. J. Biol. Chem. 276:43010-43017(2001) [PubMed: 11560933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose." Charnock S.J., Bolam D.N., Nurizzo D., Szabo L., McKie V.A., Gilbert H.J., Davies G.J. Proc. Natl. Acad. Sci. U.S.A. 99:14077-14082(2002) [PubMed: 12391332] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 335-478 IN COMPLEX WITH BETA-D-MANNOSE AND GLUCOSE.
[3]	"Ligand-mediated dimerization of a carbohydrate-binding molecule reveals a novel mechanism for protein-carbohydrate recognition." Flint J., Nurizzo D., Harding S.E., Longman E., Davies G.J., Gilbert H.J., Bolam D.N. J. Mol. Biol. 337:417-426(2004) [PubMed: 15003456] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 334-477 IN COMPLEX WITH GLUCOSE.
[4]	"Probing the mechanism of ligand recognition in family 29 carbohydrate-binding modules." Flint J., Bolam D.N., Nurizzo D., Taylor E.J., Williamson M.P., Walters C., Davies G.J., Gilbert H.J. J. Biol. Chem. 280:23718-23726(2005) [PubMed: 15784618] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 334-478 IN COMPLEX WITH BETA-D-MANNOSE AND GLUCOSE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY026754 mRNA. Translation: AAK20910.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GWK	X-ray	2.34	A/B	335-478	[»]
1GWL	X-ray	1.51	A	335-478	[»]
1GWM	X-ray	1.15	A	335-478	[»]
1OH3	X-ray	1.50	A/B	334-477	[»]
1W8T	X-ray	1.40	A	334-478	[»]
1W8U	X-ray	1.30	A	334-478	[»]
1W8W	X-ray	2.10	A/B	334-478	[»]
1W8Z	X-ray	1.85	A/B	334-478	[»]
1W90	X-ray	2.50	A/B	334-478	[»]
1W9F	X-ray	2.25	A/B	334-478	[»]
1WCU	X-ray	1.50	A	174-315	[»]

ProteinModelPortal

Q9C171.

SMR

Q9C171. Positions 17-55, 174-315, 335-478.

ModBase

Search...

Protein family/group databases

CAZy

CBM29. Carbohydrate-Binding Module Family 29.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002883. CBM10/Dockerin_dom.
IPR009034. Dockerin_dom.
IPR008979. Galactose-bd-like.
[Graphical view]

Gene3D

G3DSA:3.90.1220.10. Dockerin_CBD_5. 3 hits.

Pfam

PF02013. CBM_10. 3 hits.
[Graphical view]

SUPFAM

SSF64571. Dockering_CDD. 3 hits.
SSF49785. Gal_bind_like. 2 hits.

ProtoNet

Search...

Entry information

Entry name

Q9C171_PIREQ

Accession

Primary (citable) accession number: Q9C171

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)