ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P29031

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CHIB_POPTR
Primary accession number P29031
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on February 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 66)
Name and origin of the protein
Protein name Acidic endochitinase WIN6.2B [Precursor]
Synonym EC 3.2.1.14
Gene name None
From
Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) [TaxID: 3694] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Malpighiales; Salicaceae; Saliceae; Populus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00037049; PubMed=1912489 [NCBI, ExPASy, EBI, Israel, Japan]
Davis J.M., Clarke H.R.G., Bradshaw H.D. Jr., Gordon M.P.;
"Populus chitinase genes: structure, organization, and similarity of translated sequences to herbaceous plant chitinases.";
Plant Mol. Biol. 17:631-639(1991).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X59995; CAA42612.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P02877; 1HEV. [HSSP ENTRY / PDB]
ModBase P29031.
Ontologies
GO
GO:0008061; Molecular function: chitin binding (inferred from electronic annotation from InterPro).
GO:0004568; Molecular function: chitinase activity (inferred from electronic annotation from InterPro).
GO:0016998; Biological process: cell wall catabolic process (inferred from electronic annotation from InterPro).
GO:0006032; Biological process: chitin catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001002; Chitin_bd_1.
IPR016283; Glyco_hydro_19.
IPR000726; Glyco_hydro_19_cat.
Graphical view of domain structure.
Gene3D G3DSA:3.30.60.10; Chitin_bd_1; 1.
PANTHER PTHR22595; Glyco_hydro_19_cat; 1.
Pfam PF00187; Chitin_bind_1; 1.
PF00182; Glyco_hydro_19; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001060; Endochitinase; 1.
PRINTS PR00451; CHITINBINDNG.
ProDom PD000609; Chitin_binding_1; 1.
PD354900; Glyco_hydro_19; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00270; ChtBD1; 1.
SMART graphical view of domain structure.
PROSITE PS00026; CHIT_BIND_I_1; 1.
PS50941; CHIT_BIND_I_2; 1.
PS00773; CHITINASE_19_1; 1.
PS00774; CHITINASE_19_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P29031.
ProtoNet P29031.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     By similarity. 
CHAIN   22   303  282     Acidic endochitinase WIN6.2B. PRO_0000005317
DOMAIN   22    62  41     Chitin-binding type-1. 
REGION   82   303  222     Chitinase. 
DISULFID   24    39        By similarity. 
DISULFID   33    45        By similarity. 
DISULFID   38    52        By similarity. 
DISULFID   56    60        By similarity. 
DISULFID   253   286        By similarity. 
Sequence information
Length: 303 AA [This is the length of the unprocessed precursor] Molecular weight: 32209 Da [This is the MW of the unprocessed precursor] CRC64: 0E0D011DFA5CC8B8 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSVWAFAFFS LFLSLSVRGS AEQCGQQAGD ALCPGGLCCS SYGWCGTTAD YCGDGCQSQC 

        70         80         90        100        110        120 
DGGGGGGGGG GGGGGGGGGG GDGYLSDIIP ESMFDDMLKY RNDPQCPAVG FYTYNAFISA 

       130        140        150        160        170        180 
AKEFPDFGNT GDDLMRKREI AAFLGQTSHE TNGWWPAAQG DQYDWGYCHM NYNYGLCGDD 

       190        200        210        220        230        240 
LNLPLLQEPE LVETDPFIAF KTALWFWMTP QSPKPSCHAV ITESWTPSAA DSEAGRVPGY 

       250        260        270        280        290        300 
GVITNIINGG IECGQGGPNN ANENRIGFYK TYCDSLGTTY GSNLDCYQQR PFGYGLLGLK 


DTM
P29031 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!