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P16061

- CHI8_POPTR

UniProt

P16061 - CHI8_POPTR

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Protein

Endochitinase WIN8

Gene

WIN8

Organism
Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Defense against chitin containing fungal pathogens.

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

GO - Molecular functioni

  1. chitinase activity Source: UniProtKB-EC
  2. chitin binding Source: UniProtKB-KW

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. chitin catabolic process Source: UniProtKB-KW
  3. defense response Source: UniProtKB-KW
  4. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase WIN8 (EC:3.2.1.14)
Gene namesi
Name:WIN8
OrganismiPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Taxonomic identifieri3694 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus
ProteomesiUP000006729: Linkage group LGIV, UP000006729: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 316293Endochitinase WIN8PRO_0000005319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 41PROSITE-ProRule annotation
Disulfide bondi35 ↔ 47PROSITE-ProRule annotation
Disulfide bondi40 ↔ 54PROSITE-ProRule annotation
Disulfide bondi58 ↔ 62PROSITE-ProRule annotation
Disulfide bondi84 ↔ 146PROSITE-ProRule annotation
Disulfide bondi158 ↔ 168PROSITE-ProRule annotation
Disulfide bondi266 ↔ 298PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP16061.

Interactioni

Protein-protein interaction databases

STRINGi3694.estExt_fgenesh4_pg.C_LG_IV1532.

Structurei

3D structure databases

ProteinModelPortaliP16061.
SMRiP16061. Positions 24-64.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 6441Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3979.
HOGENOMiHOG000231411.

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16061-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRFWALTVLS LLLSLLLGVS SDTAQCGSQA GNATCPNDLC CSSGGYCGLT
60 70 80 90 100
VAYCCAGCVS QCRNCFFTES MFEQMLPNRN NDSCPGKGFY TYDAYFVATE
110 120 130 140 150
FYPGFGMTGD DDTRKRELAA FFAQTSQETS GRSIIGEDAP FTWGYCLVNE
160 170 180 190 200
LNPNSDYCDP KTKSSYPCVA DYYGRGPLQL RWNYNYGECG NYLGQNLLDE
210 220 230 240 250
PEKVATDPVL SFEAALWFWM NPHSTGAPSC HEVITGEWSP SEADIEAGRK
260 270 280 290 300
PGFGMLTNII TNGGECTKDG KTRQQNRIDY YLRYCDMLQV DPGDNLYCDN
310
QETFEDNGLL KMVGTM
Length:316
Mass (Da):35,046
Last modified:April 1, 1990 - v1
Checksum:iA441FD604B2C1615
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M25337 mRNA. Translation: AAA96702.1.
CM000340 Genomic DNA. No translation available.
PIRiA33985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M25337 mRNA. Translation: AAA96702.1 .
CM000340 Genomic DNA. No translation available.
PIRi A33985.

3D structure databases

ProteinModelPortali P16061.
SMRi P16061. Positions 24-64.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3694.estExt_fgenesh4_pg.C_LG_IV1532.

Protein family/group databases

CAZyi CBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Proteomic databases

PRIDEi P16061.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3979.
HOGENOMi HOG000231411.

Family and domain databases

Gene3Di 3.30.60.10. 1 hit.
InterProi IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view ]
PIRSFi PIRSF001060. Endochitinase. 1 hit.
ProDomi PD000609. Chitin_bd_1. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00270. ChtBD1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEi PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Systemic accumulation of specific mRNAs in response to wounding in poplar trees."
    Parsons T.J., Bradshaw H.D. Jr., Gordon M.P.
    Proc. Natl. Acad. Sci. U.S.A. 86:7895-7899(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."
    Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W., Brun A.
    , Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.
    Science 313:1596-1604(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Nisqually.

Entry informationi

Entry nameiCHI8_POPTR
AccessioniPrimary (citable) accession number: P16061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 1, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3