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Protein

Endochitinase

Gene
N/A
Organism
Brugia malayi (Filarial nematode worm)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Microfilarial chitinase, which may function to degrade chitin-containing structures in the micro-filaria or in its mosquito vector during parasite development and transmission.

Miscellaneous

Known to bind calcium.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei148Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Chitin degradation, Polysaccharide degradation
LigandCalcium, Chitin-binding

Enzyme and pathway databases

BRENDAi3.2.1.14 997

Protein family/group databases

CAZyiCBM14 Carbohydrate-Binding Module Family 14
GH18 Glycoside Hydrolase Family 18

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase (EC:3.2.1.14)
Alternative name(s):
MF1 antigen
OrganismiBrugia malayi (Filarial nematode worm)
Taxonomic identifieri6279 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaSpiruromorphaFilarioideaOnchocercidaeBrugia
Proteomesi
  • UP000006672 Componenti: Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3562163

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Add BLAST22
ChainiPRO_000001194723 – 504EndochitinaseAdd BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi480 ↔ 493PROSITE-ProRule annotation

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP29030

Expressioni

Developmental stagei

The appearance of the MF1 antigen correspond with the onset of the parasite's ability to infect the mosquito.

Structurei

3D structure databases

ProteinModelPortaliP29030
SMRiP29030
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati407 – 4201Add BLAST14
Repeati421 – 4342Add BLAST14
Repeati435 – 4483; approximateAdd BLAST14
Domaini448 – 504Chitin-binding type-2PROSITE-ProRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 400CatalyticAdd BLAST378
Regioni407 – 4483 X 14 AA approximate tandem repeats of E-T-E-A-Y-[ED]-T-D-E-T-E-E-T-SAdd BLAST42

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi401 – 448Ser/Thr-rich (linker)Add BLAST48

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

OMAiVCYQGTW
OrthoDBiEOG091G014W

Family and domain databases

Gene3Di3.10.50.10, 1 hit
InterProiView protein in InterPro
IPR002557 Chitin-bd_dom
IPR036508 Chitin-bd_dom_sf
IPR011583 Chitinase_II
IPR029070 Chitinase_insertion_sf
IPR001223 Glyco_hydro18_cat
IPR001579 Glyco_hydro_18_chit_AS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF01607 CBM_14, 1 hit
PF00704 Glyco_hydro_18, 1 hit
SMARTiView protein in SMART
SM00494 ChtBD2, 1 hit
SM00636 Glyco_18, 1 hit
SUPFAMiSSF51445 SSF51445, 2 hits
SSF54556 SSF54556, 1 hit
SSF57625 SSF57625, 1 hit
PROSITEiView protein in PROSITE
PS50940 CHIT_BIND_II, 1 hit
PS01095 CHITINASE_18, 1 hit

Sequencei

Sequence statusi: Complete.

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

P29030-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRTTLILFF IILSNTITVI HGYVRGCYYT NWAQYRDGEG KFLPGNIPNG
60 70 80 90 100
LCTHILYAFA KVDELGDSKP FEWNDEDTEW SKGMYSAVTK LRETNPGLKV
110 120 130 140 150
LLSYGGYNFG SAIFTGIAKS AQKTERFIKS AIAFLRKNNF DGFDLDWEYP
160 170 180 190 200
VGVAEEHAKL VEAMKTAFVE EAKTSGKQRL LLTAAVSAGK GTIDGSYNVE
210 220 230 240 250
SLGKNFDLLF LMSYDLHGSW EKNVDLHGKL HPTKGEVSGI GIFNTEFAAD
260 270 280 290 300
YWASKGMPKE KIIIGIPMYA QGWTLDNPSE TAIGAAASRP SSASKTNPAG
310 320 330 340 350
GTASYWEICK YLKEGGKETV HQEGVGAYMV KGDQWYGYDN EETIRIKMKW
360 370 380 390 400
LKEKGYGGAF IWALDFDDFT GKSCGKGPYP LLNAISSELE GESENPEITT
410 420 430 440 450
EEPSITETEA YETDETEETS ETEAYDTDET EETSETEATT YDTDETEGQE
460 470 480 490 500
CPERDGLFPH PTDCHLFIQC ANNIAYVMQC PATTFFNDAI KVCDHMTNAP

DTCI
Length:504
Mass (Da):55,971
Last modified:December 1, 1992 - v1
Checksum:iA78BE7BFB8E3709B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73689 mRNA Translation: AAA27854.1
PIRiA38221

Similar proteinsi

Entry informationi

Entry nameiCHIT_BRUMA
AccessioniPrimary (citable) accession number: P29030
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 23, 2018
This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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

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