CHIT_BRUMA
ID CHIT_BRUMA Reviewed; 504 AA.
AC P29030;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Endochitinase;
DE EC=3.2.1.14;
DE AltName: Full=MF1 antigen;
DE Flags: Precursor;
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1542646; DOI=10.1073/pnas.89.5.1548;
RA Fuhrman J.A., Lane W.S., Smith R.F., Piessens W.F., Perler F.B.;
RT "Transmission-blocking antibodies recognize microfilarial chitinase in
RT brugian lymphatic filariasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1548-1552(1992).
CC -!- FUNCTION: Microfilarial chitinase, which may function to degrade
CC chitin-containing structures in the micro-filaria or in its mosquito
CC vector during parasite development and transmission.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- DEVELOPMENTAL STAGE: The appearance of the MF1 antigen correspond with
CC the onset of the parasite's ability to infect the mosquito.
CC -!- PTM: O-glycosylated.
CC -!- MISCELLANEOUS: Known to bind calcium.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; M73689; AAA27854.1; -; mRNA.
DR PIR; A38221; A38221.
DR AlphaFoldDB; P29030; -.
DR SMR; P29030; -.
DR STRING; 6279.P29030; -.
DR ChEMBL; CHEMBL3562163; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR HOGENOM; CLU_002833_3_1_1; -.
DR OMA; QRFTDMV; -.
DR BRENDA; 3.2.1.14; 997.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR SUPFAM; SSF57625; SSF57625; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT CHAIN 23..504
FT /note="Endochitinase"
FT /id="PRO_0000011947"
FT DOMAIN 23..392
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REPEAT 407..420
FT /note="1"
FT REPEAT 421..434
FT /note="2"
FT REPEAT 435..448
FT /note="3; approximate"
FT DOMAIN 448..504
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 389..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..448
FT /note="3 X 14 AA approximate tandem repeats of E-T-E-A-Y-
FT [ED]-T-D-E-T-E-E-T-S"
FT COMPBIAS 389..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 78..79
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 105..108
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 149
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 212..215
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 362
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 27..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 480..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ SEQUENCE 504 AA; 55971 MW; A78BE7BFB8E3709B CRC64;
MNRTTLILFF IILSNTITVI HGYVRGCYYT NWAQYRDGEG KFLPGNIPNG LCTHILYAFA
KVDELGDSKP FEWNDEDTEW SKGMYSAVTK LRETNPGLKV LLSYGGYNFG SAIFTGIAKS
AQKTERFIKS AIAFLRKNNF DGFDLDWEYP VGVAEEHAKL VEAMKTAFVE EAKTSGKQRL
LLTAAVSAGK GTIDGSYNVE SLGKNFDLLF LMSYDLHGSW EKNVDLHGKL HPTKGEVSGI
GIFNTEFAAD YWASKGMPKE KIIIGIPMYA QGWTLDNPSE TAIGAAASRP SSASKTNPAG
GTASYWEICK YLKEGGKETV HQEGVGAYMV KGDQWYGYDN EETIRIKMKW LKEKGYGGAF
IWALDFDDFT GKSCGKGPYP LLNAISSELE GESENPEITT EEPSITETEA YETDETEETS
ETEAYDTDET EETSETEATT YDTDETEGQE CPERDGLFPH PTDCHLFIQC ANNIAYVMQC
PATTFFNDAI KVCDHMTNAP DTCI
