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 27-MAR-2024, entry version 138. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 InParanoid; P29030; -. DR OMA; LIPHAND; -. 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 CDD; cd02872; GH18_chitolectin_chitotriosidase; 1. DR Gene3D; 3.10.50.10; -; 1. DR Gene3D; 2.170.140.10; Chitin binding domain; 1. DR Gene3D; 3.20.20.80; Glycosidases; 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 PANTHER; PTHR11177; CHITINASE; 1. DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1. 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; (Trans)glycosidases; 1. DR SUPFAM; SSF54556; Chitinase insertion domain; 1. DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 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 //