ID A0A0L0CEG1_LUCCU Unreviewed; 1014 AA.
AC A0A0L0CEG1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative chitinase 3 {ECO:0000313|EMBL:KNC29864.1};
GN ORFNames=FF38_13517 {ECO:0000313|EMBL:KNC29864.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC29864.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC29864.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC29864.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC29864.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC29864.1}.
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DR EMBL; JRES01000611; KNC29864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0CEG1; -.
DR STRING; 7375.A0A0L0CEG1; -.
DR EnsemblMetazoa; KNC29864; KNC29864; FF38_13517.
DR EnsemblMetazoa; XM_046951667.1; XP_046807623.1; LOC111689192.
DR OMA; MDDFNGT; -.
DR Proteomes; UP000037069; 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:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProt.
DR CDD; cd02872; GH18_chitolectin_chitotriosidase; 2.
DR Gene3D; 3.10.50.10; -; 2.
DR Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
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:SF399; CHITINASE 7; 1.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00636; Glyco_18; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 2.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01095; GH18_1; 2.
DR PROSITE; PS51910; GH18_2; 2.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1014
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005536383"
FT DOMAIN 122..493
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 559..923
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 949..1008
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 27..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 258..285
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 41..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 114153 MW; 6ECDF534BC88B8B1 CRC64;
MLPPRIFKFV FLICLIIVLI SQTTDSAQTK TRRRLRRPTS APEESSSSSV SVSNARSTRV
SYKKATESSA EKQTDQESSP STAVTRSRLR SKSKLRSGDS TGLIASGSSL KGKKTKADDG
GKKIVCYYTN WSQYRPKIGK FMPEDIPADL CTHIIFAFGW LKKGKLSSYE SNDETKDTVP
GLYDRMMTLK KANPKLKILL ALGGWSFGTQ KFKEMAATRY TRQTFIYSAI PFLRKRGFDG
FDLDWEYPKG SDDKKNFVLL LKELREAFEA EAQELKKQRL LLSAAVPVGP DNVRGGYDVP
AVASYLDFIN LMAYDFHGKW ERETGHNAPL YAPSTDSEWR KQLSVDNAAN MWVKMGAPKE
KLIIGMPTYG RSFTLANTAK HGPNAPATGG GREGIYTKES GFLAYYEICE MLLNGAVYVW
DDEMKVPYLV DGDQWVGFDD ERAIRNKMNW IKTNGFGGAM VWTVDMDDFK GEVCGGNVKF
PLIGAMREEL LGISRGKEAK DVNWSEVAAT FEDLEEEEVE KPEPIKISVD EILAKVRKPV
KKHKVKSGLV AKDQNSRPAQ VFCYLTSWSS KRPGAGKFEP SHINPKLCTH VVYAFATLKD
HKLAENSDED PDNYEQVIAL RDTNPDLQIL LAIGGWAFGS TPFKELTSNV FRMNQFVYEA
IDFLRDYKFN GLDVDWEYPR GSDDRAAYVN LLRELRVAFE GEAKSSGLPR LLLTAAVPAS
FEAIAAGYDV PEISKYLDFI NVMTYDFHGQ WERTVGHNSP LFPLESTTGY QKKLTVDYSA
REWVKQGAPK EKLLIGMPTY GRSFELINET QFDIGAPASG GGSPGKFTNE AGFLSYYEVC
SFLAADNTTL VWDSEQQVPF AYRGNQWVGF DDERSLKTKM EWLKEQGFGG IMVWSIDMDD
FTGRCGNGKY PLLNALNDEL KDYKVTLEYD GPYESRGPRG AYTTKDPHEV TCEEEDGHIS
YHKDWSDCTH YYMCEGERKH HMPCPANLVF NPQENVCDWP ENVEGCHVPT EAPA
//
