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Database: UniProt
Entry: I6QMM8_SPOEX
LinkDB: I6QMM8_SPOEX
Original site: I6QMM8_SPOEX 
ID   I6QMM8_SPOEX            Unreviewed;       987 AA.
AC   I6QMM8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Chitinase 7 {ECO:0000313|EMBL:AFM38213.1, ECO:0000313|EMBL:QCQ82721.1};
OS   Spodoptera exigua (Beet armyworm) (Noctua fulgens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7107 {ECO:0000313|EMBL:AFM38213.1};
RN   [1] {ECO:0000313|EMBL:AFM38213.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Li H., Li F.;
RT   "Cloning and sequence analysis of the lethal genes of the beet armyworm,
RT   Spodoptera exigua (Lepidoptera:Noctuidae).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QCQ82721.1}
RP   NUCLEOTIDE SEQUENCE.
RA   He L., Yu H., Xu C., Zhao Y., Yang F., Huang G.;
RT   "Molecular characterization, activity analyzation and transcriptional
RT   detection of chitinase encoded Spodoptera exigua.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   EMBL; JQ653039; AFM38213.1; -; mRNA.
DR   EMBL; MK050859; QCQ82721.1; -; mRNA.
DR   AlphaFoldDB; I6QMM8; -.
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   2: Evidence at transcript level;
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..987
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5036283792"
FT   DOMAIN          94..465
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          529..893
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          919..978
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
SQ   SEQUENCE   987 AA;  111544 MW;  0FA3E5100AC8DDFC CRC64;
     MWPPRLLRWA FAVLLIVAII TPTSDSTNVR RRLRKPSKVS TSVTSSVSRS SDQIISASVN
     RPKIRGRPNV ASRKSSAAID NSVTTDLHKD KDGYKIVCYY TNWSQYRTKI GKFTPEDIQP
     DLCTHIIFAF GWLKKGKLSS FESNDETKDG KTGLYDRINA LKKANPKLKT LLAIGGWSFG
     TQKFKEMSAT RYARQTFIYS AIPYLRDRNF DGLDVDWEYP KGGDDKKNYV LLLKELREAF
     EAEAQEVKKP RLLLTAAVPV GPDNIKGGYD VPAVASYLDF INVMAYDFHG KWERETGHNA
     PLYAPSSDSE WRKQLSVDHA AHLWVKLGAP KEKLIIGMPT YGRTFTLSNP NNFKVNSPAS
     GGGKAGEYTK EGGFLAYYEV CEILRNGGTY VWDDEMKVPY AINGDQWVGF DDEKSIRNKM
     RWIKDNGFGG AMVWTVDMDD FSGSVCGGDV KYPLIGAMRE ELRGISRGKD AQDVDWASVA
     SSALIEVTEK PEPIKISLSD VLKRVKKPVK NVIIKNNNNA AIDKNRREPQ ILCYLTSWSS
     KRPSAGRFLP ENVDPTLCTH IIYAFATLKD HKLTEGDEKD AEMYDKVVAL REKNPNLKIL
     LAIGGWAFGS TPFKELTSNV FRMNQFVYEA IEFLRDYQFN GLDVDWEYPR GADDRAAFVS
     LLKELRLAFE GEAKTSGQPR LLLSAAVPAS FEAIAAGYDV PEISKYLDFI NVMTYDFHGQ
     WERQVGHNSP LFPLESATSY QKKLTVDYSA REWVRQGAPK EKLMIGMPTY GRSFTLINDT
     QFDIGAPASG GGAAGRFTNE AGFMSYYEIC EFLREDNTTL VWDNEQMVPF AYRDDQWVGF
     DDERSLKTKM AWLKEEGFGG IMVWSVDMDD FRGSCGTGKY PLITAMKQEL GDYKVRLEYD
     GPYESSNPNG QYTTKDCNEV VCEEEDGHIS YHPDKADCTM YYMCEGERKH HMPCPQNLVF
     NYNENVCDWP ENVEGCTHHT QAPAAKR
//
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