ID A0A0K0E589_STRER Unreviewed; 536 AA.
AC A0A0K0E589;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Endochitinase {ECO:0000313|WBParaSite:SSTP_0000467300.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000467300.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000467300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR AlphaFoldDB; A0A0K0E589; -.
DR STRING; 6248.A0A0K0E589; -.
DR WBParaSite; SSTP_0000467300.1; SSTP_0000467300.1; SSTP_0000467300.
DR Proteomes; UP000035681; 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:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 2.
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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF01607; CBM_14; 2.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR SMART; SM00494; ChtBD2; 2.
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; 2.
DR PROSITE; PS50940; CHIT_BIND_II; 2.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..536
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005327699"
FT DOMAIN 32..370
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 398..455
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 484..536
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
SQ SEQUENCE 536 AA; 59635 MW; 679E8B00883C331D CRC64;
MYSLIHWLFI FLSLQGIFFT ATLSALSQDT QYIRPCYFTN WAQYRQGQGK FLPEDYIPGL
CTHILFAFGW MNEDYTAKAY DPADLPNDWA GAGMYSRINS LKQKDPNLKT LLSFGGWTFG
TRLFEVLLGF FNKVNYVAFI KELRLAADEE STKTGKDRLL ITAAVSAAVE TIRSGYDIPA
LADYFDFILL MSYDFHGTWE SQTGFNAPLY PRIGETNTDW NVAGAAHYWA QHGMPKNKII
IGAATYGRGW TLTNSKEFGV GAAGTKATTT KFVGEAGVGA YYEFCEMLAQ GATRYWDDQA
KVPYLVFGDQ WFSYDDVESI QYKAEFVKEH GFGGMFIWTL DFDDFGGRCS GGGNIKYPLI
SKISEVLGGK TLSITSSTPK STTTLKIVPS TSSENELEGF CDELSDGFHS LAPYSCIQFM
LCLNKSSYLM ECPSNLQYNE KIGYCVLPKD SGCSSSFPPT TIITSTVSTT TITSTVSTIK
KVEKFVCIVD GFHADPNSCF RFYRCVNLTP YLFDCPGGLA YNKEAKLCDR IGVSGC
//