ID S4T9T0_9HEMI Unreviewed; 603 AA.
AC S4T9T0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:AFW03959.1};
GN Name=Chi {ECO:0000313|EMBL:AFW03959.1};
OS Poophilus costalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Cercopoidea;
OC Aphrophoridae; Poophilus.
OX NCBI_TaxID=798439 {ECO:0000313|EMBL:AFW03959.1};
RN [1] {ECO:0000313|EMBL:AFW03959.1}
RP NUCLEOTIDE SEQUENCE.
RA Chang S.-C., Shih H.-T., Lu K.-H.;
RT "Molecular cloning of chitinase cDNAs from the spittlebug Poophilus
RT costalis.";
RL Submitted (MAR-2012) 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; JQ806339; AFW03959.1; -; mRNA.
DR AlphaFoldDB; S4T9T0; -.
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 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:SF144; CHITINASE 5; 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 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..603
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004533115"
FT DOMAIN 29..404
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 544..600
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 407..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 68062 MW; 374A423E0685ED01 CRC64;
MGSWNFWLCG SAVVLLFVAT VSSQPTDDGR VVCYFSNWAI YRPGLGRYTI DDIPGEYCTH
IIYSFIGVSN VTWEVLVLDP EVDVEQNGYK NFTSLKEKYP GIKTSVAVGG WGEGGRKYSG
LVSMKERRDS FIKSVVEFMY KYDFDGFDLD WEYPGAADRG GSFSDKDLFF YFVEELRRAF
DKEGKGWEIT MAVPLAKFRL NEGYHVPELC ELVDAIHVMA YDLRGNWAGF ADVHSPLYRR
PHDQYAYETL NVNDGLQLWV DYGCSPTKLV VGVPFYGRSF TLSAGNTNYN LGSYINKEAG
GGAPGNYTKA KGFISYYEIC SEIQEEDSGW TIKWDEAGYC PYTYKGTQWI GYENEKSLQI
KMDWIKSKGY AGAMNWAIDM DDFNGLCGTK NPLIKVLYKN MKDYKVPAPT VTTSPRPEWS
RPKSTTSTSD DEYQKPTTVR TTPAYKPRPK PKPKPTTVRP ETEKPSVEKP VQKPTRKPVK
PTTQKPEESG GCGCDEESPS KPSATTTIKP IRTTTPKRKT TTTEEVDLES VSESNTGDNE
VPAAVDCAED GFKPHPACNK YYQCVYGEPL EFTCKLGTVW HQEMTICDWP ENSRRPQCKN
FKA
//
