ID Q0Z939_TRICA Unreviewed; 2700 AA.
AC Q0Z939;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 08-NOV-2023, entry version 91.
DE SubName: Full=Chitinase 10 {ECO:0000313|EMBL:ABG47448.1};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:ABG47448.1};
RN [1] {ECO:0000313|EMBL:ABG47448.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18342250; DOI=10.1016/j.ibmb.2007.06.010;
RA Zhu Q., Arakane Y., Banerjee D., Beeman R.W., Kramer K.J.,
RA Muthukrishnan S.;
RT "Domain organization and phylogenetic analysis of the chitinase-like family
RT of proteins in three species of insects.";
RL Insect Biochem. Mol. Biol. 38:452-466(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; DQ659250; ABG47448.1; -; mRNA.
DR RefSeq; NP_001036067.1; NM_001042602.1.
DR SMR; Q0Z939; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GeneID; 652967; -.
DR KEGG; tca:652967; -.
DR CTD; 3355116; -.
DR HOGENOM; CLU_228329_0_0_1; -.
DR OrthoDB; 3716108at2759; -.
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; 4.
DR Gene3D; 3.10.50.10; -; 5.
DR Gene3D; 2.170.140.10; Chitin binding domain; 5.
DR Gene3D; 3.20.20.80; Glycosidases; 5.
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:SF359; CHITINASE 10-RELATED; 1.
DR Pfam; PF01607; CBM_14; 5.
DR Pfam; PF00704; Glyco_hydro_18; 5.
DR SMART; SM00494; ChtBD2; 5.
DR SMART; SM00636; Glyco_18; 5.
DR SUPFAM; SSF51445; (Trans)glycosidases; 5.
DR SUPFAM; SSF54556; Chitinase insertion domain; 5.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 5.
DR PROSITE; PS50940; CHIT_BIND_II; 5.
DR PROSITE; PS01095; GH18_1; 3.
DR PROSITE; PS51910; GH18_2; 5.
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2700
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004179327"
FT DOMAIN 175..541
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 557..611
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 637..994
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1100..1154
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1204..1257
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1276..1330
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 1398..1767
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1823..2192
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 2234..2286
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 2321..2690
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 996..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..1816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2202..2224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2287..2313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2700 AA; 305406 MW; 7C74074910AB5856 CRC64;
MELLHITLCA FLILTPTDQR VVTRTIPSFL RDDVERYPSG PELSDRSAAY TNRELYGTRA
LPLRSAVEHI PDLIADSRRL PLRDAVEKRP PPDEPIDDYE PSFDLFYYPS RQTLYTPVQY
FKDLVAEAYV SPFRIDNESQ ELLKYPSFAR GRSLYDSRGR HSEIVETVYD PREDDRVVCY
VQAAARYRKE PLAFSPEDLD PFACTHVIYA FATIDPHNFN MISNDDESDI IQGGYISVTG
LKRVNPKLKV LISVGEGRDG SHRFSTMVSS ANRRREFIRS AITFIKQYNF DGMDIHWEYP
GAEKMGGQLS DKEYLNLFLE ELSEIFKPRG WVLTIAVPAS RFRVEDGFNP QRLGSLVDFI
NLQAFDFHRE REPVADHHAN LYSRPGDSGL DLFLSVDYAV KFWTKKGFPK SKIVLGVPFF
GRSFTLQFTN ETQVGAPIKG PGREGFYTQN PGFLAYFEIC DMLLNEGWHK GMDESGSPYM
VYGDQWVGYD DSESVEKKVN YVQEMNLGGV FIWATDLDDF KGVCGMKWPL LSTINRHLRG
NELLPMQQSQ NPPTKPYGTC RSEGIFSDPK NCAAYYVCRS GLSYHLSCAE NMMFDPMSGK
CEYSLGEKCR PGQIIQVANS LRQYEDLLEY EAKEEGPKVV CYMTNWAFYR KAEGKFVPEH
IDQRLCTHVV YAFASLDPEK LLLKEFDPWA DLDNNLYERV TSLKDTKAIL SLGGWTDSAG
DKYSRLVGDG SARRRFVVAV VGFLRRHNFK GLHLDWNYPV CWQSNCKKGA SSDKPNFTKL
IQVVPTMELR REFDKQKPPL ILAAAISGYK EVIDVAYDLP ALGTVLDFMS VMTYDYHGAW
ERQTGHNFTM EYLVSRGAPR GKLLVGVPFY GQSFTLTKGN NHDQGVPSAG PGEAGEYTKQ
PGMLAYYEIC NRIRNQRWIV NRDTSGATGP FAYHGDQWVG FEDIKSVRDK AEYIKTKGFG
GAVAWTIDLD DFSNRCCGGS FPLLRSLNRG LGLIPDNPSR EDCTKPPEPV TPAPPQVTTG
VDTGASSTEH MHPDWTTKPS TWWSSTTTSP WWTTTTTRRT TTTRPTTTST TTRPTTTNWP
TQGTTIPPPA VVMPEVDKPS QPCEPGQYVP DPHNCNAYYR CVLGELRKQY CAGGLHWNKE
RKICDWPKSA KCEEKKPGHK PSTSSWQKPT KPSYRPPSTT NHWQTKTTTS TTTRPTTTVS
QLIDDKCDSG QYYPHESCSS FYVCVNGHLV PQNCAPGLHY NPEEHMCDWK YKVKCVGRKQ
LAQKYQLPKM GGPQPYSACS ENAFAAYPGD CTRYLHCLWG KYEVFNCAPG LHWDNNKNIC
DWPEKATCDG TSNVNVVDIV TTAKPAQSTT SVSTTTSWNP GSTTNYPEWQ PTEWHPPIPP
TSEKPPLPEE LKPQSGYFKI VCYFTNWAWY RKGLGKYLPE DIDPDLCTHI VYGFAVLDFE
NLIVKAHDSW ADFDNQFYKR VTGYKAKGIK VSLALGGWND SQGDKYSRLV NNPAARARFI
KHVLQFLEKW NFDGLDLDWE YPKCWQVDCK KGPDSDKQAF AAWVTELKQA FKPKGYLLSA
AVSPSKTVID AGYDVPVLAQ NLDWVAVMTY DFHGQWDKQT GHVAPLYYHP EDEVVFYNAN
FSINYWISEG VPRRKIVMGM PLYGQSFRLE KPENHGLNAK APGPGQAGEY TRAAGFLAYY
EICHNIKTQG WTVVQDPNRR MGPYAYKGDQ WVSFDDREMI KRKSEFIRKM DLGGGMIWAL
DLDDFKNRCG EGRHPLLTTI RNVLADAGTG QQETIPPIDE EPPSVEAVEE EREEAPPSVH
SSTVVPPPQH STTQSLVDPK SEFKVVCYFT NWAWYRQGVG KYLPSDIDPD LCTHIVYGFA
VLNGDQLIIK PHDTWADFDN KFYEKVTAYK SKGIKVLVAI GGWNDSAGDK YSRLVNNPSA
RRRFIAHVVD FIETNNFDGL DLDWEYPKCW QVDCNKGPAS DKSAFADFVK ELHEAFKPKG
WLLSAAVSPS RRVVDAGYDV PTLSKYLDWI AVMCYDYHGQ WDKITGHVAP MYAHPEDADA
TFNTNFTIHY WIEKGADRRK LVMGMPMYGQ SFSLADNNQN GLNAATYGGG EAGEETRARG
FLAYYEICTN VIKKGWKVVR DRRGRIGPYA YLRDQWVSFD DIGMIRHKSE FIKAMGLGGG
MIWALDLDDF KNLCGCEEYP LLRTINRVLR GYAKPDPKCI LGRDNDKTKP KPTTMKPTTT
IGYEPQEPVL PAEVVPCQGR LFVADDTNCA QYYLCNQGQL QLQVCPNGLF WNKDHCDWPE
NTECHPDASS TMAPSTTPMV PDKPVTTTTS RPIGTDTSDD YKVVCYFTNW AWYRQGDGKY
LPSDIDPSLC THINYGFAVL DSSSMTLKPH DSWADIDNEF YKKVVSYKSR GVKVLIALGG
WNDSAGNKYS RLVNDPQARA AFIAHVLAFI EEWNFDGLDL DWEYPKCWQV DCNKGPDSDK
EAFAAFVREL SAAFKPKNLL LSAAVSPSKA VMDAGYDVPA LSQYLDWIAV MTYDFHGHWD
KQTGHVAPLY YYPGDVYDYF NANFSLNYWI EKGADPGKIV MGMPLYGQSF SLADAADRGL
NAKSYGPGEA GEFTRAGGFL AYYEICERVK KRGWTVTRDP QGRIGPYAYL SNQWVSYDDI
AEIRRKSRLV KALKLGGGMV WALDLDDFKN RCGCGKHPLL KTLNNELRGT PSDISVTNCT
//
