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Database: UniProt
Entry: Q0Z941_TRICA
LinkDB: Q0Z941_TRICA
Original site: Q0Z941_TRICA 
ID   Q0Z941_TRICA            Unreviewed;       496 AA.
AC   Q0Z941;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   SubName: Full=Chitinase 8 {ECO:0000313|EMBL:ABG47446.1};
DE   SubName: Full=Putative chitinase 2-like Protein {ECO:0000313|EMBL:EFA06693.1};
GN   Name=AUGUSTUS-3.0.2_09624 {ECO:0000313|EMBL:EFA06693.1};
GN   ORFNames=TcasGA2_TC009624 {ECO:0000313|EMBL:EFA06693.1};
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:ABG47446.1};
RN   [1] {ECO:0000313|EMBL:ABG47446.1}
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).
RN   [2] {ECO:0000313|EMBL:EFA06693.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA06693.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [3] {ECO:0000313|EMBL:EFA06693.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA06693.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
RN   [4] {ECO:0000313|EMBL:EFA06693.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA06693.1};
RA   Shelton J.M., Herndon N., Coleman C., Lu N., Brown S.J.;
RT   "Tools and pipelines for BioNano data: molecule assembly pipeline and FASTA
RT   super scaffolding tool.";
RL   Submitted (NOV-2014) 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; DQ659248; ABG47446.1; -; mRNA.
DR   EMBL; KQ971352; EFA06693.1; -; Genomic_DNA.
DR   RefSeq; NP_001038094.1; NM_001044629.1.
DR   AlphaFoldDB; Q0Z941; -.
DR   STRING; 7070.Q0Z941; -.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EnsemblMetazoa; TC009624_001; TC009624_001; TC009624.
DR   GeneID; 661428; -.
DR   KEGG; tca:661428; -.
DR   CTD; 37390; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   HOGENOM; CLU_002833_3_1_1; -.
DR   InParanoid; Q0Z941; -.
DR   OMA; QTQNHIN; -.
DR   OrthoDB; 2663738at2759; -.
DR   Proteomes; UP000007266; Linkage group 7.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR   GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR   CDD; cd02872; GH18_chitolectin_chitotriosidase; 1.
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:SF360; CHITINASE 12-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..496
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010134250"
FT   DOMAIN          24..389
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          440..496
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          389..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  54066 MW;  45CC475C16CA14C9 CRC64;
     MSKALVASFL LVYFSGALVS ATTDKVVCYW GTWSTYRWGN GRFTVDHIDP YLCTHIIYSF
     VGLQADGNVR HLDEYLDVDA GTIAKLNALK VKNPNLKTLI AIGGWNEGSE TYSQVAADAA
     KRATFIKSAL NLVQKWGFDG FDLDWEYPGQ RGGAAADIQN YATLIKEFRE VWDQHGLLLT
     AAVAAAGPSV DLSYHVPSLS KYLDFINVMA YDLHGSWESV TGQNAPLYAS SIDVEGSQKL
     LNVDASIRGW IERGADPGKL VLGLGVYGRS FTLASASNNK LGAPIVAGGD AGRYTGERGM
     MGYNEIVEAQ NAGGWTTVWD DEQKTPYMYK GNQWVGYDNP KSIAIKVQYA KSLNLAGVMI
     WSIETDDFNG LSGTKYQILN AINAALKSDE IPPEPVPTPE PQPTQTTESE PTQASEQPTE
     SSTTQKPQTT KTPESGNESD GVCTKEGIVR DPSDCSVYYT CVSDGSKLVS IQRKCNHGLV
     YDLELNICNY PQVVQC
//
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