ID F4WNS8_ACREC Unreviewed; 538 AA.
AC F4WNS8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Endochitinase {ECO:0000313|EMBL:EGI64271.1};
GN ORFNames=G5I_07432 {ECO:0000313|EMBL:EGI64271.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI64271.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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; GL888237; EGI64271.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WNS8; -.
DR STRING; 103372.F4WNS8; -.
DR EnsemblMetazoa; XM_011058364.1; XP_011056666.1; LOC105147384.
DR eggNOG; KOG2806; Eukaryota.
DR InParanoid; F4WNS8; -.
DR Proteomes; UP000007755; 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: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-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 3: Inferred from homology;
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:UP000007755};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..538
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003320556"
FT DOMAIN 27..406
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 481..537
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 411..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 60280 MW; 3A11D305BF1EA80C CRC64;
MTSMMKKLLF SLLSFLALLA YGATVSPRLV CYFSNWAIHR PGIGSYGIDD IPTDMCTHII
YSFIGVSNVT WQVLILDEEV DVQKGGFNKF VALKEKQPSL KAQVAIGGWG EGGRKYSQMV
SVKARRDALI SSIVDLMHKH KFDGIDLDWE YPAATDRGGS FNDKNNFFYF VEELRTAFDK
AGKGWEITMA VPIPMFRLNE GYHVPELCKL ADAIHVMTYD LRGNWGGFAD VHSPLYRRPH
DQYAYEKLNV HDGLQLWEDK GCPASKLVVG IPLYGRTFTL SQGNNNFKPG TYINKEAGGG
EPGNYTDAKG FISYYEICME LQQPNQNGWT KDYDDVGKVP YMYKGGKSPQ WVGYEDADSI
VHKMNFIKEK KYLGAMVWAC DMDDFKGVCG PTNPLITTIY NGLKGYTVTS KNYNTTPRPE
WDRPPSTPSS TGEKPRPTPN PESTSNPEST PNPEPTTNPE PISNIDVTSH PTQSTSDDKN
EVVCNGQIMI SGKDCSEYFI CVHGKPMKSH CPTGLVFHTT NLICDWPENA DRKECKKI
//