ID F4WH20_ACREC Unreviewed; 955 AA.
AC F4WH20;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Sialidase {ECO:0000313|EMBL:EGI66499.1};
GN ORFNames=G5I_04973 {ECO:0000313|EMBL:EGI66499.1};
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:EGI66499.1}
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.
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DR EMBL; GL888148; EGI66499.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WH20; -.
DR STRING; 103372.F4WH20; -.
DR eggNOG; ENOG502S014; Eukaryota.
DR InParanoid; F4WH20; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR PANTHER; PTHR22933:SF42; FI17806P1-RELATED; 1.
DR PANTHER; PTHR22933; UNCHARACTERIZED; 1.
DR Pfam; PF01607; CBM_14; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT DOMAIN 497..555
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 104..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..879
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 91926 MW; 60DD6540E31DC59D CRC64;
MSAGAHPWWG RISTWGAIKD IYADEVTSTI SHCLDLPQHC GVFCTYGSVG TSSSTWEELT
KSDARNVAAI SVGFPLEKTE RLAEIAVSWT EKRKFAICDV SQRQADDEGY NYPRPTNQLI
PGTSGGGTGK PGGFPTAPGG YPSGGPGTPG VPGEQGVPGG QPGRPGGYPS GPPGFSERPG
GTQPGRQPSF PSGPGPSEGY PSGRPSIPFP SGEPTGRPGT GPGIPSGPSG PEGFPTGPSG
GYPSGRPGGQ GPGGFPSGQR PSGYPSGGPG QGKPGPGYPT GRPGGQGPSG GYPSGQAPGG
YPGQAQKPSG PESGYPSGGP GAGYPGGTQR PPSGPGVQGG YPGGKNGLQS PGPQGGPGGY
PSGRPGAQRP GGYPGGPGPQ GPGGFPGGPG PQGPGLQGPG FPGGPGPQAP GPQGPGGFPG
RPGGPGPQAP GPQGPGFPGG PGPQAPGFPE TGHPVGPGGP GEYTHEDEGT YDEGDYSAIP
GEPGRDYPIY SEIPETSFRC DAQQFPGYYA DVEAQCQVFH ICANNKTYDF LCPNGTIFHQ
QFFVCVWWNQ FDCNSAPSLY YLNENIYDYT IMGTQGQGPA GPSRPSTYPG GPGVPSGPGG
PSYPGGPGTP SGPSYPGGPG APSGPSYPGG PGAPSGPSYP GGPGAPSGPS YPGGPGAPSG
PSYPGGPSAP GGPSYPGGPG APSGPSYPGG PGAPSGPSYP GGPGAPSGPS YPGGPGAPSG
PSYPGGPSAP GGPSFPGGPG APSGPSYPGG PQRPGGPGYP AERPQGPSGP QGPSGPQGPS
RPGGPGYPGG PGAPSGPGPQ GPSGRPGPGY LGPPSGPSGP QGPQGPGGPG YPGRPQGPSG
PTGPSTRPQG PSGPGYPAPG GPSPGYPAPG GPSPGYPGQP QGPTGTQGPS FPGAPGRSQG
PSGPNGYPSG RPSGPAFPSG PPGSGGIPGK PETGSPFPPQ GPAKPDREYL PPRIG
//