ID D8Q478_SCHCM Unreviewed; 543 AA. AC D8Q478; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 50. DE SubName: Full=Glycoside hydrolase family 13 protein {ECO:0000313|EMBL:EFI96752.1}; DE Flags: Fragment; GN ORFNames=SCHCODRAFT_108800 {ECO:0000313|EMBL:EFI96752.1}; OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum. OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431}; RN [1] {ECO:0000313|EMBL:EFI96752.1, ECO:0000313|Proteomes:UP000007431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431}; RX PubMed=20622885; DOI=10.1038/nbt.1643; RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E., RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A., RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V., RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S., RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J., RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V., RA Woesten H.A.B.; RT "Genome sequence of the model mushroom Schizophyllum commune."; RL Nat. Biotechnol. 28:957-963(2010). CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|ARBA:ARBA00008061}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GL377306; EFI96752.1; -; Genomic_DNA. DR RefSeq; XP_003031655.1; XM_003031609.1. DR AlphaFoldDB; D8Q478; -. DR STRING; 578458.D8Q478; -. DR VEuPathDB; FungiDB:SCHCODRAFT_02689018; -. DR eggNOG; KOG0471; Eukaryota. DR HOGENOM; CLU_024572_2_0_1; -. DR InParanoid; D8Q478; -. DR OMA; MQYFEWN; -. DR OrthoDB; 2728918at2759; -. DR Proteomes; UP000007431; Unassembled WGS sequence. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11318; AmyAc_bac_fung_AmyA; 1. DR Gene3D; 2.40.30.140; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR013776; A-amylase_thermo. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1. DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000313|EMBL:EFI96752.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007431}. FT DOMAIN 66..449 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT REGION 13..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 543 FT /evidence="ECO:0000313|EMBL:EFI96752.1" SQ SEQUENCE 543 AA; 61503 MW; 69CA72DC030A44CD CRC64; MFSDLHKRFA NVFRPGHRRT QSAARPTGGG GATPAAAAPP PAAHHAAGPG LSRMRLGTED DPEQNPLMIE FFTWDALRDD MSWWQHLEQE LPEMARMGIT QVWIPPPNKA AAKTGRGYDA YDIWDLGEFD QKGMVRTRWG SKEELLRACR TAKQVKVDVI VDAVINHKLG ADRVETFPAV RVDTQNRLKE LSKVHEIEGW TAFDFPGRGD KVGFTSYTGL DWDQRTQQQG IYRIAGKGHH GWSRNVGTEF GNYDYLLGVD IDHRHPEVQE DFLRWGPWML ETLGAAGFRI DAAKHIDYKF MLQWITATRR NAQEPRMFCV CEFWSGDVKL ILPYIRAFKG EAVFFDVPLH MRLCEASRKR ERYDLRDLMS STLARLRPGD AVTFVDNHDT VEGMDLESWV EENFKIQAYA LILLRPEGYP CIFYGDLYPN KKCYNANTAA NLRRLIEARR LYAYGPVQDY NAGKNCIGFV RGGTGRHPGC VVLLSNRDEA GPLHTIRMNV GPARAGAIYR SYMTQGGEVQ IDAHGWGEFS CFANAVQVWV PAA //