ID A1CHT9_ASPCL Unreviewed; 254 AA.
AC A1CHT9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Polysaccharide deacetylase family protein {ECO:0000313|EMBL:EAW10444.1};
GN ORFNames=ACLA_049160 {ECO:0000313|EMBL:EAW10444.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10444.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW10444.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
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DR EMBL; DS027054; EAW10444.1; -; Genomic_DNA.
DR RefSeq; XP_001271870.1; XM_001271869.1.
DR AlphaFoldDB; A1CHT9; -.
DR STRING; 344612.A1CHT9; -.
DR EnsemblFungi; EAW10444; EAW10444; ACLA_049160.
DR GeneID; 4704029; -.
DR KEGG; act:ACLA_049160; -.
DR VEuPathDB; FungiDB:ACLA_049160; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR HOGENOM; CLU_021264_11_1_1; -.
DR OMA; GAIITHC; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10951; CE4_ClCDA_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..254
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633182"
FT DOMAIN 52..236
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 254 AA; 28544 MW; E48F55314DE1E7BC CRC64;
MVFTNWWTAF VLFITPASLF YQTWASPLNL TVGTRGSFVP FGALIDRCTV SGTVALTFDD
GPYIFTPDLL ELLSEYGARS TFFLNGQNLG SLYGDAAVVQ RILEEGHQVG SHTWGHPYLT
SLDYNAIVAQ MTQLEAAFIS VLGFYPTYMR PPYFAYNELV LSAMGDLGYH VIMASIDTKD
YENDHPDLIF RSFEKFRNEL NAGGSIVLAH DVHEQTVTTL TRAMLEEIRA RGLQTVTVGQ
CLGDPKEYWY RTSR
//
