ID A0A166U8H1_9PEZI Unreviewed; 402 AA.
AC A0A166U8H1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Chitin deacetylase (Polysaccharide deacetylase) {ECO:0000313|EMBL:KZL73089.1};
GN ORFNames=CT0861_01857 {ECO:0000313|EMBL:KZL73089.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL73089.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL73089.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL73089.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZL73089.1}.
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; LFIV01000049; KZL73089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166U8H1; -.
DR STRING; 708197.A0A166U8H1; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000076552; 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:UP000076552};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..402
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007880420"
FT DOMAIN 58..247
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 255..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 42658 MW; 1FF4ADF84A63A085 CRC64;
MLLRVHSLSL LAAIVASGEL ATAVPLDSSS AFTTRDLDRP RFGNVPYGVD ITHCTVNGKV
ALTFDDGPGE YTEKVLDTLE KNGNIKATFF LVGTNGNNGV ANPAYTPLLK RMLGAGHQLA
SHSWSHKDFN TISRDQQVEE LVKNEEIFAK TLGIVPTYFR PPYTHCDDKC ISTLNDLSYH
VADYDLDTKD WVDGGANSKQ TYSSAINSAN PSSLSFIALA HDIQPFTVNG FVQYMIDVAK
EKGFEFTTVG ECLGDPASNW YRDPKSGEPW GGKEEPKPTT TSKPVAPTTT SISATSTPET
KTTASTTESE TEKPSVTGKT TSETEETETE TDGPTSTGIS PPTATRTVDG GANIGIPVTP
TGTTAASRPT STNTVVEVNA AGRAVFSAGG ALAGALAWAM MI
//
