ID L2FHG9_COLFN Unreviewed; 385 AA.
AC L2FHG9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Chitin deacetylase {ECO:0000313|EMBL:ELA25183.1};
GN ORFNames=CGGC5_13605 {ECO:0000313|EMBL:ELA25183.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA25183.1};
RN [1] {ECO:0000313|EMBL:ELA25183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA25183.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; KB021181; ELA25183.1; -; Genomic_DNA.
DR RefSeq; XP_007285779.1; XM_007285717.1.
DR AlphaFoldDB; L2FHG9; -.
DR STRING; 1213859.L2FHG9; -.
DR EnsemblFungi; ELA25183; ELA25183; CGGC5_13605.
DR HOGENOM; CLU_021264_11_3_1; -.
DR OrthoDB; 1343935at2759; -.
DR PHI-base; PHI:3972; -.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10951; CE4_ClCDA_like; 1.
DR CDD; cd00035; ChtBD1; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR46471:SF4; CHITIN DEACETYLASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..385
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012429497"
FT DOMAIN 25..69
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 102..298
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DISULFID 35..47
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 40..54
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 385 AA; 41442 MW; 6FEB689085EF6F69 CRC64;
MHALLSLVLS GAAMAATLNN PLRKRAECGP GIGSCAPGEC CSEAGWCGTT EEYCGGSQCQ
LEYSDSCDTF FPPPGASTES ISRTLVGSVP YGSIITTCAN PGSLALTFDD GPYIYTSQLL
DLLEAQNVTA TFFVAGNNIG KKRIDDATTP WPAILRRMYG LGHQIASHTW THRNLNEVNS
TIQRTEIIYN EMAFRNLFGW IPTYMRPPFL ECNAGSGCQT LMRTLGYHII NVNVDTKDYE
NDSPTLIQVS KDRFSNGVST NAAANSYIEL SHDVHYQTVV NLTQFMIDTA KERGYRLVTV
GECLNDPREN WYRTAGGALS TGSTASTTAS RATASSTLIV SSRASTSSAP AATGNVSPDQ
TCGGTTGYTC LNSAFGNCCS YYGFW
//
