ID A0A1Y1WI48_9FUNG Unreviewed; 363 AA.
AC A0A1Y1WI48;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:ORX72998.1};
DE Flags: Fragment;
GN ORFNames=DL89DRAFT_220728 {ECO:0000313|EMBL:ORX72998.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX72998.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX72998.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX72998.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC {ECO:0000256|RuleBase:RU004453}.
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:ORX72998.1}.
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DR EMBL; MCFD01000002; ORX72998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1WI48; -.
DR STRING; 61395.A0A1Y1WI48; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000193922; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF406; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000193922};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..363
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012734033"
FT DOMAIN 22..363
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT NON_TER 363
FT /evidence="ECO:0000313|EMBL:ORX72998.1"
SQ SEQUENCE 363 AA; 39550 MW; FD6EB429A547042F CRC64;
MRVTAIALAA GTLFCAVVQA DLAVFGYLPT WNRDAAAKVD YSKYTHVALA FGVPKADGSL
KFDGTSYLSS VVSQLHSTKT KALVSVGGWT DSNHFSTILK SPSARSTFLN ALVNLVKDHG
IDGIDIDWEY PGHEGNPGNA IDPQNDTKNL LALVKDLRAQ FDSRFGKGSK LITLAGSTAP
FWGPKGPLSD VKDFAGPVDF FNLMNYEING SWQPTTGPNA PLYFETNKGS QASFDSSVRA
WTKAGIPSKK LLGGLAFYGH GYKASVDMTS NPKNQYVAHT GDAVGDWTYV SLRRNGILSG
PTTAAGDWVR YYDSTTRTPW VFNKKTKVYV TYDDTQSLKE KRDYSANNNL GGVMVWSIDQ
DYD
//
