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Database: UniProt
Entry: A0A1M2V6T4_TRAPU
LinkDB: A0A1M2V6T4_TRAPU
Original site: A0A1M2V6T4_TRAPU 
ID   A0A1M2V6T4_TRAPU        Unreviewed;       472 AA.
AC   A0A1M2V6T4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=TRAPUB_6203 {ECO:0000313|EMBL:OJT03206.1};
OS   Trametes pubescens (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT03206.1, ECO:0000313|Proteomes:UP000184267};
RN   [1] {ECO:0000313|EMBL:OJT03206.1, ECO:0000313|Proteomes:UP000184267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBCC735 {ECO:0000313|EMBL:OJT03206.1,
RC   ECO:0000313|Proteomes:UP000184267};
RA   Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA   Hilden K.;
RT   "Genome sequence of the basidiomycete white-rot fungus Trametes
RT   pubescens.";
RL   Submitted (OCT-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:OJT03206.1}.
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DR   EMBL; MNAD01001625; OJT03206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M2V6T4; -.
DR   STRING; 154538.A0A1M2V6T4; -.
DR   OMA; WNTFGEG; -.
DR   OrthoDB; 360175at2759; -.
DR   Proteomes; UP000184267; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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   CDD; cd12215; ChiC_BD; 1.
DR   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR045321; Cts1-like.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding 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   Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
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:UP000184267};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..472
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009890589"
FT   DOMAIN          29..330
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          330..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  48743 MW;  8C0F057C37182D5F CRC64;
     MASFWLSSIL SALSLGALHV SAFDNSRSDN LAVYWGQNSY GATHSDTANF QKSIATYCQD
     DSIDAFPIAF LNVFFGAGNE PSIDLSNICS SVDDPVFPGT SMPDCSFLAS DIQFCQSKGK
     IVTISLGGAT GAASFTSDEQ AAAFGDTIWN TFLGGSGAIR PFGGAVLDGI DLDIEGGGTT
     HFAAFVNQIR SHAAGANKQY YVTAAPQCPF PDAFLGTVLN AVAFDAVYVQ FYNNFCGLTN
     FNNPNAWDFD QWDSWAKNTA VNKNVKIYIG APASPSAAGS GYVDATTLAN IALETRSQFS
     SFGGIMLWDA SQAFANNRYD AAIKNAIRQG SGGGSTSVPV TVSTSSVPTA PTSAPPTTTA
     HSTTALPTTT AQSGSCAGVA AWVSNVAYEG GDTVIFNGHL WTAKWWSFGD TPGGNAVLPA
     SRPRSLAYCV LTAGVAGDWT DSGACTSFAA AVPTAHVAAA PATVASVPTA TA
//
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