ID A0A421JJL7_9ASCO Unreviewed; 615 AA.
AC A0A421JJL7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=JA1_004516 {ECO:0000313|EMBL:RLV90511.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV90511.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV90511.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV90511.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) 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 -!- 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:RLV90511.1}.
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DR EMBL; NSGQ01000050; RLV90511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JJL7; -.
DR STRING; 2028339.A0A421JJL7; -.
DR Proteomes; UP000285775; Unassembled WGS sequence.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:UniProt.
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; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR025928; Flocculin_t3_rpt.
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; PF13928; Flocculin_t3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
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:UP000285775};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..615
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019521898"
FT DOMAIN 21..305
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 307..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 64168 MW; A84AE221F34DBDB4 CRC64;
MLPLKTLITA AFLTASALAD SQIAVYWGQN GFSGQDRLAT YCQNTNMDIV LLSFLNDFPD
PLNVNFANQC GGSFPDSDLL HCTYIGEDIK TCQGLGKKVL LSMGGAYGDY GFDNTQDATD
FADVLWNKFG GGSDDERPFD DAVVDGFDFD IESGSDTGYA ALATALKTKF AEDSSKSYYL
SAAPQCPYPD AYVGDLIANV PLDYIFIQFY NNNCQVQGDF NFDVWQAFAE SAPNPSVELF
VGVPGAPSDQ ISGFVTPDQL ATALDTIKCD SNFAGVSLWD ASGAYQDYNS NGAFIDQVKE
VLDNLDTDEC NPQSTTEPPS TSEDPTSTDQ TSEDPTSSDP TSEDATTSDP VSTDATTSDP
VSTDATTSDP VLADPATTED PTSSADPAST QDPAEDPITS ADPVSSTGPS LETSSIFYGN
SSLAAAQSTQ TVADIHTTVI TITSCSENKC SATPVTTGYV VVTDVNTVYT TYCPLTNEAS
TVAGATSAAQ STVTVTTVCH EEKCQAITKT VPVVVLPTNK GIVAVGSTTV AAAAAQPSVE
VSQETETYVS GDITSTITVQ VTSTLQGAVP TLASASSAAG NGTAPVYTFE GGAAADSSRV
ALWTTIPLLM LAALF
//
