ID A0A3F3PUB5_9EURO Unreviewed; 1524 AA.
AC A0A3F3PUB5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=BDQ94DRAFT_161391 {ECO:0000313|EMBL:RDH30342.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH30342.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH30342.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH30342.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) 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. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
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; KZ852061; RDH30342.1; -; Genomic_DNA.
DR STRING; 1341132.A0A3F3PUB5; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
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; cd00035; ChtBD1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_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:SF401; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 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; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
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:UP000253729};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1524
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017597447"
FT DOMAIN 54..419
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 76..119
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 90..102
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 95..109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 113..117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1524 AA; 166034 MW; D3D8A19CB59A8298 CRC64;
MPRISAARRG PPWDFLLVAL VLLFLSSQVQ AQTTYHCNAT TPCYNGACCG VTDGQGICGY
GSDFCGDTCV SNCNATAACG QYAAVPGTTC PLNVCCSKYG FCGTESDFCD ADCQSNCAAP
IEPGCTSNDV LKRVIGYYEG WSSDRVCDSW SPSNIAASAL THLNSWALSV LNMLETYGFD
GVDLDWEYPV ASDRGGKAAD KKNYVSLIST LRNVLDGSGK AYGISFTTPS SYWYLQNFDV
PGMLEAGADW TNIMTYDLHG TWDASDVWIG SVMLAHTNLT EIKSALDLMW RAGVDASDIV
LGIGFYGRSY TMSDTACYQP GCPFIGAGNA GSCTVTPGVL SYSEIIELMQ DEDTEVIWDD
TDAVNYMVWG DQWVSFDTNV TFQQKVDYAN TKCLGGLMIW SVDQDTYDWQ ALSGLLGKSV
TSNNLLSGGT LGDSDKKDLS HIYSAFTGTD CYVSECFYWN SGWCETGYST LDYVHQGLYG
IVADPDTMTC ATGEEGDTDA QYRMICCPTD AMPEGCAWAG STVSDQCGAV GCSSGQYELV
ADPYVDRTGS EKCGGSNSRS LCCNTDSALE KCSWSTCGQA SFCCPSEDTY TGCDWYGCDD
KCPDTKVLIT QRSEIVLDGN AVTCTSGANK LCCDPPDGSN SWPVDPEDLF KYPDEENVSY
YYSVQKSSND EDTDNASEDP FALVMIDGDA SAYDESLVDQ WTFLDDENEL SKRGLKMHKR
HNLFEHRNDT FDNVIETYHI QCVSLFVNGS ACTSIFNGGA SNTIVKMPAD IGAGPYARVI
KLAPVGSDRS DMKPRSTGEV YELTVDYDFA AAAEEQKGDV NFRIDYTNLQ EYWKDITDTP
ASRKRWFGSF DNWLRKMTTI VKDEKGSLPL DYEETIKLFH GHEYCPAWNT DATFDIDAFI
HLELNGQYGY YFEGSILPTP NLISAYGYFS IEPTAAILLT IPELFSLGFP GMSIKGLINI
GPELALYGQL DASLQVSGEL NAGVALLFKR TEVYFPQDAA GAAASVAPAD LDDNDDATYS
FDPTFDAQLT AEGNLALSLT PEVRFGVSVL GGDLMSGYVT AGISNTINLG ISAEASYSGD
GASAGFCYWA DYVYSIFLRA DMSFLGDVAY WGGNYDVTSP SDPLELVSMT CTSYSSGDSL
TKRTDTESLV ANTTGSACFG GIISCQTIED NTTTASNLSC PIVCDGSDSG SCTVLDTAPD
PESTSSKKRQ GPASAATNGM CYHWPALWYN CAWFPDKDLP NLDSNTNSLP NNQYWTAPVL
KLLAGICRNV ANYLYQHQAS WSPGYMGPNF MRLTYKKSGP KSPNRAAACG SSTTRNTPAW
NCVQIKSSLW PAAVQKAWAA NDPNYQFMQG WSDPISCDEF PCRATACAPV EQQSYQSLAN
NMISHIKDNS VNMVWSATAF TGYPQHFTVN LFNTYSNQHV VNSLGPYGGY YDSGENLPLT
DIAAGVNLFS SPIWSLSSSN AVCRIDGGPP INDLQRGISY YHLTTCQVIY EDPNQSGRWW
KRDDDDSYDG PDHLHPRYWQ IKGA
//
