ID A0A3D8REL5_9EURO Unreviewed; 1755 AA.
AC A0A3D8REL5;
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=DSM5745_07558 {ECO:0000313|EMBL:RDW72386.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW72386.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW72386.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW72386.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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: 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:RDW72386.1}.
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DR EMBL; PVWQ01000009; RDW72386.1; -; Genomic_DNA.
DR STRING; 1810919.A0A3D8REL5; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000256690; 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 CDD; cd00035; ChtBD1; 1.
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:SF401; CHITINASE; 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:UP000256690}.
FT DOMAIN 79..431
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 733..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1581..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1755 AA; 195433 MW; 90EC9E4A5CD7E373 CRC64;
MVPAVLGTTF AAMDARDLVT PTRNAASMRS RKTFHALSIK WGFCGTTAEF CDDECQNEGG
CQDVERPSCS ASTDAMALDV RIGYYGMWGA TRDCDTYQPE NIPAGALTHI NLAFEYVSED
HEITDTQGSI VARVSRLKEK YPGLKVSIAL GGWVFNDPPT QYRFSEMAST VPNREKFIAS
LIRYIRRYGL NGVDLDWEYP VAEDRGGKEE DYNNLVLLCQ DIREAFDRED PGWKLTLTLP
SSYWYLRGFS LAKLEKYVDW FNVMTYDIHG IWDQWNIWTG PYLKGHTNLT EIEDGMDLLW
RNGVSPEKVV MGFGFYGRSF TMSDTQCTTP PNCQFDSAGF AGECTGEAGI LSYSEVVSKR
GQLSSNEYYD EESSVKWMVY SSNQWISYDD AESFEKKKEY LTSRCLKGLM VWSLDLDTQD
YQAMTSLLGE RAMESALVDT GLNKQEAEQL AFDLSPWTGE LCYTTPTCTD GSSGERTGDQ
VCKGGFTAVS MAHSPLQRNG DYEMHGECAE DWWRYICCPT KAMPQECEWV GAPDRNVFGC
ERGCGDSQFE LNIDTYVDHE GHGSCYTGAR SLCCSGTEIL DKCHWTGCEA TPIGDPCADD
EDYIATRYDD DNGEMCPSEY MGPAHGDRYA SRALCCPKED KFENCDWAVD DCKPSQCPTD
KLAVDHAAIP ETIFDASLTA SRECYGYSIP AMTSPDYKLC CDPPWRYDEE WPVEPSYLWS
HYYDDEDDDV SWQFSNNFGN NNQDNRPNDL DDDPGTDPYG FVMLDGPPGS INNAFDEQYT
LATRDEPGRM AKRSLVTTNQ TTLDSVFEHV EETVLVYCNY PAGSKECREI FYKGAEDTII
RLPAHVGEGP WARVVSMEPV PQSQKDLPSW VVRKRDASEN ANGVYALTFD YDFHKIKRED
TQVNIRVDYT NLLPYWEEIT DSPSSRKRSM GEVPSFADWK AMVDEAKAHE PAPQGNRTTQ
GQLQVRTDQA PNSLSRRWWG SFVNWVKKMT TVTKTDGGVL PMGFMRSLVL YSGRLVCSNE
AVTFTAGMDI TADFNMEMNA RYAYYFSGTV VPPAVTDMYA YVGANPRVYA GVGIRGNAEL
YYPSERKKII DTLTYPGLAI KGIAAVGPTM DLWGQIDGRV TVSGDLQVGL TYAFKPVELY
FPNNDEAENK LDVEDLHDAR INQEGLVPEI SGNVRADVDI NIHATPEINL GIKVGGGIGS
LQGTLADAHV SAFANTTLNF HAQASASTSG GWSYGYSVTF LYRFGFGCVA EIYKYGKWAS
GLWFPFPQQA IPIISQTVSS GDSADKRGLY NGPELPMQSL PGALFGTHEI SNDYWPQADL
STLQTGNWTS SDLLKRADDA QVGKETQFKL GSFQCTTSAG SVCEDVASSF NLKRAPTDLA
VRPVYALQKR AATDCPKRIP RLYYNCVSFF SDFTFNGPTG TTNIPGICTN VARFLNNNRR
GNTGYTLTWE SSSQSNRRGK SCPSNFCDAD NAARKLVAFG PGLGPRELTN CDEFPFASVE
EGGEAWLGLN PAVTTGTTRT CVPTWMNSMQ GNCHNLLNNL ETNVNYFNDP KNPTDANEYW
ASWSQTSWNR KDAWNGRQRL ADYPNDQPHT NVPGLTADDR RYPKRSFFQK RNFTLHLAFP
QANANPDSQW PDQAFTSGTI SGGTGRNRPV TRTVGSSTWI ICAVNKMGQQ RYRYAGANGY
CWDGASTKGA WSSVGQIIRV FQCKITFAGS AGPAKRDGQP LGYFGDDAVL DIEEVQGTEE
FHAVPADWEG GSHFV
//
