ID A0A397HKD7_9EURO Unreviewed; 1467 AA.
AC A0A397HKD7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=CDV56_107113 {ECO:0000313|EMBL:RHZ62458.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ62458.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ62458.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ62458.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-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: 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:RHZ62458.1}.
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DR EMBL; NKHU02000037; RHZ62458.1; -; Genomic_DNA.
DR STRING; 41047.A0A397HKD7; -.
DR VEuPathDB; FungiDB:CDV56_107113; -.
DR OrthoDB; 11640at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
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; cd00035; ChtBD1; 1.
DR CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00118; LysM; 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 Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR029226; Ecp2.
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 InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR47700:SF1; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF14856; Hce2; 1.
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; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 2.
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:UP000215305};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1467
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017404572"
FT DOMAIN 295..340
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 359..407
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 498..862
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1467 AA; 158708 MW; C650DCAEDCE7AB72 CRC64;
MVALTWLSAA AALVLSAWPT AASATPGFRK AASPSYRSSA SACPERCSDA GPNTGNWSVY
ADFKQIHKCK ETMFYDFSLF DDVDDRNGTH RIQACSSYGP DFASLPASTA RIASAEFVDV
DFELGWWHEG FGLAAAGLRS IVKQMRRYAE GGHGPTDRPF IIYGQSGQAT IGLYIGQGLL
NQGLSESALK LFQDNLDKLE VSTPSLAMQL CEEGYDSTHV FGIMATSNGT FAPIQSAIKA
WANATCLSFS GSTKFAGSAK FTTPLLNGNH TTTNSTILAR NLARNLVTRA DGECTTVQVD
AGNSCADLAV KCGISGADFT KYNPGDGFCS KLKPKQHVCC SSGDLPDFRP QPNEDGSCKA
YQVQADDNCD SLAAEYSLEM DDLEEFNKNT WGWNGCKLLF KDTVMCLSEG TPPFPAEISN
AVCGPQKPGT NPPTDGSDIA DLNPCPLNAC CNIWGQCGIT ADFCIDTNTG APGTAEPGTY
GCISNCGMDV VKGSGSGGVK IAYYEGYCLS RQCLFQDASQ IDTSQYTHLH FGFGTLTASW
DVKTGDELST YQFGEFKKIS GVKRILSFGG WDFSTMPETY QIFRNGVKPA NRLTMATKIA
NFIKENDLDG VDIDWEYPGA PDLPDFDPGT EEDGPNYLAF LVILKNLLPG KSVSIAAPAS
YWYLKQFPIK NIAKVTDYIV YMTYDLHGQW DAHNSNSQEG CATGNCLRSQ VNLTETRQSL
AMITKAGVPG EKVIVGVTSY GRSFKMANAN CWGPDCLYTG DRLNSNAKKG KCTGTAGYLA
DAEIAEIMKD SSRVVKNYVD ATSNSDVLIY DTDEWVGYMS AATKKTRTSL YAAWGLGGTT
DWASDLQTYH DVPKPAKSWA NFIELARAGE DPKTDHTRNG NWTDFDCTDP AVVDFLDYTP
SQRWRLMGAD AAWDDVVRIW KDTDSQRDGV NFTQSVESTT HFGGQQGCGD LTTASCSTVE
CEKGADSDTS GPAAQFIWNS LAEIHGIYKS YYDTLFKALT IVSTALDDME NKFAPIPPEE
DDTWLLILID MITLGALGTA GPFFNTILKK HDWFAGKTGS ALDNAKDTAM TLIGQSTTIA
KDALPGGDAA SWTPEKQNEF SAYLGQVVYG WANITSLALE DLFSGSDVAI DALWQAMSDG
KLIEGKKEGD LPATGNAQNE LLANINKCII GFALPALWRQ SGSYTFIIDA GHACNEDKDL
SDYLDDDTMG ATGVCVDDWQ YYLAYPDGDA TKCTCERVTD AGPCQTICRD NKFSAPKGIE
YISDGNNYNG ITKTELVKGS VRTWIGNGRE NGAKVADPTN EGTMSDLMEV DVTSPGFMRI
PVCSPERAFQ SWDTANKDSS PNWPCDIPPG KDECGDSTFV DQTSDASPKV EDCRQIIKNI
EGDGSTDWTT QVVGHNQREI ASHASCHFGV EATKTDGNVN FKVGGQDVID IINNAIAQFG
RDGLIGAKGD MNCNGNIKSQ PVLWGIY
//
