ID A0A2K3QLF6_9HYPO Unreviewed; 1163 AA.
AC A0A2K3QLF6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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=TCAP_01712 {ECO:0000313|EMBL:PNY28367.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY28367.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY28367.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY28367.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:PNY28367.1}.
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DR EMBL; NRSZ01000274; PNY28367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QLF6; -.
DR STRING; 45235.A0A2K3QLF6; -.
DR OrthoDB; 11640at2759; -.
DR Proteomes; UP000236621; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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; 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:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
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:UP000236621};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1163
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014439169"
FT DOMAIN 282..327
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 344..392
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 486..776
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1163 AA; 126649 MW; F6133109AF9915F9 CRC64;
MVSLIGMYKL LAAALGLLNL VRATSAESPV ELDPCPASCD LVGLNSTDWG VFHSLQRFSS
CSHPLLVVTS LYNSLDGNQP ITLRSCAING LSLPKHGAQR PSQSAIQAGH TQRLGVQIAW
KNSQASSSGA DIVSHAQVMA EVAGQGAQML ARLGDDPFTA FIYHPETSTS VGLFAPAGLN
TSQLVDLFVE HVNQRGFAGH LLAQGNCADH GAGSLTFGIV ATSGPDSLAA AQRVVRSWGD
STCISGGYDG RYTTSVILHV AGDDGKSSVP SPSPLEKRAS CRTVEVVTGD LCAALAKRCG
ISTTDLLKYN PKDKFCNTLR IGQKVCCSSG GLPIPRPNGD GSCFTYLVKQ KDTCWDIAQG
NLVTVAEIEK YNTNTWGWGG CKALQQGILI CLSSGKPPLP LPVANAVCGP TVRGTRPPPE
GTALSSLNPC KLNACCNVWG QCGTTAEFCL PAPPGPPGAP QKEGSPNCIS NCGMDIVNKG
TPPKNWMSIG YFEGYGPSRP CQRVDIRTVD LKKYTHIHFA FATLTAGTYT VSMGPTLAQF
YWFKRLSGVK KILSFGGWTF STDPATYGIF RAGVQSANRE KMAQNIASFV KSEGLDGIDI
DWEYPDAPDL PDIPPGDPTE GENYLQFLTI LKRLLPDKSA GIPTNKIAVG VTSYGRSFKM
TTPGCTGAMC TFTGKASGAT PGRCTGTAGY LSNSEIREII KTKSNVQQHI DANSNSNILV
YDEVQWVAYM DDGVKDSRKQ LYKGMNFAGV SDWAISLDEQ GLMPSPITIG PGDGFPTPQN
AVDPRIHTSC EKYKDIIYEA WAEAGELSKA PIKWSRWNKY QNALNTYLGK KSGQVPLFTD
HIWGNFQRHY QAHFGGSGSQ RGIYNYYYCD ADQMPQKVKD RMRVKSCKWF PKKKQGTTAT
TWRFPGTVWS EYYTLLCPLW LGVQDGAPIF RNLKTIAYEG DSFEALRTQI DSWGSGMRAG
TIYHETAHWN DISWPRCDGN ELYGPEQIVS KSQYGGDDGY EFNLRNAHSW TLTTLAMWMM
QRWDKIDVPM PRKPIPTTVP DALANPDDAE DSLDEDWFDP AQVNPADFIP LSHYGSIGSE
RLIGCFEGTY EFEDQCLLLC DRGDAGRNCS QNSDKTWKCS GCRKEPTTCT DGLYKSWDDC
FANCLNGLCS VNAGEKGMMR CRC
//
