ID G3J3D4_CORMM Unreviewed; 1714 AA.
AC G3J3D4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=CCM_00318 {ECO:0000313|EMBL:EGX95664.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX95664.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX95664.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX95664.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126399; EGX95664.1; -; Genomic_DNA.
DR RefSeq; XP_006665541.1; XM_006665478.1.
DR STRING; 983644.G3J3D4; -.
DR GeneID; 18162353; -.
DR KEGG; cmt:CCM_00318; -.
DR VEuPathDB; FungiDB:CCM_00318; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_001837_3_1_1; -.
DR InParanoid; G3J3D4; -.
DR OMA; CHWIGKG; -.
DR OrthoDB; 2582538at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06921; ChtBD1_GH19_hevein; 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; 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; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 125..170
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 184..546
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 139..151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 144..158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 164..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1714 AA; 187956 MW; 856912C9236DC6F4 CRC64;
MAPPNGRLAS KTSKTSKLAI TLLIFSITLA FFLALPSFGR SPASSKITPV RRQNESAEPV
SALLYDEYSE HNNTLVRRID PYKCTKDIPC HTKACCGSFG ADGVGTCGFG PTFCGSDCAS
QCDAKPECGQ YAVPAGKTCP LNVCCSKFGF CGTTSLFCDT SEGCQSNCGT PAVPPGKSAK
PVTHRVIGYY EAWSARRECY PFPPAAIPIE GLTHLNFAFG YIAPSSYEVT PMDGATPASL
FTQTADVRSL KSGLSDLKVY ISLGGWTFSD NGTDTQPLFS EIASTESNRK KFANNLVDFM
KKYGFDGVDI DWDRYPGAPD RGGEEHDTSN FVALLKTLKE TFDASIHGPY GLTFTIPSSY
WYLRWFDVPG MLKYADWTNI MSYDLHGVWD KENPIGSIVQ SHTNLTEIKL SMELLWRNNV
APEQVVLGLG FYGRSFQLQD KSCSTPGCEF AGAAEPGSCT KNGGTLAYFE IQDIIKDQNP
KVIHDKAAAS KYFVYGRDQW VSFDDADTFT QKVDYANSVG LGGLMIWSVD QDDKEFSAMQ
GLLGMSLQSY SVLLKRAETT DAGKWTSLNG QKCVMSDCGV PAQCPDGYGM APGGEGFEDD
CGSSKFRIIC CPLNSMPESC LWRGGEGTSG RPSCHGQCHV GETTLFHSRH ATKNCLRPGW
QAFCCTAQTW AHQIAACKYS KCRGSCGDTD DTKGMKKVAS ISDDCIFGYK EICCPPDAAF
ENCHWVGKGS CDDNECADND VQLALDPFGD NQNRCGLNRK KVLCCNTPKN LNPFLPVSLD
KVFPTMPPET DYPQFDLQAL GATNPVTIDL DHNVFGMVII VGPASTVHTL RRSDGSDAYV
LDCPKIKQEG LSRIRLVCED GGPDSSCNKI HLDGAQGTII RLPAGCGPGH YAVLHSARDV
SQISTLPGNV ARSVPANRTI VELEVSHDFS KVKRDAGDIF VRIDYSNSNQ YWSKIVQGDP
IKHKRGMAPD LHKRFYSSAS SDWKDKFDSL RNLQQPSSLN SNGQLSKDNI KVTLSGEQKE
KCTAKGDDGF LNMDIAGKMY EDLEFGFTFV GTIAPTFHIE EANGYYDTSI SFNAQLTFDG
KGSLDIPAGL ESQKLFHSPV SAWGFSHPGI CDFGPTVNVE VAMTGKGNID AKFTAAFSIA
NSNAVTDSLP TGTGPHDGGV FNKLVSNAWS GDLSLPTKLQ PHSIKKARAA SPGTGSTILA
LRLRTISQMK LDLDFYGQKS VATDTQFNQT IESLFRISRE SNGDAIVAFS NDQATVESFT
TGDLPWGDDD SQRVVGRGDA LVLHSGTSTP PARSAPDVEG YPIFGGHDIM SCSDGTGNGG
GGSHLDTCVC WNYLDRYDRS LDLDPDTGAP YENVNLRRRR RMRMNDLLFA DPLLALNPDT
GKPYDEGLIT ELLEGRAPIQ YGSAENYAVT GPSGRRWNVR MGRYPQGRDG DSLNQLNPQA
GRYDAEDCYD CSNIAVTSSS TNPDIRVVTE HINERQTEPR AQEFMMNAQT RRGDGSLERS
AYPAIPERFL DDNSHLHEDY STWDPNGPYG NRGRPIDEIT NAYGSDTNPG VLVNTEAVLN
GIKARMWVGN QPMSDSLWNE NGFNLEDPQR SNAAISYIRA TMQVVVYLND AVVNDNWAHI
IQDVVDAYRR YAERVQAVDG VTIHPAEMYQ EYVLNVVIHN LEDTDRWMLR RIEQLRSVWR
NSNHPEAQGV LDQLQETEDQ VEELLIDMSR LPLD
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