CHI2_METAN
ID CHI2_METAN Reviewed; 419 AA.
AC Q4U4T0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Endochitinase 2;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase 2;
DE Flags: Precursor;
GN Name=chi2;
OS Metarhizium anisopliae (Entomophthora anisopliae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=5530;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=E6;
RX PubMed=16874542; DOI=10.1007/s00284-006-0078-6;
RA Baratto C.M., Dutra V., Boldo J.T., Leiria L.B., Vainstein M.H.,
RA Schrank A.;
RT "Isolation, characterization, and transcriptional analysis of the chitinase
RT chi2 Gene (DQ011663) from the biocontrol fungus Metarhizium anisopliae var.
RT anisopliae.";
RL Curr. Microbiol. 53:217-221(2006).
RN [2]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION,
RP AND VIRULENCE.
RX PubMed=19649636; DOI=10.1007/s00294-009-0267-5;
RA Boldo J.T., Junges A., do Amaral K.B., Staats C.C., Vainstein M.H.,
RA Schrank A.;
RT "Endochitinase CHI2 of the biocontrol fungus Metarhizium anisopliae affects
RT its virulence toward the cotton stainer bug Dysdercus peruvianus.";
RL Curr. Genet. 55:551-560(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ALTERNATIVE SPLICING (ISOFORM
RP CHI2-1).
RX PubMed=20406672; DOI=10.1016/j.gene.2010.04.005;
RA Boldo J.T., do Amaral K.B., Junges A., Pinto P.M., Staats C.C.,
RA Vainstein M.H., Schrank A.;
RT "Evidence of alternative splicing of the chi2 chitinase gene from
RT Metarhizium anisopliae.";
RL Gene 462:1-7(2010).
CC -!- FUNCTION: Secreted chitinase involved in the degradation of chitin, a
CC component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Participates in the infection
CC process and directly acts in the penetration process of the host
CC cuticle. {ECO:0000269|PubMed:19649636}.
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:0000269|PubMed:19649636};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19649636}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=chi2-2;
CC IsoId=Q4U4T0-1; Sequence=Displayed;
CC Name=chi2-1;
CC IsoId=Q4U4T0-2; Sequence=VSP_055327;
CC -!- INDUCTION: Only transcribed when chitin is the carbon source. The
CC promoter contains the consensus motif for the creA/crel/crr1 carbon
CC catabolic repressor. {ECO:0000269|PubMed:16874542}.
CC -!- DISRUPTION PHENOTYPE: Decreases the mortality of the host cotton
CC stainer bug Dysdercus peruvianus after infection.
CC {ECO:0000269|PubMed:19649636}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; DQ011663; AAY34347.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4U4T0; -.
DR SMR; Q4U4T0; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18B_METAN; -.
DR PHI-base; PHI:2388; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism; Chitin degradation;
KW Chitin-binding; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..419
FT /note="Endochitinase 2"
FT /id="PRO_0000429866"
FT DOMAIN 35..343
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 383..419
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 343..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 391..419
FT /note="CGGEGYSGPTQCVPPYQCVKQGDWWSSCR -> VILSMCSLKKKRISRGSSH
FT SSDV (in isoform chi2-1)"
FT /evidence="ECO:0000305"
FT /id="VSP_055327"
SQ SEQUENCE 419 AA; 43687 MW; 485A1D6116A52FCA CRC64;
MHHLRALVGV GLAGLAAGVP LTDKISVKPR QAPGAQNVVY WGQNGGGTIE NNDLAAYCQP
NSGIDVLVLA FLYQFGNGGN IPSGTIGQSC YISTSGQGQN CEALTAAIHT CQSAGVKIVL
SLGGATSSYS LQTQAQAEQI GQYLWDSYGN SGNKTVQRPF GSNFVNGFDF DIEVNGGSSQ
YYQYMIAKLR ANFASDKSNT YLITGAPQCP IPEPNMGVII SNSVFDHLYV QFYNNNNYTV
PCALGINGNA PFNYNNWTSF IADTPSAGAK IFIGVPASPL ASTGTPSGAQ YYAAPEQLAA
IVGEYRSDAH FGGIMMWSAG FSDANVNDGC TYAQQAKSIL VNGAPCPSSG PPSSTPATAP
APTATTMPSS TSVSSPTASP TGGTVPQWGQ CGGEGYSGPT QCVPPYQCVK QGDWWSSCR
