ID CHI2_COCP7 Reviewed; 855 AA.
AC P54197; C5PIX5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 13-SEP-2023, entry version 122.
DE RecName: Full=Endochitinase 2;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=CTS2; ORFNames=CPC735_058480;
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C735;
RX PubMed=8566773; DOI=10.1016/0378-1119(95)00654-0;
RA Pishko E.J., Kirkland T.N., Cole G.T.;
RT "Isolation and characterization of two chitinase-encoding genes (cts1,
RT cts2) from the fungus Coccidioides immitis.";
RL Gene 167:173-177(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- FUNCTION: May be associated with endosporulation.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92642.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EER24478.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L41662; AAA92642.1; ALT_FRAME; Genomic_DNA.
DR EMBL; ACFW01000049; EER24478.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003066623.1; XM_003066577.1.
DR AlphaFoldDB; P54197; -.
DR SMR; P54197; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyCosmos; P54197; 1 site, No reported glycans.
DR GeneID; 9692093; -.
DR KEGG; cpw:CPC735_058480; -.
DR HOGENOM; CLU_009107_2_0_1; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.20.20.80; Glycosidases; 1.
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 PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF47; ENDOCHITINASE A; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Chitin degradation; Chitin-binding;
KW Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..826
FT /note="Endochitinase 2"
FT /id="PRO_0000011928"
FT PROPEP 827..855
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000252289"
FT DOMAIN 29..340
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 341..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT LIPID 826
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 855 AA; 90609 MW; A53628680FE0CA9D CRC64;
MGPTNILAAF IAVSSLFIQS LALNPYAKSN LAVYWGQGAG QNRLSYFCEK TSFDIIVVGF
INVFPDQGPA GWPGSNFGNQ CADSYYYTKN GTKTKLLDGC YQIKEDLPKC KALGKTILLS
LGGGAVHDFY EVKSEESALN FADFLWGAFG PLTPDWTGPR PFGEASVDGF DFDIEKGSNF
GYSIMVRRLR ELFLQDPLNR YYISAAPQCI MPDKYLSHAI SNSAFDFIFI QFYNNPSCSA
KRWVTNPKSV TYTVDDWVKY IRKSGNPLAK LFIGLPASKS AAAKEDYLTP GEATKIVSTY
MAKYPSTFGG MMVWEATASE NNKLGGLPYA DIMKEVLLRC DPDPPTSTVT STTSASTSTQ
TSSQSTTMET KTLSASTTPS SPSTVSPSST MQTTSTGSTS IETVTTRSQE PPSTTISTRS
ASTEPVTTRS QEPPSTTIST RSASTETVTT RSQEPPSTTI STWSASTETS TSSQDSPSTT
ISTKSAPTGT VTTRSQDLPS TTISTRSPET ETETATTKSQ GSPSITLSTR SSSAETVSTR
SQHSSSTTIS TKSAPTETGT TSEHSTSMPV STRSASTETV ITRSQNSDSQ SMTVSTRSPS
TESITTRSQG SPSETFSTKS VPVDTISTEL PSQTPTTIIT GTPSDPVSAP TTTVPPNPTL
TLAPSSSTTE DRTTITTIIT TSYVTVCPTG FTTVTITYTT TYCPETASLT PTQPPIPGAP
APPPDGWTTI VTVCPQCAPT PTTVTLTVPT RSAFLPARTE TRPVVTVVPV PENPIKNVKP
SESGDFVTVT TAAPATVTKT LEYNNPVDSD VNVQPTGGSS PVEFEGSAMT VRSMDVVAKA
LITAGAAVLG LFLGL
//
