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   25-MAY-2022, entry version 118.
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   EnsemblFungi; EER24478; EER24478; CPC735_058480.
DR   GeneID; 9692093; -.
DR   KEGG; cpw:CPC735_058480; -.
DR   HOGENOM; CLU_009107_2_0_1; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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; cd02877; GH18_hevamine_XipI_class_III; 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   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 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