ID   CHI2_COCIM              Reviewed;         895 AA.
AC   Q1EAR5; J3KGU1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Endochitinase 2;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CTS2; ORFNames=CIMG_00348;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
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).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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=EAS34994.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; GG704911; EAS34994.3; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001246577.2; XM_001246576.2.
DR   AlphaFoldDB; Q1EAR5; -.
DR   SMR; Q1EAR5; -.
DR   STRING; 246410.Q1EAR5; -.
DR   EnsemblFungi; EAS34994; EAS34994; CIMG_00348.
DR   GeneID; 4565656; -.
DR   KEGG; cim:CIMG_00348; -.
DR   InParanoid; Q1EAR5; -.
DR   OrthoDB; 923272at2759; -.
DR   Proteomes; UP000001261; 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; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..866
FT                   /note="Endochitinase 2"
FT                   /id="PRO_0000252287"
FT   PROPEP          867..895
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000252288"
FT   DOMAIN          29..340
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          343..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..712
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           866
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   895 AA;  94380 MW;  C34ECF3D2609C3CF CRC64;
     MGLTNILAAF 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 STISASTSTQ
     TSSQSTTMET KTLSASTTPS SPSTVSPSST MQTTSTGSTS TGTGTTSSQV TSSTTISTRS
     ASTETVTTRS QEPPSTTIST RPASTETVTT RSQEPPSSTI STRSASTETV TTRSQEPPSS
     TISTRSASTE TSTSSQDSPS TTISTKSAPT GTVTTRSQDL PSTTISTRSP ETETETVTTK
     SQDSPSITLS TRSSSAETVS TRSQHSSSTT ISTKSAPTET GTTSEHSTSM PVSTRSASTE
     TVITRSQNSD SQSMTVSTRS PSTESITTRS QGSPSETFST KSVPVDTIST ELPSQTHSTT
     DSTPVSSSPT IPSGSTTIIP GTASDPVSAP TTTVPPNPTL TLAPSSSTTE DRTTITTIIT
     TSYVTVCPTG FTTVTITYTT TYCPETASLT PTQAPIPGAP APPPDGWTTI VTVCPQCAPT
     PTTVTLTVPT RSAFLPAPTE TRPVVTVVPV PENPIKNVKP SESGDFVTVT TVAPATVTKT
     LEYNNPVDSD VNVQPTGGSS PVEFEGGAMT VRSMDVVAKA LITAGAAVLG LFLGL