ID CHI1_COCIM Reviewed; 427 AA.
AC Q1E3R8; J3KAA2; Q400W2; Q9C0M7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Endochitinase 1;
DE EC=3.2.1.14;
DE AltName: Full=Complement-fixation antigen;
DE Short=CF-AG;
DE Short=CF-antigen;
DE Flags: Precursor;
GN Name=CTS1; ORFNames=CIMG_02795;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-151.
RC STRAIN=IFM 45815, IFM 45816, IFM 46868, IFM 50992, and IFM 50995;
RX PubMed=16699492; DOI=10.3314/jjmm.47.113;
RA Sano A., Miyaji M., Kamei K., Mikami Y., Nishimura K.;
RT "Reexamination of Coccidioides spp. reserved in the Research Center for
RT Pathogenic Fungi and Microbial Toxicoses, Chiba University, based on a
RT multiple gene analysis.";
RL Nippon Ishinkin Gakkai Zasshi 47:113-117(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-145.
RC STRAIN=RMSCC 1694 / CA2, RMSCC 2019 / CA4, and RMSCC 2267 / CA1;
RX PubMed=9144263; DOI=10.1073/pnas.94.10.5478;
RA Koufopanou V., Burt A., Taylor J.W.;
RT "Concordance of gene genealogies reveals reproductive isolation in the
RT pathogenic fungus Coccidioides immitis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5478-5482(1997).
RN [5]
RP ERRATUM OF PUBMED:9144263.
RA Koufopanou V., Burt A., Taylor J.W.;
RL Proc. Natl. Acad. Sci. U.S.A. 95:8414-8414(1998).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE20296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20300.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20303.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GG704911; EAS37441.1; -; Genomic_DNA.
DR EMBL; AB232752; BAE20296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232753; BAE20297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232755; BAE20299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232756; BAE20300.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232759; BAE20303.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ408865; CAC29131.1; -; Genomic_DNA.
DR EMBL; AJ408866; CAC29132.1; -; Genomic_DNA.
DR EMBL; AJ408867; CAC29133.1; -; Genomic_DNA.
DR RefSeq; XP_001249024.1; XM_001249023.2.
DR AlphaFoldDB; Q1E3R8; -.
DR SMR; Q1E3R8; -.
DR STRING; 246410.Q1E3R8; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyCosmos; Q1E3R8; 1 site, No reported glycans.
DR GeneID; 4566471; -.
DR KEGG; cim:CIMG_02795; -.
DR VEuPathDB; FungiDB:CIMG_02795; -.
DR InParanoid; Q1E3R8; -.
DR OMA; TWENGVW; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
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; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..427
FT /note="Endochitinase 1"
FT /id="PRO_0000252286"
FT DOMAIN 38..401
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 102..103
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 129..132
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 172
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 237..240
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 378
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 427 AA; 47398 MW; F55F6DF8D0FCB15D CRC64;
MRFLIGALLT LQTLVQASSM SSMPNSYPVP EAPAEGGFRS VVYFVNWAIY GRGHNPQDLK
ADQFTHILYA FANIRPSGEV YLSDTWADTD KHYPGDKWDE PGNNVYGCIK QMYLLKKNNR
NLKTLLSIGG WTYSPNFKTP ASTEEGRKKF ADTSLKLMKD LGFDGIDIDW EYPEDEKQAN
DFVLLLKACR EALDAYSAKH PNGKKFLLTI ASPAGPQNYN KLKLAEMDKY LDFWNLMAYD
FSGSWDKVSG HMSNVFPSTT KPESTPFSSD KAVKDYIKAG VPANKIVLGM PLYGRAFAST
DGIGTSFNGV GGGSWENGVW DYKDMPQQGA QVTELEDIAA SYSYDKNKRY LISYDTVKIA
GKKAEYITKN GMGGGMWWES SSDKTGNESL VGTVVNGLGG TGKLEQRENE LSYPESVYDN
LKNGMPS
//
