CHI1_COCP7
ID CHI1_COCP7 Reviewed; 427 AA.
AC C5P230; P54196; Q00432; Q00435; Q400W4; Q400W5; Q400W6; Q9C0M7; Q9C2W1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Endochitinase 1;
DE EC=3.2.1.14;
DE AltName: Full=CiX1;
DE AltName: Full=Complement-fixation antigen;
DE Short=CF-AG;
DE Short=CF-antigen;
DE Flags: Precursor;
GN Name=CTS1; ORFNames=CPC735_036390;
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 -!- 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=AAA92643.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L41663; AAA92643.1; ALT_SEQ; Genomic_DNA.
DR EMBL; ACFW01000012; EER28933.1; -; Genomic_DNA.
DR RefSeq; XP_003071078.1; XM_003071032.1.
DR AlphaFoldDB; C5P230; -.
DR SMR; C5P230; -.
DR PRIDE; C5P230; -.
DR EnsemblFungi; EER28933; EER28933; CPC735_036390.
DR GeneID; 9696573; -.
DR KEGG; cpw:CPC735_036390; -.
DR VEuPathDB; FungiDB:CPC735_036390; -.
DR HOGENOM; CLU_002833_1_3_1; -.
DR Proteomes; UP000009084; 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 Gene3D; 3.10.50.10; -; 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 Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 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; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..427
FT /note="Endochitinase 1"
FT /id="PRO_0000387962"
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 SITE 169
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 103
FT /note="K -> N (in Ref. 1; AAA92643)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="T -> I (in Ref. 1; AAA92643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 47400 MW; 7DDA4A82DD67A21B CRC64;
MRFLIGALLT LQTLVQASSM SSMPNSYPVP EAPAEGGFRS VVYFVNWAIY GRGHNPQDLK
ADQFTHILYA FANIRPSGEV YLSDTWADTD KHYPGDKWDE PGKNVYGCTK 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
