ID   CHID1_DICDI             Reviewed;         385 AA.
AC   Q54G42;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Chitinase domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=chid1; ORFNames=DDB_G0290417;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR   EMBL; AAFI02000163; EAL62224.1; -; Genomic_DNA.
DR   RefSeq; XP_635730.1; XM_630638.1.
DR   AlphaFoldDB; Q54G42; -.
DR   SMR; Q54G42; -.
DR   STRING; 44689.DDB0266404; -.
DR   PaxDb; Q54G42; -.
DR   EnsemblProtists; EAL62224; EAL62224; DDB_G0290417.
DR   GeneID; 8627648; -.
DR   KEGG; ddi:DDB_G0290417; -.
DR   dictyBase; DDB_G0290417; chid1.
DR   eggNOG; KOG2091; Eukaryota.
DR   HOGENOM; CLU_035132_2_0_1; -.
DR   InParanoid; Q54G42; -.
DR   OMA; YSINERI; -.
DR   PhylomeDB; Q54G42; -.
DR   Reactome; R-DDI-114608; Platelet degranulation.
DR   PRO; PR:Q54G42; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0070492; F:oligosaccharide binding; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..385
FT                   /note="Chitinase domain-containing protein 1"
FT                   /id="PRO_0000327682"
FT   DOMAIN          78..385
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   385 AA;  44679 MW;  1DE3268813C585EE CRC64;
     MKKQLILCLF LLSLLMISTF VTNADDNDNE IYEEEEDFTT NRDVKQRGLV RENVSAKQII
     NNYNKYFKNV DIKNFEQGNT LVYITPWNGK GYDVATKWAK KFTHISPVWH QVKFENNKVM
     IEGDHNIDKK WMEKVKENSD QKSKILPRFS FEGQQWGSKE SFQKYIDPKL IDSLVSTVKK
     NNYDGLVIEG IVHINKQLRD PFLISLSEKL HSIGKEIILV IYPFRQKGQE TGFGAKDFEL
     LSNHIDGVSL MTYDFGPSGG MNAPKVWVED NLKFLLPNGE NKNSKKIFMG IPFYGYKIGE
     NDQSDAIVGS EFISVLKQNK SKKLKFDQNT HEHIFTYKNK KNQQVSMTYP SLLFIEDRIQ
     LANKYKVSIS IWEIGQGLDY FMDLL