DIAC1_DICDI
ID DIAC1_DICDI Reviewed; 373 AA.
AC Q7KWW8; Q550Q6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable di-N-acetylchitobiase 1;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=ctbs1; ORFNames=DDB_G0276795;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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 -!- FUNCTION: Involved in the degradation of asparagine-linked
CC glycoproteins. May hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-
CC acetylglucosamine chitobiose core from the reducing end of the bond.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000019; EAL68899.1; -; Genomic_DNA.
DR RefSeq; XP_642876.1; XM_637784.1.
DR AlphaFoldDB; Q7KWW8; -.
DR SMR; Q7KWW8; -.
DR STRING; 44689.DDB0238380; -.
DR PaxDb; Q7KWW8; -.
DR EnsemblProtists; EAL68899; EAL68899; DDB_G0276795.
DR GeneID; 8620742; -.
DR KEGG; ddi:DDB_G0276795; -.
DR dictyBase; DDB_G0276795; ctbsB.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_061189_1_0_1; -.
DR InParanoid; Q7KWW8; -.
DR OMA; HQMWFDN; -.
DR PhylomeDB; Q7KWW8; -.
DR PRO; PR:Q7KWW8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
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 Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..373
FT /note="Probable di-N-acetylchitobiase 1"
FT /id="PRO_0000328002"
FT DOMAIN 21..369
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 53..54
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 82..85
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 128
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 191..194
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 347
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 373 AA; 42433 MW; B55257242C3C6863 CRC64;
MKIFIIISLI LTILIIQSKS KECPCSNVEL CKPLEIGPRK EFIGFSVNST FYPYYNWDHL
TTIGIFYSED IEDELLCMAK TNGVRLVYSA FYPVEQLSNE TYIDQWINEK LELVQNTFTD
GLNFDVEYPI TDPIVAQQYT QLVAATNNAF KSVNLYYQIS VDVAWDASNC IDYRCYDYLG
LSKASDFLVV MDYDMKLDGY YFKTCLASAN SPPSSVLSGM VNFTKLGIDE SSLVMGLPWY
GYNYPCIGSN YTLQTFECII PPSSYLGYNC TDASGIEINY SIIMNMLNDT AIQNGGVQWD
SESESPYFNF IDLFSGTQHQ MWFDNPDSLT IKVNIARTMN LRGVGVWNID QLWDDHSLSS
GMWGALNSFF KIN
