DIAC2_DICDI
ID DIAC2_DICDI Reviewed; 385 AA.
AC Q8T293; Q554T5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable di-N-acetylchitobiase 2;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=ctbs2; ORFNames=DDB_G0274233;
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}.
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DR EMBL; AAFI02000012; EAL70009.1; -; Genomic_DNA.
DR RefSeq; XP_644238.1; XM_639146.1.
DR AlphaFoldDB; Q8T293; -.
DR SMR; Q8T293; -.
DR STRING; 44689.DDB0238379; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; Q8T293; -.
DR EnsemblProtists; EAL70009; EAL70009; DDB_G0274233.
DR GeneID; 8619666; -.
DR KEGG; ddi:DDB_G0274233; -.
DR dictyBase; DDB_G0274233; ctbsA.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_061189_1_0_1; -.
DR InParanoid; Q8T293; -.
DR OMA; YKWIMKQ; -.
DR PhylomeDB; Q8T293; -.
DR PRO; PR:Q8T293; -.
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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..385
FT /note="Probable di-N-acetylchitobiase 2"
FT /id="PRO_0000328003"
FT DOMAIN 16..377
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 385 AA; 43203 MW; CB809387881EEB4D CRC64;
MRIILLLFLI VFVVAQSSSS SSSSGCPCDS SYLCEPLQIA PRQEFLGFSL NSTQYPNYYW
NQLTTLAIFY ETIEDELLCI AHENDVRLVW GTTFPIENLG NSSYIEEWIQ EQIEKVQSTF
TDGLNFDVES PITDPTIAQQ YTELVSATNK AFKAINPFYQ ISIDVAWSPS CIDKRCYDYA
GLASNSDFLV AMDYDERSQV FGEKVCTAGA NSSPSNALAG INNFTDLGIS TDQLVMGLPW
YGYIYKNCLN GDEAGLETVV CQIESVPFRG ANCSDAAGSE YDYSYLVQLL QDQTINSSAV
QWNTEWQSPY FNYIDPITGN VDQVWFDNPQ SLSIKVQLAQ KLNLRGVAVW NIDFLDFSDQ
YNSRPMWDAL ASFFPQSASS EQSLN
