ID D7B2R3_NOCDD Unreviewed; 295 AA.
AC D7B2R3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:ADH66761.1};
DE EC=3.2.1.14 {ECO:0000313|EMBL:ADH66761.1};
GN OrderedLocusNames=Ndas_1329 {ECO:0000313|EMBL:ADH66761.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH66761.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH66761.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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DR EMBL; CP002040; ADH66761.1; -; Genomic_DNA.
DR RefSeq; WP_013152368.1; NC_014210.1.
DR AlphaFoldDB; D7B2R3; -.
DR STRING; 446468.Ndas_1329; -.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR KEGG; nda:Ndas_1329; -.
DR eggNOG; COG3179; Bacteria.
DR HOGENOM; CLU_045506_0_0_11; -.
DR OMA; TISTWYW; -.
DR OrthoDB; 3614862at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd00325; chitinase_GH19; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR22595:SF79; CHITINASE 12; 1.
DR PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001060-2};
KW Glycosidase {ECO:0000313|EMBL:ADH66761.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADH66761.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..295
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003093045"
FT DOMAIN 33..75
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT REGION 66..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001060-1"
FT DISULFID 167..175
FT /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
FT DISULFID 263..295
FT /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
SQ SEQUENCE 295 AA; 31562 MW; 44EB137E8B3081CC CRC64;
MIRRLLSQLA ALGALAAVLI VLPATVAQAA TCAAAWSASA VYTGGGQVSY DGRNYTAKWW
TQNERPGTSD VWTDQGACGN DGGGEEPNPT GFVVTEAQFN QMFPNRNPFY TYSGLTAALS
SYPAFTNTGS TEVRRREAAA FLANVSHETG GLVHIRETNE ANYPHYCDGN QPFGCPAGQA
AYYGRGPIQL SWNYNYKAAG DALGIDLLNN PYLVEQNASV AWRTGLWYWN TQTGPGTITS
HNAIVNGHGF GETIRSINGA HECDGGNPAQ VQSRINKFTQ FAQILGTTTG SNLSC
//