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Database: UniProt
Entry: Q48494_9BACL
LinkDB: Q48494_9BACL
Original site: Q48494_9BACL 
ID   Q48494_9BACL            Unreviewed;       699 AA.
AC   Q48494;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   SubName: Full=Chitinase {ECO:0000313|EMBL:BAA09831.1};
OS   Kurthia zopfii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1650 {ECO:0000313|EMBL:BAA09831.1};
RN   [1] {ECO:0000313|EMBL:BAA09831.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ikeda S., Toyoda H., Matsuda Y., Ouchi S.;
RT   "DNA sequence determination of a chitinase gene chiSHI cloned from gram-
RT   positive bacterium Kurthia Zopfii and its application to biological control
RT   of Powdry Mildew of Barley.";
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   EMBL; D63702; BAA09831.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q48494; -.
DR   SMR; Q48494; -.
DR   CAZy; CBM12; Carbohydrate-Binding Module Family 12.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12214; ChiA1_BD; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024}.
FT   DOMAIN          44..454
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          467..554
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          562..647
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          449..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   699 AA;  73495 MW;  2AE9599A604BF513 CRC64;
     MIPFNKHTAL KKTATFLLGL SLLLSIIVPS FVLQPATASA ADAYKIVGYY PSWAGYGRNY
     NVTDIDPTKV THINYAFADI CWNGVHGNPD PSGPNPVTWT CQNEKSQTIN VPNGTIVLGD
     PWIDTGKTFA GDTWDQPIAG NINQLNKLKQ INPNLKTIIS VGGWTWSNRF SDVAATAATR
     EVFANSAVDF LRKYNFDGVD LDWEYPVSGG LDGNSKRSGD KQNYTLLLSK IREKLDAAGA
     VDGKKYLLTI ASGASTTYAA NTELANIASI VDWINIMTYD FNGAWQKVSA HNALLNYDPA
     ASAAGVPDAN TFNVAAGAQG HLNAGVPAAK LVLGVPFYGR GWDGCAQAGN GQYQTCTGGS
     SVGTWEAGSF DFYDLETNYI NKNGYTRYWN DTAKVPYLYN ASNKRFISYD DAESIGYKTA
     YIKSKGLGGA MFWELSGDRN KTLQNKLKAD LPTGGTVPPA DTTAPSVPGN ARSTGVTVNS
     VTLAWNASTD NVGVTGYNVY NGANLAASVN GTTATISGLS AGTSYTFTIK AKDAAGNLSA
     ASNAVTVSTT TQPGGDTQAP TAPTNLASTA QTTSSITLSW AASTDNVGVT GYDVYNGTAL
     ATSVTGTTAT ISGLAADTSY TFTVKAKDAA GNSSVASNAL TVKTAAGTTN PGVSAWQANT
     AYTVGQLVTY SGKTYKCLQS HTSLPGWEPS NVPALWQVQ
//
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