ID F8WSQ1_9NEIS Unreviewed; 844 AA.
AC F8WSQ1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Family 18 chitinase {ECO:0000313|EMBL:BAK53888.1};
GN Name=chiD {ECO:0000313|EMBL:BAK53888.1};
OS Chitiniphilus shinanonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Chitiniphilus.
OX NCBI_TaxID=553088 {ECO:0000313|EMBL:BAK53888.1};
RN [1] {ECO:0000313|EMBL:BAK53888.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SAY3 {ECO:0000313|EMBL:BAK53888.1};
RX PubMed=22178339; DOI=10.1016/j.jbiosc.2011.10.018;
RA Huang L., Garbulewska E., Sato K., Kato Y., Nogawa M., Taguchi G.,
RA Shimosaka M.;
RT "Isolation of genes coding for chitin-degrading enzymes in the novel
RT chitinolytic bacterium, Chitiniphilus shinanonensis, and characterization
RT of a gene coding for a family 19 chitinase.";
RL J. Biosci. Bioeng. 113:293-299(2012).
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DR EMBL; AB649129; BAK53888.1; -; Genomic_DNA.
DR AlphaFoldDB; F8WSQ1; -.
DR BRENDA; 3.2.1.14; 13869.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd12214; ChiA1_BD; 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; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF02839; CBM_5_12; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 3.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
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:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..844
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003385729"
FT DOMAIN 365..810
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 116..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 89749 MW; 20AC1D8AA378B38F CRC64;
MNRNARNLRL LAAGLVALLT AAGLYAAPWA EGSTYTAGTV VQYNGKDYKA LVTHTAYVGT
NWNPAATPTL WQVVTSSPTP TPTPVVTPTP TPVVTPTPTV TPTPVVTPTP TPVVTPTPTP
VVTPTPTPVV TPTPTPVTPT PPAGTCPTWA PGLSITAGSS LLYNGKSYKA LVTHTAQAGW
DPASVGALFQ PDTACGGTTP TPTPGGPTPT PAPTTPFCAP EWVATKIYPK GKVVGYKGAA
YEALVDTYAI PPDSTVYTNQ WKLVGVPNGD LCPVSVPNNI NYGTAQPVTG NANSGVVKPA
GAISATRISN TASTAAAGTR GGINPATDPG GNHPGFDADT GGRVAKLPPG TLTLQHNVYT
ATAGQERVAY LGDWAIYGRR FDFSKLPVKN LDRLVYGFAG ICFPAAKNTQ DPGFPTTAPA
AVNRTCGLGT TKLPDGAMAM ADYEAAFLRN QPGGQTAKIS GIEGMYEIGK DDVGGVFGVL
YNLRKANPNL KLDLSVGGWT LSEGFPWMAS DPTRRKVFVD SIVAFLERYD FDGIDIDWEY
PASDGAVPGM ARPDDPQNYL QLLKDLRAAM DWLTVKTGKK YRLSSAIPAT QGKIDKLAWT
EINKYLDRLY VMTYDLTGAW ERNISHHTPL YNNPNANGSS TGSSASWMIE YLNRQYGVPF
NKMMIGVANY HRSKAILPGD ITEYTNGLKG DTTFGDPNWT GTSFITGIAG VGSWEAGVVE
GYDLYQNYLD REIKPRNGYH LYTDKLSNAD FAVNPIGPSG WSYISLETPR TAGLKAQYAK
DKGLAGVFFW QIEQDNGYNL NAVNHVLGNT LVSDVADGKP QDQIATCGEN VTAAECKELI
KSIK
//