ID A0A0C1DW46_9FLAO Unreviewed; 1613 AA.
AC A0A0C1DW46;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KIA98535.1};
GN ORFNames=OA93_08515 {ECO:0000313|EMBL:KIA98535.1};
OS Flavobacterium sp. KMS.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA98535.1, ECO:0000313|Proteomes:UP000031466};
RN [1] {ECO:0000313|EMBL:KIA98535.1, ECO:0000313|Proteomes:UP000031466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:KIA98535.1,
RC ECO:0000313|Proteomes:UP000031466};
RA Smith A.K., Newman J.;
RT "Flavobacterium sp. KMS.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIA98535.1}.
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; JSYP01000007; KIA98535.1; -; Genomic_DNA.
DR RefSeq; WP_039112752.1; NZ_JSYP01000007.1.
DR STRING; 1566023.OA93_08515; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000031466; Unassembled WGS sequence.
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; cd06548; GH18_chitinase; 1.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR013784; Carb-bd-like_fold.
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 InterPro; IPR013783; Ig-like_fold.
DR NCBIfam; NF033708; T9SS_Cterm_ChiA; 1.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF49478; Cna protein B-type domain; 2.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS01095; GH18_1; 2.
DR PROSITE; PS51910; GH18_2; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000031466};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1613
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002148839"
FT DOMAIN 25..462
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1178..1519
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1613 AA; 172764 MW; 255B2BAA7A41145B CRC64;
MKHYYRLLLL FLFPIVLFAQ PAHNKKVVGY YAQWAIYARD FNVPKIDGSK LTHLNYSFYG
TTFDPAHPEN TKLKCLDTYA DFEHMEGGIP WDAPVKGNFY DLMKLKQKYP HLKILISVGG
WTKGQDLSPI SASPVARAAL AADMANFLVT YPFIDGFDID WEYPLSGGTD GTEVINGAPI
PPQKYSPDDN KNLVYLLKAM RQAMPNKLVT IAAGNNVRKV GAQYLGPNNR AQYGMTEDIS
TYCDYITYFG YDFGGNWYDK TCYNAPLYPS GNTNDPLYNA TQSESLDELT NQYLNVIGIP
ANKLVMGLPF YGKIFKNVGT TNTVPNMPGL FVTAPRDAVS GCTNPQNPTG TWDGPAACEK
SGSIEICDLV GNPVTNSHPY LDPNTMLVTP AAASAGWVRY WDNATKVPYL YNASLHQFIS
YEDKQSMELK AEYIKSKNLG GGMIWELSQD TRGAIPNALL GQVNTTFSAA VIGTLTVSGS
VKNGTNLVPA VTVQLKDATN AIVQTVNSTD GNYTFNNVVS GANYTVTALK ASYTFTSVTL
TNLVANQANV VIQGTQPLYT ISGTVLDGTT AVSGVTVTAT AGTTTFTAVT NASGAYTVTA
LTAGLNYTVT AAKTGVTFTP ASTVYSVLSE NKVLNFTQTV YYTISGSVMN GATAVSEATV
TATSTAGTFT SVSSATGAYS IANLPSGANY TVTIAKAGVT FSPASTVYNN LTASKVLNFT
QNAAPASKIS GTVKNGSNPV AGAKVELIFN WTDNAHPYAS FLATTDAQGK YSFDNAIFSG
YTIIASLKMN SWQNNDVTYS PSNLTNLPIP ATSQVYDFST GTVAPLKVAG ESVPSEVVAV
SETKTPSVTT VDKSLVESKV LSVTQELVAP GTIISGTVKN GTTPVSGAKV ELVVPWTDST
HNWKSVIATT DAQGVFSYDN TVTAGYTQVL SLKLNGWENN NTAYFPNNLV NFAMPTTPQV
YNFNTNTVSP PQVTITAPSA ATVAIALGTA IQLKATASVD ASLTISSVVF NINGQNITAA
LSGTEYVANW TPVAADFNKN YTLKATVTAS SGTTAENTKA FSLQCSGTTC PNSLPVIAWV
SPATTTINQP SGFQPVALSV NVTDADGTIA SVSVSINGTS FPMTKGTGNA YNYTFTPNAY
VTYSLIVKAI DNAGGEKLLN QSITITNSTR IFIPLPAKVL LGYAHSWENA GAPFLYFSQM
VGSKFNVVDY SFVETVNRDG YTPVLTTNDT RYLTNGVFDK QLLKNDIKTL RDSGVPVIVS
IGGQNGHVVL DNVTQKNIFV NGLKAIIDEY QFDGVDIDFE GGSMNFNAGA LRDISYAGIS
AYPRLKNVVD AFKELKAYYG PGFLLTAAPE TQYVQGGYST YNDTFGSFLP IIQNLRNELD
LLAVQLYNTG GENGLDGQYY GSAKKSNMVT ALTDMIIKGY NIATTGMRFD GLPASKVLIA
LPACPSAAGS GYLTPTEGIN AMHYLRTGTT FTGRTYTMQP GGPYPSLRGL MTWSVNWDAS
SCGNSSELSK AYAAYFASQT AKIKAEDKIE VTSNKTIAYF KDNALAISNE ANNIGKVEVY
NTIGQSILSY ENIQNSNNLL LENRSFITKQ LFIVVVTDKS GNRKSFKVMN FLN
//
