ID A0A418YFB5_9GAMM Unreviewed; 793 AA.
AC A0A418YFB5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:RJG47884.1};
GN ORFNames=D1Z90_09225 {ECO:0000313|EMBL:RJG47884.1};
OS Motilimonas pumila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadales genera incertae sedis; Motilimonas.
OX NCBI_TaxID=2303987 {ECO:0000313|EMBL:RJG47884.1, ECO:0000313|Proteomes:UP000283255};
RN [1] {ECO:0000313|EMBL:RJG47884.1, ECO:0000313|Proteomes:UP000283255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLHSC7-2 {ECO:0000313|EMBL:RJG47884.1,
RC ECO:0000313|Proteomes:UP000283255};
RA Wang F.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RJG47884.1, ECO:0000313|Proteomes:UP000283255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLHSC7-2 {ECO:0000313|EMBL:RJG47884.1,
RC ECO:0000313|Proteomes:UP000283255};
RA Wang F.-Q., Ren L.-H., Lin Y.-W., Sun G.-H., Du Z.-J., Zhao J.-X.,
RA Liu X.-J., Liu L.-J.;
RT "Motilimonas pumilus sp. nov., isolated from the gut of sea cucumber
RT (Apostichopus japonicus).";
RL Submitted (JAN-2019) 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:RJG47884.1}.
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DR EMBL; QZCH01000010; RJG47884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418YFB5; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000283255; Unassembled WGS sequence.
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:0004568; F:chitinase activity; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd02848; E_set_Chitinase_N; 1.
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; 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; IPR013540; ChitinaseA_N.
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 InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF08329; ChitinaseA_N; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 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; SSF81296; E set domains; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
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:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000283255};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..793
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019413866"
FT DOMAIN 166..597
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 621..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 84696 MW; E3722E18B5D3D79A CRC64;
MTSQRNGLMK RNLLAASILA AVSGSVMAAP AAPSIDMYGS NNLQFSKIQL AMDTTSGYNS
MVQYNEEAEI GIKFNQWSGT PGDTYRVLFD GVEVATGPIT GSQTTTSFKY SKGGVYQVVI
EACDSTGCTA SAAAELTLAD TDGSHLAPLT MNIDPNNKTY NTDKNTVVGT YFVEWGIYER
GYTVDNIPAD NLTHILYGFI PICGPNESLK SVGGNSYNAL KTACQGVNDY EVVIHDPWAA
YQKSFKQAGH DFNTPIKGNF AMMMALKNRY PDLKIVPSIG GWTLSDPFFD FTDKANRDVF
VASTKKFLQT WKFFDGVDID WEFPGGGGEN ASLGDPVNDG PAYIALMAEL RAMLDELSLE
TGKEYEVTSA IGVGYDKIED VDYGQAVQHM DYIFAMTYDF YGGWNNVPGH QTALYCGSFM
APGQCDGTGV DAEGVPFKGP AYTADNGIQL LLAQGVPANK LVLGAAMYGR GWDGVMPSSL
TDPNDPMTGT GNGKLTGTKA QGVWEAGVID YKGIKEYMLG ANNQGINGFE YGYDEQAQAP
YVWNRSTGQL ITFDDDRSTK TKGAYVRDLG LAGIFSWEID ADNGDILNAM HEGLAGYVPV
TPVPTEPPVT EVPVTEAPVT EAPVTEAPVT EAPVTEAPVT EAPVTEAPVT EAPVTEAPVT
EAPVTEAPVT EAPVTGVTPW VAGSTKVANG DVVSYMGACF QAKNNPGTWE APKAGGNWFW
TEVPCEGGVV TPTDAPVVTE APTIPGGGSN WDASAVYTGG QQVTVNGVTY EAKWWTQGDN
PEQAGDWGVW KKL
//
