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Database: UniProt
Entry: A0A495VST7_9PSEU
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Original site: A0A495VST7_9PSEU 
ID   A0A495VST7_9PSEU        Unreviewed;       850 AA.
AC   A0A495VST7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Chitinase (Glycosyl hydrolase family 18) {ECO:0000313|EMBL:RKT51543.1};
GN   ORFNames=C8E97_0022 {ECO:0000313|EMBL:RKT51543.1};
OS   Saccharothrix australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=2072 {ECO:0000313|EMBL:RKT51543.1, ECO:0000313|Proteomes:UP000282084};
RN   [1] {ECO:0000313|EMBL:RKT51543.1, ECO:0000313|Proteomes:UP000282084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43800 {ECO:0000313|EMBL:RKT51543.1,
RC   ECO:0000313|Proteomes:UP000282084};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) 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:RKT51543.1}.
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DR   EMBL; RBXO01000001; RKT51543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495VST7; -.
DR   OrthoDB; 3882626at2; -.
DR   Proteomes; UP000282084; Unassembled WGS sequence.
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:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 2.60.40.290; -; 2.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
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; PF00553; CBM_2; 2.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00637; CBD_II; 2.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS51173; CBM2; 2.
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:ARBA00023277};
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:UP000282084};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..850
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019861254"
FT   DOMAIN          15..125
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   DOMAIN          124..233
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   DOMAIN          240..326
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          335..420
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          424..850
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          307..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  89592 MW;  F168391B42363E5F CRC64;
     MRRLAIALVA LATIATTVTP ASAAAGLTAT FTRTGTTGKF VVSNPTSAAV TGWSIKFDVP
     AGVTVSGAQN ASTTQNGTRV TLTPAYYINT IQPGRNTDPF SPTFTLSREA DPTSCTLNGA
     NCDGTGPEPP APAPVTADFS LSGSTGKFIV ANNTDATLSD WAITFTLPSG VTASNANNGT
     VSQTGNTVTL APVHYNKSVG PRKTTEPYSP TFTLSRAVEP VTCRINNANC DGSPDVPPTA
     PGDLRSPAKT TKSVSLAWNA STAGSLPVAG YDVYNGSTLA TTVTGTSATV TGLTPNTAYS
     FTVKAKDTKG TQSPASNALS VTTNNPADDT QPPSAPGNLR GTGKDAGSVT LTWDAATDNS
     KVANYDVYQG STVRATVTET TAKIDGLSPS TEYTFSVKAR DIYDNVSGAS NSVKVTTSDI
     VGGYAKVGYF VQWGIYGRQF FVKNLDTNGA AAKLTHINYA FGNIDPVNLT CLHGVTKGTS
     PNPQDPNQGD GAGDAEADYS RPFSSAQSVD GVADTGWEPL RGNYNQLKKL KAKHPHLKIL
     ISLGGWTYSK YFSDVAATDA SRKKFVASCL DIYLKGNLPT YNGAGGPGTA AGIFDGVDLD
     WEWPGAEGHP GNHISPNDKR NNTLLIEEFR KQMDELSKTT GKRYQLTAFT PADRAKIDAG
     WELAEVAKSM DIFNVQGYDF HGSGSDNSWE PNRTGHQGNL YKDADDPYPF HFSVEDTVNA
     YLEAGVNPRK ITVGLAFYGR GWQGVQDGGK KGEWQSATGA APGQFAEEAG TRGYSNLLAS
     VPNCTVYHDE AAVATSCFTG NGGQWWTFDD AWAIQKKTAW MKQRGLLGAM IWEMSGDTGV
     LMSAVDNGLK
//
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