ID A0A1Q4YIP9_9ACTN Unreviewed; 624 AA.
AC A0A1Q4YIP9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:OKI34374.1};
GN ORFNames=A6A29_19100 {ECO:0000313|EMBL:OKI34374.1};
OS Streptomyces sp. TSRI0281.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI34374.1, ECO:0000313|Proteomes:UP000186952};
RN [1] {ECO:0000313|EMBL:OKI34374.1, ECO:0000313|Proteomes:UP000186952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI34374.1,
RC ECO:0000313|Proteomes:UP000186952};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI34374.1}.
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DR EMBL; LWLE01000035; OKI34374.1; -; Genomic_DNA.
DR RefSeq; WP_073727274.1; NZ_LWLE01000035.1.
DR AlphaFoldDB; A0A1Q4YIP9; -.
DR STRING; 1718998.A6A29_19100; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000186952; 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; 1.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
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; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS50853; FN3; 1.
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:UP000186952};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..47
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 48..624
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012953729"
FT DOMAIN 44..151
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 161..246
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 256..624
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 230..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 64615 MW; 53A3F073F30B2441 CRC64;
MSTETPQRRT RFRWSLTRNG RAKAVAGFTA LLLPLAAMVG LASPASAATS ATATYLKKSD
WGSGFEGQWT VKNTGTTALS SWTIEWDFPA GTAAGSAWDA TVTSSGNHWT AKNLSWNGSI
APGASLSFGF NGTGSGSPTG CKLNGASCDG GSVPGDNAPS APGTPTASAI TDTSAKLGWS
AATDDKGIKN YDVLRDGAKV ATVTGTTYTD TALTAGTDYS YTVQARDTAD QTGPVSGAVK
VRTTGGGTGP GPGGDKVNLG YFTNWGVYGR NYHVKNLVTS GSAQKITHIN YAFGNVQGGK
CTIGDSYADY DKAYTADQSV DGVADTWDQP LRGNFNQLRK LKAKYPHIKV LWSFGGWTWS
GGFGAAAQNP AAFAQSCYDL VEDPRWADVF DGIDIDWEYP NACGLTCDTS GPAALKNLAS
ALRTKFGTSN LVTAAITADG SDGGKIDAAD YAGAAQSMDW YNVMTYDFFG AWAAKGPTAP
HSPLTSYAGI PQAGFNSADA IAKLKAKGVP AKKLLLGIGF YGRGWTGVTQ AAPGGTATGA
APGTYEAGIE DYKVLKNTCP ATGTVAGTAY AHCGTNWWSY DTPATIGAKM TWAKNQGLGG
AFFWEFSGDT ANGELVSAMG SGLQ
//
