GenomeNet

Database: UniProt
Entry: A0A1Z1WSI8_9ACTN
LinkDB: A0A1Z1WSI8_9ACTN
Original site: A0A1Z1WSI8_9ACTN 
ID   A0A1Z1WSI8_9ACTN        Unreviewed;       583 AA.
AC   A0A1Z1WSI8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=SMD44_08887 {ECO:0000313|EMBL:ARX89400.1};
OS   Streptomyces alboflavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX89400.1, ECO:0000313|Proteomes:UP000195880};
RN   [1] {ECO:0000313|EMBL:ARX89400.1, ECO:0000313|Proteomes:UP000195880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDJK44 {ECO:0000313|EMBL:ARX89400.1,
RC   ECO:0000313|Proteomes:UP000195880};
RA   Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT   "Streptomyces alboflavus Genome sequencing and assembly.";
RL   Submitted (MAY-2017) 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   ---------------------------------------------------------------------------
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; CP021748; ARX89400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z1WSI8; -.
DR   STRING; 67267.GCA_000716675_04756; -.
DR   KEGG; salf:SMD44_08887; -.
DR   eggNOG; COG3469; Bacteria.
DR   Proteomes; UP000195880; Chromosome.
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; cd00063; FN3; 1.
DR   CDD; cd02871; GH18_chitinase_D-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_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; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 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:UP000195880};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..583
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012757537"
FT   DOMAIN          202..283
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          294..582
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   583 AA;  59590 MW;  3FC59DDC2E1B0942 CRC64;
     MDRVRKDRLG VRRRISAVMA VGAATALAVT ALAAPAQSAD TNTAGTKAAS TRAADVNVAK
     NAGFEADLNN WTCAANSGAA VTSPVHGGAK ALKATPSGQG TAECSQIVAV KPNSTYKLSS
     WVQGSYAYLG ARGTGTTDVS TWTPGTSSWQ QLSTSFTTGA NTTSVTVYTH GWYGQSAYYV
     DDVSVFGPDG GGGPDPVEIP PVPAGLAAGT ATPTSVELSW TPSSTATGYT VYRDGTKVAS
     SSGASTTVTG LTPETTYSFQ VSASNAAGES AKSTAVSVTT PKGDGGGDGT VPRHAVTGYW
     QNFNNGATVQ KLRDVSSQYD IIAVSFADAT PTPGQITFNL DPAVGYASTA DFKADIAAKK
     AAGKSVILSV GGEKGTISVN SDASATAFAN SAYALMQEYG FNGVDIDLEN GINPTYMTKA
     LRQLSAKAGP KMVLTMAPQT IDMQSTSGGY FQTALNVKDI LTVVNMQYYN SGSMLGCDGK
     VYSQGSVDFL TALACIQLEG GLDPSQVGIG VPASTRGAGS GYVAPSIVNN ALDCLTRGTG
     CGSFKPSKTY PSLRGAMTWS TNWDATAGHA WSNAVGPKVH SLP
//
DBGET integrated database retrieval system