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Database: UniProt
Entry: P36909
LinkDB: P36909
Original site: P36909 
ID   CHIT_STRLI              Reviewed;         619 AA.
AC   P36909;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   01-OCT-2014, entry version 92.
DE   RecName: Full=Chitinase C;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=chiC;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8515228;
RA   Fujii T., Miyashita K.;
RT   "Multiple domain structure in a chitinase gene (chiC) of Streptomyces
RT   lividans.";
RL   J. Gen. Microbiol. 139:677-686(1993).
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
CC   -!- INDUCTION: By chitin.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
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DR   EMBL; D12647; BAA02168.1; -; Genomic_DNA.
DR   ProteinModelPortal; P36909; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; -; 2.
DR   InterPro; IPR008965; Carb-bd_dom.
DR   InterPro; IPR012291; CBD_carb-bd_dom.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR001919; Cellulose-bd_dom_fam2_bac.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR001223; Glyco_hydro18cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
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; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 2.
DR   SUPFAM; SSF54556; SSF54556; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS01095; CHITINASE_18; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL        1     30       {ECO:0000255}.
FT   CHAIN        31    619       Chitinase C.
FT                                /FTId=PRO_0000011911.
FT   DOMAIN       31    134       CBM2.
FT   DOMAIN      144    229       Fibronectin type-III.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   REGION      240    619       Catalytic.
FT   ACT_SITE    382    382       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10053}.
SQ   SEQUENCE   619 AA;  65200 MW;  A23CEE5B3C5D6F21 CRC64;
     MRFRHKAAAL AATLALPLAG LVGLASPAQA ATSATATFAK TSDWGTGFGG SWTVKNTGTT
     SLSSWTVEWD FPTGTKVTSA WDATVTNSGD HWTAKNVGWN GTLAPGASVS FGFNGSGPGS
     PSNCKLNGGS CDGTSVPGDA APSAPGTPTA SNITDTSVKL SWSAATDDKG VKNYDVLRDG
     AKVATVTGTT YTDNGLTKGT AYSYSVKARD TADQTGPASG AVKVTTTGGG DGGNPGTGAE
     VKMGYFTNWG VYGRNYHVKN LVTSGSADKI THINYAFGNV QGGKCTIGDS YADYDKAYTA
     DQSVDGVADT WDQPLRGNFN QLRKLKAKYP NIKILYSFGG WTWSGGFPDA VKNPAAFAKS
     CHDLVEDPRW ADVFDGIDLD WEYPNACGLS CDETSAPNAF SSMMKAMRAE FGQDYLITAA
     VTADGSDGGK IDAADYGEAS KYIDWYNVMT YDFFGAWAKN GPTAPHSPLT AYDGIPQQGF
     NTADAMAKFK SKGVPADKLL IGIGFYGRGW TGVTQSAPGG TATGPATGTY EAGIEDYKVL
     KNSCPATGTI AGTAYAHCGS NWWSYDTPAT IKSKMDWAEQ QGLGGAFFWE FSGDTANGDW
     WRHRQRPQVT PAVRTTRRH
//
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