ID A0A3M2LPE8_9ACTN Unreviewed; 860 AA.
AC A0A3M2LPE8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=EBO15_34380 {ECO:0000313|EMBL:RMI37965.1};
OS Actinomadura harenae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2483351 {ECO:0000313|EMBL:RMI37965.1, ECO:0000313|Proteomes:UP000282674};
RN [1] {ECO:0000313|EMBL:RMI37965.1, ECO:0000313|Proteomes:UP000282674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-Ht49 {ECO:0000313|EMBL:RMI37965.1,
RC ECO:0000313|Proteomes:UP000282674};
RA Hu J.;
RT "Isolation from soil.";
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:RMI37965.1}.
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DR EMBL; RFFG01000095; RMI37965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2LPE8; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000282674; 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:0005975; P:carbohydrate metabolic 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 6, ISOFORM C; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..860
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018117007"
FT DOMAIN 15..126
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 124..235
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 242..328
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 337..422
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 426..854
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 323..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 89404 MW; E0D3778C8E657478 CRC64;
MRRLLAALIA VFVTAALAAP AHAADGRLTA AFSLSGTTGK YVVSNPGTTA VSGWTLVFEL
PSGVTASNPQ NATITQNGTK VTLKPAFYID TLQGGKNTEP YSPTFTLSQA VQPTSCLLNG
ANCDGTGAPP PTLTGVTADY SVSGSTGTFV IANHGTAAVN GWTVVFTLPS GVTASNANNG
SISQTGTTVT LTPAYFNTTI AAGKTTDPYS PTFTLSSSGA EPTSCRVNDV NCDGTPDTPP
SAPTGLKVVV KTTKTVTLGW DAAKAGSLPV TGYDVYNGST VAASVSDTTA TIGGLTPNTA
YSFTVKAKDR KGGASAASAA VSVTTNNPSD DTTPPSVPGN LHSTGKDSSS VKLAWDASTD
NTGVANYDVL VNGATATTVT GTSATVTGLS PSTTYAFTVL ARDQYDNVSA QSTPLQVTTA
DVVSGYARVG YFVQWGIYGR QYFVKNLDST GNAAKLTHIN YAFGNIDPTN LTCLEGVTKG
TTSDPEDPSQ GDGAGDADAD YARPMSAAQS VDGQADTGYE PLRGNFNQLR KLKAKYPNLK
ILISLGGWTY SKYFSDVAAT DASRKKFVSS CIDTYIKGNL PSYNGAGGAG TAAGIFDGID
VDWEWPGAEG HPGNHVGAND KANLTLLLAE FRSQLDALGK QNSKRYLLTA FSPADPAKIS
AGWDLPGTAK SLDIYNVQGY DFHGAGSDNS WEPNRTGHAG NLYTDTNDPY SFHFSVENAV
NAYLTAGVNP RKLDIGFAYY GRGWQGVTDG GVHGEWQAAQ GAAPGQFQEE AGTRGYSNLM
SSVPNCTVYH NEQAVASYCY TGNGGQWWSF DDPWSIGKKT AWLKSKGLLG AMIWELSGDT
GTLTTALDTG LGQIAAAKRK
//