ID A0A136PVA8_9ACTN Unreviewed; 325 AA.
AC A0A136PVA8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Glucanase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AWW66_08250 {ECO:0000313|EMBL:KXK62470.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK62470.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK62470.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK62470.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXK62470.1}.
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DR EMBL; LRQV01000019; KXK62470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136PVA8; -.
DR Proteomes; UP000070620; Unassembled WGS sequence.
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 Gene3D; 2.60.40.290; -; 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; IPR018366; CBM2_CS.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR13817:SF73; IG-LIKE AND FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR13817; TITIN; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00041; fn3; 2.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS50853; FN3; 2.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000070620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 23..114
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 125..220
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 217..325
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 33721 MW; 355D49D142CBB8D1 CRC64;
MSAASNTVDA TSSTPPADLP PTAPRNLAVS RITSTSATLT WTAAEPGCCD ITGHTIGYFQ
AFHDLGESVR VGNVTTATIT LRPATQYRVI VQATDSAGHS SPSSDPLTII TPATDNGPDT
VPPSAPGTLT ASDVTTTSAT LNWTPSTDNV AVTGYNVYRW DGVFTSTLVA TVPGTSYTAS
LVPSVRNRYY VRARDAAGNV SIATNEVRID PPTGPTTPPP SATCTVTYQK QSEWQGGFVT
DITIMNTATT AVNGWTLDFT FPGDQRITTL WSATHAQSGS AVTIRNASWN GTIAAGASVS
FGFQGTWSGS NAAPTSFSLN GAPCL
//