ID A0A069JL77_9ACTN Unreviewed; 896 AA.
AC A0A069JL77;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Xyloglucanase {ECO:0000313|EMBL:KDQ65799.1};
GN ORFNames=DT87_00690 {ECO:0000313|EMBL:KDQ65799.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ65799.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ65799.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ65799.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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:KDQ65799.1}.
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DR EMBL; JJOB01000001; KDQ65799.1; -; Genomic_DNA.
DR RefSeq; WP_037881916.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069JL77; -.
DR OrthoDB; 9764804at2; -.
DR Proteomes; UP000027475; 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; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF00553; CBM_2; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 786..896
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 755..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 93102 MW; A1378AA8A9CE9674 CRC64;
MAALALTAGL AITGTPAVAR SDEAPAAMEA SDVSIAADTY TWKNARIDGG GFVPGIVFNR
SEKNLAYART DIGGAYRWDQ AGKRWTPLLD WVDWDRWGWT GVVSLASDSA DPDNVYAAVG
TYTNSWDPTT GAVLRSSDRG ASWKAATLPF KLGGNMPGRG MGERLAVDPN KNSVLYLGAP
SGNGLWRSTD AGATWSEVTA FPNPGNYAQD PTDTSGYGND NQGIVWVTFD ERSGSAGGAT
KDIYVGVADK QNTVYRSTDG GTTWSRIAGQ PTGYLAHKGV LDSATGYLYL TLSDTGGPYD
GGKGQIWRYD TGSGAWKDVS PVAEADTFYG FGGLSVDRQK PGTLMATAYS AWWPDTQIFR
STDSGATWTQ AWDYTSYPDR SNRYTLDVSS VPWLSWGASP APPETAPKLG WMTESLEIDP
FDSDRMMYGT GATVYGTENL TAWDSGGSLR ITPMVRGIEE TAVNDLASPP SGAPLLSALG
DIGGFRHTDL DAVPGMMFTS PNLDSTTSLD FAETSPGTVV RVGNSDTAPH IGFSTDNGAN
WFQGSEPSGV TGGGTVAAAA DGSGFVWSPE GAGVHHTTGY GSSWTASTGI PAGATVESDR
KNPKKFYGFA GGTFYVSTDG GATFTAKATG LPSAGNVRFQ ALPGTEGDIW LAGGSATGAY
GLWRSTDSGA TFTKAANVQQ ADSVGFGKAA PGASYQTVFV SAKIGGVRGI FRSTDAGANW
TRINDDAHQW AWTGAAITGD PRVYGRVYVS TNGRGIQVGE SSDTGGGGTG PGTDPGPDPG
TDPGTEQPGS AACAVTYTVT NEWPGGFQAD VTVTNTGDAA YDGWTLGWSF PGGQRISQMW
NASYQQDGAR VTATDAGWNG TVAPGSSAGF GFTGSRSGGN AEPSAFTLDG EVCTVG
//
