ID   A0A1A5PDH5_9ACTN        Unreviewed;       898 AA.
AC   A0A1A5PDH5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Xyloglucanase {ECO:0000313|EMBL:OBQ53483.1};
GN   ORFNames=A4U61_04690 {ECO:0000313|EMBL:OBQ53483.1};
OS   Streptomyces sp. H-KF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1727216 {ECO:0000313|EMBL:OBQ53483.1, ECO:0000313|Proteomes:UP000093719};
RN   [1] {ECO:0000313|Proteomes:UP000093719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-KF8 {ECO:0000313|Proteomes:UP000093719};
RA   Undabarrena A., Ugalde J.A., Seeger M., Camara B.;
RL   Submitted (APR-2016) 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:OBQ53483.1}.
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DR   EMBL; LWAB01000002; OBQ53483.1; -; Genomic_DNA.
DR   RefSeq; WP_065000765.1; NZ_LWAB01000002.1.
DR   AlphaFoldDB; A0A1A5PDH5; -.
DR   OrthoDB; 9764804at2; -.
DR   Proteomes; UP000093719; 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   Reference proteome {ECO:0000313|Proteomes:UP000093719};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..898
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008334372"
FT   DOMAIN          788..898
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          769..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   898 AA;  94906 MW;  04BECC7CB99D81B0 CRC64;
     MRRTRVLTAV FALAAGLLTG GPPALAAAPP DRPAAESDAP ARSALAADTY TWKNARIDGG
     GFVPGIVFNR SEKNLAYART DIGGAYRWQE ATKSWTPLLD SVGWDDWGHT GVVSLASDPV
     DPDRVYAAAG TYTNDWDPGN GAVLRSTDRG ASWRKAGLPF KLGGNMPGRG MGERLAVDPH
     RNSVLYLGAP SGKGLWRSTD SGASWSQVTA FPNPGTYVQD PGDTSGYASD NQGIVWVTFD
     ESTGTPGSAT RTIYVGVADT ENAVYRSTDA GATWQRVAGQ PTGYLAHKGV LDTENGHLYL
     AYSDKGGPYD GGKGRLWRYT TATGTWTDIS PVAEADTYYG FSGLTVDRQN PGTLMATAYS
     SWWPDTQIFR STDSGATWTQ AWDYSPYPDR VDRYTMDVSS VPWLTWGADP SPPEQSPKLG
     WMTEALEIDP FDPDRMMYGT GATVYGTENL TNWDRDATFT IAPMVRGLEE TAVNDLISPP
     SGAPLLSGLL DIGGFRHTDL TKVPSMMFTQ PNFTATTSLD FAESRPDTMV RAGDLDSGPH
     IAFSTDNGAH WFAGTDPSGV SGGGTVAAGA DGSRFVWSPR GAGVHHTTGF GTSWSASSGI
     PEGAVVESDR VDPKTFYGFK SGKFYVSTDG GATFAASPAT GLPSGDSVRF KALPGTKGDI
     WLAGGESGGT YGLWHSVDGG QSFTRLRGVD EADTVGFGKA APGASYRTVF TSAKIDGVRG
     IFRSTDRGQS WTRINDDAHQ WGWTGAAITG DPRVYGRVYV ATNGRGIVYG DTSETGGGDD
     GGGGTDPGPD PAGACKVTYE VTNQWSDGFQ AQVQVVNTGS DAWNGWSLAW SFADGQRVSQ
     LWNGAHTQSG PTVTVRNTDW NGTVAAGSSV GFGFTASRSG TNTKPAAFTL GGRTCTVT
//