ID A0A0J8CFL5_STRVR Unreviewed; 887 AA.
AC A0A0J8CFL5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Xyloglucanase {ECO:0000313|EMBL:KMS76775.1};
GN ORFNames=ACM01_02720 {ECO:0000313|EMBL:KMS76775.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS76775.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS76775.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS76775.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-2015) 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:KMS76775.1}.
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DR EMBL; LFNT01000002; KMS76775.1; -; Genomic_DNA.
DR RefSeq; WP_048579374.1; NZ_LGUR01000117.1.
DR AlphaFoldDB; A0A0J8CFL5; -.
DR PATRIC; fig|1938.3.peg.142; -.
DR OrthoDB; 9764804at2; -.
DR Proteomes; UP000037432; 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; 2.
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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..887
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009778756"
FT DOMAIN 777..887
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 760..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 93418 MW; B4734078A73E2B42 CRC64;
MRRTRILTAV LALAAGLLAG TPPALAAPAA KDVSIAADTY TWKNARIDGG GFVPGIVFNR
TEKNLAYART DIGGAYRWQE SSKTWTPLLD SVGWEDWGHT GVVSLASDSV DPDRVYAAVG
TYTNSWDPKN GAVMRSSDRG ASWQKTELPF KVGGNMPGRG MGERLAVDPN KNSVLYLGAP
SGKGLWRSTD SGVTWSQVAN FPNVGNYVQD PSDTSGYASD NQGIVWVTFD ESTGTSGNAT
KTIYVGVADK DNAVYRSTDA GATWSRVAGQ PTGYLAHKGV LDAANGYLYL AYSDKGGPYD
GGKGQLWRYA TASGTWTNIS PVAEADTYYG FAGLTVDRQK PGTVMATAYS SWWPDTQIFR
STDSGGTWTK AWDYSSYPNR ANRYTMDVSS SPWLTWGANP SPPEQTPKLG WMTEALEIDP
FDSNRMMYGT GATIYGTEDL TKWDSGSQFT IRPMVRGLEE TAVNDLASPP SGAPLLSALG
DIGGFRHTDL TKVPSMMFTQ PNFTTTTSLD FAETNPNTVV RVGNLDSGPH IAFSTDNGAN
WFAGTDPSGV SGGGTVAAAA DGSRFVWSPA GTGVQYTTGF GSSWAASSGI PSGAIVESDR
VDPKTFYGFK SGKFYVSTDG GATFTASSTT GLPSGDSVRF KALPGVKGDV WLAGGATDGA
YGLWHSTDGG ASFTKLSNVE QADAIGFGKA APGASYQALY TSAKIGGVRG IFRSVDKGAS
WTRVNDDARQ WGWTGAAITG DPRVYGRVYV ATNGRGVIYG DTADGGTTDP DPDPDPDPTP
TGACAVSYKV TNQWSGGFQA DVQLSNTGSS AWSGWSLGWT FADGQRITQV WNADHTQSGS
AVTAKNVGWN GSVAAGSSVS FGFTGSWQGA NAKPTAFKLG DQSCTVS
//