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Database: UniProt
Entry: A0A177HXD2_9ACTN
LinkDB: A0A177HXD2_9ACTN
Original site: A0A177HXD2_9ACTN 
ID   A0A177HXD2_9ACTN        Unreviewed;       894 AA.
AC   A0A177HXD2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Xyloglucanase {ECO:0000313|EMBL:OAH15370.1};
DE            EC=3.2.1.- {ECO:0000313|EMBL:OAH15370.1};
GN   ORFNames=STSP_12330 {ECO:0000313|EMBL:OAH15370.1};
OS   Streptomyces jeddahensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH15370.1, ECO:0000313|Proteomes:UP000077381};
RN   [1] {ECO:0000313|EMBL:OAH15370.1, ECO:0000313|Proteomes:UP000077381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA   Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA   Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Streptomyces sp. G25.";
RL   Submitted (DEC-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:OAH15370.1}.
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DR   EMBL; LOHS01000044; OAH15370.1; -; Genomic_DNA.
DR   RefSeq; WP_067273060.1; NZ_LOHS01000044.1.
DR   AlphaFoldDB; A0A177HXD2; -.
DR   STRING; 1716141.STSP_12330; -.
DR   PATRIC; fig|1716141.3.peg.1302; -.
DR   OrthoDB; 9764804at2; -.
DR   Proteomes; UP000077381; 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, ECO:0000313|EMBL:OAH15370.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OAH15370.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077381};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..894
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008063321"
FT   DOMAIN          784..894
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          759..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  94148 MW;  D006B8923A9DEB8F CRC64;
     MRRTRTLTAA LALAAGLLVG SPPAVAAADD PVTIAADTYT WKNVRIDGGG FVPGIVFNRT
     EKDLAYARTD IGGAYRWQES TKTWTPLLDS IGWDDWGHTG VVSLASDSVD PDKVYAAVGT
     YTNDWDPGNG AVLRSSDRGA SWQKAELPFK LGGNMPGRGM GERLAVDPHD NSVLYLGAPS
     GKGLWRSTDS GATWSEVTSF PNPGNYAQDP NDTSGYASDN QGIVWVTFDE STGSGTSKTQ
     TIYVGVADKD NAVYRSTDAG ATWSRVAGQP TGYLAHKGVL DAENGYLYLA YSDTGGPYDG
     GKGQVWRHAT ATGEWKNISP VAEADTYYGF SGLSVDRQNP GTVMVTGYSS WWPDTQIFRS
     TDSGGTWTRA WDYTSYPNRE NRYTMDVSSS PWLTWGANPS PPEETPKLGW MTESLEIDPF
     NSNRMMYGTG ATIYGTENLG QWDSGGKITI KPMVQGLEET AVLDIASPPS GAPLLSGLGD
     IGGFRHTDLT KVPPMMYTSP NFTSTTSLDF AETKPDVVAR VGTIDSGAHV AFSTDNGANW
     FAGQDPSGVT GGGTIAAAAD GSRFVWSPDG TGVQTTSGYG SSWTASSGIP AGAIVESDRV
     DPKKFYGFKS GKFYVSTDGG VTFTEKASTG LPAEGDVRFK AVPGEEGDIW LAGGSANGTY
     GLWHSKDAGA TFTKLSSIEQ ADTIGFGKAA PDASYQTLYT SAKIGGVRGI FRSTDAGESW
     VRINDDAHQW GWTGAAITGD PRVYGRVYVS TNGRGIVYGD TAATGGETDP GEGDGDGDGD
     GDTDPPAEGA CAVTYKITNE WSGGFQADVT LTNIGDEAWS GWSLGWSFPD GQKVSQAWNA
     SHTQDGSAVT VKDVGWNANV APGASVAIGF TRSSSGTNGK PTAFAVGEEA CTVT
//
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