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Database: UniProt
Entry: D9XYE3_9ACTN
LinkDB: D9XYE3_9ACTN
Original site: D9XYE3_9ACTN 
ID   D9XYE3_9ACTN            Unreviewed;       348 AA.
AC   D9XYE3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Cellulose-binding, family II, bacterial type {ECO:0000313|EMBL:EFL42751.1};
GN   ORFNames=SSRG_05555 {ECO:0000313|EMBL:EFL42751.1};
OS   Streptomyces griseoflavus Tu4000.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL42751.1, ECO:0000313|Proteomes:UP000002968};
RN   [1] {ECO:0000313|EMBL:EFL42751.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu4000 {ECO:0000313|EMBL:EFL42751.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG657758; EFL42751.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9XYE3; -.
DR   STRING; 467200.SSRG_05555; -.
DR   eggNOG; COG2755; Bacteria.
DR   HOGENOM; CLU_044083_0_1_11; -.
DR   Proteomes; UP000002968; 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; cd01833; XynB_like; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
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; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR30383:SF2; CELLULOSE-BINDING PROTEIN; 1.
DR   PANTHER; PTHR30383; THIOESTERASE 1/PROTEASE 1/LYSOPHOSPHOLIPASE L1; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
PE   4: Predicted;
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..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..348
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003132591"
FT   DOMAIN          240..347
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
SQ   SEQUENCE   348 AA;  35491 MW;  5B63496A677704D3 CRC64;
     MAALLLPLGA TTAAAAPTAA DPTVADPVRI MPLGDSITGS PGCWRALLWN RLLDAGHTDI
     DFVGTLPAQG CGVAHDGDNE GHGGELVTNV ADQNLLPARL AATLPDIVVM HFGTNDVWSS
     VSPDRILAAY TKLVRQMRES NPDMRVLVAR IIPMNPATCA ACAQRVVDFN ARIPAWAAAT
     GTDRSPVTVV DQWTGFDTAT DTYDGVHPND AGNVKIAAHW FPALDALLDE GVPGGPGDPG
     GPGDATCTAS FRAVSVWQGG YQGEVTVRNT SAAPVTGWKV TVVPSGGARV GQVWNGTLGT
     AADGTATVTD AGWNGSLAPG ASAAFGFIAT TPATSTAPTA TVDCTAAS
//
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