ID D9X2U2_STRVT Unreviewed; 503 AA.
AC D9X2U2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Cellulose-binding protein {ECO:0000313|EMBL:EFL35779.1};
GN ORFNames=SSQG_06297 {ECO:0000313|EMBL:EFL35779.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL35779.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
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 viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657757; EFL35779.1; -; Genomic_DNA.
DR RefSeq; WP_003993916.1; NZ_GG657757.1.
DR AlphaFoldDB; D9X2U2; -.
DR STRING; 591159.SSQG_06297; -.
DR eggNOG; COG1595; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_037519_0_0_11; -.
DR OrthoDB; 3401948at2; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR Pfam; PF00553; CBM_2; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 233..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 394..502
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 53330 MW; 3D0F9E10425445DD CRC64;
MPDLPTPQDA AEAALFSECW DAVLAYADLC TSGSTAAAQL GREAFAHGTR EARAAEAGPV
RSAGRRPARL PRIPLLLTAV RTMAASWEED GQGHKLDPDL RLWLNSDKAA RYTGPPLQRP
LALRGLRDLQ QADAELLWLA EVEALDLPVV ARRLGLDPDT VAEELQQVRT LFRDRCHRNH
LDTPMDARCR SYARLLDAVT RSCAADAPGD LSRHLATCVQ CAEAAACLRL HGGGLPGALA
GGVIGWGGLA YLERRRRAAE VRLGAGRPGP AGKAAGEEED GTQKARVARN GLLVAAVLVS
LLALGVSMMP FGGSGDDLGA RGDARRQPVA DPNPSLPSPP SLPPATSKPA ATATATASEG
EEHTERPGKP EDGDDDRRTE PQGTSSPTGR TEPGESEDPA CRVEYDLVNQ WPDGFQATVT
VTSSAALDSW RVSWSFRDGQ RVGQMWDASV SQDGSRVTAT AADYNKSVPA GSDLAFGFIA
SWRGKNSPPY GFTLNGHDCA KSG
//
