ID L7F8I0_9ACTN Unreviewed; 371 AA.
AC L7F8I0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cellulose binding domain protein {ECO:0000313|EMBL:ELP67346.1};
GN ORFNames=STRTUCAR8_09322 {ECO:0000313|EMBL:ELP67346.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP67346.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP67346.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP67346.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
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:ELP67346.1}.
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DR EMBL; AEJB01000291; ELP67346.1; -; Genomic_DNA.
DR RefSeq; WP_006377533.1; NZ_AEJB01000291.1.
DR AlphaFoldDB; L7F8I0; -.
DR STRING; 85558.T45_05004; -.
DR PATRIC; fig|698760.3.peg.3922; -.
DR Proteomes; UP000010931; 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 Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..371
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003973298"
FT DOMAIN 260..367
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 371 AA; 38307 MW; 633992E799D76D2A CRC64;
MRSTRHLPPL RILLATLLLS LGVALAPTAT AAPGTTAADT TAPAAAAAVR IMPLGDSITG
SPGCWRAMLW NSLQSAGYTN IDFVGTLNQQ GCAQAHDGDN EGHGGEQVTA VADQNLLPAR
LSATRPDIVV MHFGTNDVWS SFTPDRVLAA YTTLVQQMRA SNPDMKILVA QLIPLNPDNC
TGCAQRVVDF NARIPDWART TSTSRSPVTV VDQWTGFNTA TDTYDGVHPS DPGNQKIAAR
WYPALSALLV KGDPGDPGDP GGEEPACTAT FRAVSSWQGG YQGEVTVTNA SASPVSGWTA
TVVPATGARL TQLWNGSLTT AADGSATVTN AAWNGTLAPG ASATFGFIAT TPTTASTPSA
TVGCTARAAI S
//
