ID A0A402DTB0_9CELL Unreviewed; 513 AA.
AC A0A402DTB0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=CBM2 domain-containing protein {ECO:0000259|PROSITE:PS51173};
GN ORFNames=CBZ_24450 {ECO:0000313|EMBL:GCE77389.1};
OS Cellulomonas biazotea.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1709 {ECO:0000313|EMBL:GCE77389.1, ECO:0000313|Proteomes:UP000289954};
RN [1] {ECO:0000313|EMBL:GCE77389.1, ECO:0000313|Proteomes:UP000289954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC12680 {ECO:0000313|EMBL:GCE77389.1,
RC ECO:0000313|Proteomes:UP000289954};
RA Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA Otoguro M., Yanagida F., Hayakawa M.;
RT "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:GCE77389.1}.
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DR EMBL; BIMR01000204; GCE77389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402DTB0; -.
DR OrthoDB; 9801375at2; -.
DR Proteomes; UP000289954; Unassembled WGS sequence.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
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 CDD; cd01831; Endoglucanase_E_like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; IPR040794; CE2_N.
DR InterPro; IPR037461; CtCE2-like_dom.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR37834; GDSL-LIKE LIPASE/ACYLHYDROLASE DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_2G00620); 1.
DR PANTHER; PTHR37834:SF2; PUTATIVE-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF17996; CE2_N; 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.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..513
FT /note="CBM2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019318521"
FT DOMAIN 413..513
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 375..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 53386 MW; 65FA5180FB6FCDE9 CRC64;
MRRLRAAVAL TSIATCVALI PGAAIAVPAL AAGSVPTASS GLAATAHTAG RVAVAGDTWQ
HAWPGVYVEG RFRGTGVGIV LADTTGDYDV AVDGRTVATL VTPGSTTHRV SGLTSGEHTV
RVVKRSEVPW ATSTFGGFVP VDGSTILPAP PDRDLQLEFV GDSYTAGYGN TSTSRECTGD
QVTRTTNADL SFGALTARAL GADYQLNAFS GRGMVRNYAG GEPGTSYRTY YDRALPGVAG
DVWDRPASWQ PDAVVVGLGI NDFSTALGSG EAWASTTALR EAWVDAYHGF LDTLRSRYPD
AFLVVSATYV HTGTDLPDLA QRVVDERRAD GDDRVRYWYY GNEGLDYGGC HWHPSVRDHE
VIAGKLTAFL TALPLGGGPT PTPTPTVTPT PTPTPTPTVT PTPTPTPTPT PTPTVQPSAC
RAALTVGGRW PGGYQASVEV TATTAIRRWT TTLTLPAGGA LTQLWSGDAT TSGQVVTVTS
KDWNGTLAAG RTTVYGFLGT GTPPADGALP CSA
//
