ID A0A328VEL3_9CHLR Unreviewed; 965 AA.
AC A0A328VEL3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=CBM2 domain-containing protein {ECO:0000259|PROSITE:PS51173};
GN ORFNames=A4R35_07020 {ECO:0000313|EMBL:RAQ95281.1};
OS Thermogemmatispora tikiterensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC Thermogemmatisporaceae; Thermogemmatispora.
OX NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ95281.1, ECO:0000313|Proteomes:UP000248706};
RN [1] {ECO:0000313|EMBL:RAQ95281.1, ECO:0000313|Proteomes:UP000248706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T81 {ECO:0000313|EMBL:RAQ95281.1,
RC ECO:0000313|Proteomes:UP000248706};
RA Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA Levin D.B.;
RT "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT Carbohydrate Degradation Ability.";
RL Submitted (AUG-2016) 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:RAQ95281.1}.
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DR EMBL; MCIF01000002; RAQ95281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328VEL3; -.
DR OrthoDB; 9801859at2; -.
DR Proteomes; UP000248706; 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; 2.
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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000248706};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..965
FT /note="CBM2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016376012"
FT DOMAIN 856..965
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 809..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..849
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 102057 MW; C243CBF725BE19F1 CRC64;
MPLLALFAIL LPTITLASVH SRAASAAPAA TQPYTWQNVV TGGGGGFVVD VVFNPKQKDL
IYARTDIGGA YRWNPSTGTW TQLMAWVTPD NWNMAGVESI ATDPVQPNRL YIAAGMYTNN
WTNQNGVILR STDYGNTFQI TQMPFKMGGN MPGRGMGERL AVDPNDDAIL YFGARSGNGL
WRSTDYGVTW SKVTNFPDTG PFAENPNDPS GYLSDPVGVV WVTFDPSTGT PGSPTKTIYV
GVADNRSGAY NIYRSTDAGA TWAPIPGEPT CNVSGTTVTC TGGATWSTTS DASTGYLPHQ
GKVDSQGTLY VTYSDWEGPY NGSRGDVWKF TPSSGTWTKI SPVPGSDSAN DYFGYGGLAV
DWQHPGTIVV ASVNSWWPDA QLFRTTNGGA SWEPIWTWAS YPNRNLYYTI DVSNAPWLDF
GNKNPVPPVP AVKLGWMIEG MNIDPFNSDR LMYGTGATLY STNNLTAWDN YQNGGIVNFK
STALGIEEEY VTDLVSPPAN AHLYSTMADV SGFRHDDLTK SPSEMYYIPY AGSYAAIDYA
EQNPNFMVRV GYGNPSASPP VTSTAFSYDG GATWFAGNKD IPGVSQNGGT VAAAADASRV
LWAPVNAPVS YSTDNGNSWV ASANVPQNAV VASDRVNPKK FYAYGQGKFW YSTDGGATFT
ASSATGLPQA GDSVVVKAVP GHEGDVWVAG GNAWTSDYGL WHSTDGGQTF TKLTSLAGAD
KIGFGMPAPG QSYPAIYISG IVGNVRGIFR SDDGGNTWVL INDSQHQYGN ITTITGDPRI
YGRVYLGTNG FGIVYGDIAG AATTPTPTAT VTAAPTPTAA ASPTPTPTPT PPPTVTPTPT
AAVTPTPTPI PTATSTPVAG LQCSVHYAVN QWPGGFTANL TVTNTGTTTI NGWTLTFTFP
GNQTVTQGWN GVFSQQGSQV TITNASYNGS IAPGSSVYPG FNGSWSGSNP SPTAFYLNGT
ACTIV
//
