ID A0A1Q7VZ10_9ACTN Unreviewed; 435 AA.
AC A0A1Q7VZ10;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=CBM2 domain-containing protein {ECO:0000259|PROSITE:PS51173};
GN ORFNames=AUG49_15230 {ECO:0000313|EMBL:OLE23740.1};
OS Catenulispora sp. 13_1_20CM_3_70_7.
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE23740.1, ECO:0000313|Proteomes:UP000186605};
RN [1] {ECO:0000313|EMBL:OLE23740.1, ECO:0000313|Proteomes:UP000186605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC galactose ester bond in pectin. Active against paranitrophenyl-acetate,
CC methyl ferulate and wheat arabinoxylan.
CC {ECO:0000256|ARBA:ARBA00025250}.
CC -!- SIMILARITY: Belongs to the faeC family.
CC {ECO:0000256|ARBA:ARBA00010278}.
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:OLE23740.1}.
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DR EMBL; MNJN01000242; OLE23740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7VZ10; -.
DR ESTHER; 9actn-a0a1q7vz10; FaeC.
DR Proteomes; UP000186605; Unassembled WGS sequence.
DR GO; GO:0030600; F:feruloyl esterase 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 Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR043595; FaeB/C/D.
DR PANTHER; PTHR38050; -; 1.
DR PANTHER; PTHR38050:SF1; FERULOYL ESTERASE C; 1.
DR Pfam; PF00553; CBM_2; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..435
FT /note="CBM2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013225938"
FT DOMAIN 326..435
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 44484 MW; FF9C4AD4FD696A6F CRC64;
MGPVALAMLL VALISALVAS QGLGSAAAAP LGAQAATTAG CGKAPLASGT HTIQSGGQTR
SYILRVPANY DNNHPYRLIF GLHWRGGTMN DVDSGGTDGY NWSYYGLRKL ADADGNGTIF
VAPQGNGNGW ANPNNQDVNF IDDVLSQLES GLCVDTSLVF SGGFSYGAAM SYALACARPN
EFRAVAVYSG ANLSGCSPGT QPVGYIGLHG LRDDVLPIAN GRSLRDTFVR NNGCTPQNPP
EPAQGSLTHI VTAYSGCKPG YPVTWAAFDG AGHDPGPIDG CTCDGWHTWT SGVVWNFFTQ
FQSSTSSSSS SSSSSSSSSS SSSSSPPPPP GGCKVADAVN GWNTGLTESI TITNTSSNAI
SNWSLVFTLR PGQTITSGWN ANYSPNSGQV TATNVSYNGS LPPGGSTTIG FQGTHTGDAG
APASFSLNGQ TCSAG
//
