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Database: UniProt
Entry: A0A429BP95_9ACTN
LinkDB: A0A429BP95_9ACTN
Original site: A0A429BP95_9ACTN 
ID   A0A429BP95_9ACTN        Unreviewed;       341 AA.
AC   A0A429BP95;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Cellulose-binding protein {ECO:0000313|EMBL:RSN14349.1};
GN   ORFNames=DMB42_07455 {ECO:0000313|EMBL:RSN14349.1};
OS   Nonomuraea sp. WAC 01424.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=2203200 {ECO:0000313|EMBL:RSN14349.1, ECO:0000313|Proteomes:UP000286861};
RN   [1] {ECO:0000313|EMBL:RSN14349.1, ECO:0000313|Proteomes:UP000286861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 01424 {ECO:0000313|EMBL:RSN14349.1,
RC   ECO:0000313|Proteomes:UP000286861};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) 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:RSN14349.1}.
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DR   EMBL; QHHZ01000002; RSN14349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429BP95; -.
DR   OrthoDB; 468550at2; -.
DR   Proteomes; UP000286861; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000286861};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..341
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018988318"
FT   DOMAIN          239..341
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
SQ   SEQUENCE   341 AA;  35414 MW;  B9100E0737C81C49 CRC64;
     MRRISALLTA MLALAGTVLF LTTGPAGAAA VRIMPLGDSI TGSPGCWRAL LWNKLQSTGY
     TGVDFVGTLP PQGCGVAHDG DNEGHGGYLA TNIANQGLLP GWPAATRPDI VVMHLGTNDV
     WSNIAPATIL GAFTTLVNQM RASNPAMRIL VAKIIPMNPP TCSECAQRVV AFDNAIPAWA
     AATTTQQSPV TVVDQWTGFS TSTDTYDGVH PNASGDQKMS DAWYPALTAA MSVTTPSPTP
     SGGAGCTAVV KTVGQWQGGF QGEVTVKNTD ASPTTGWNVG WTFADGQRIT QLWGGLLTQT
     GSSVSVRNET WNGALAPGAT TTFGFLSSWT TANTPPTPTC T
//
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