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Database: UniProt
Entry: A0A402DSD9_9CELL
LinkDB: A0A402DSD9_9CELL
Original site: A0A402DSD9_9CELL 
ID   A0A402DSD9_9CELL        Unreviewed;       742 AA.
AC   A0A402DSD9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=CBM2 domain-containing protein {ECO:0000259|PROSITE:PS51173};
GN   ORFNames=CBZ_20420 {ECO:0000313|EMBL:GCE76986.1};
OS   Cellulomonas biazotea.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1709 {ECO:0000313|EMBL:GCE76986.1, ECO:0000313|Proteomes:UP000289954};
RN   [1] {ECO:0000313|EMBL:GCE76986.1, ECO:0000313|Proteomes:UP000289954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC12680 {ECO:0000313|EMBL:GCE76986.1,
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:GCE76986.1}.
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DR   EMBL; BIMR01000159; GCE76986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402DSD9; -.
DR   Proteomes; UP000289954; 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   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR045690; DUF6055.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF19527; DUF6055; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS51173; CBM2; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..742
FT                   /note="CBM2 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019414175"
FT   DOMAIN          643..742
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          583..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..644
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  78316 MW;  3B6B24317B7C3488 CRC64;
     MPHARPVRRA RLRALLLALT LLVVPFAVTL PAGPAQAADK TVWIPERWRT TNEVAWADNR
     KAESENFVVL WGELSGTSPT TAPTAYRFDP ANVLRELESA YSFYVDDMKF TPETGLLAQH
     KIIVIITNTW SSNPNLNAWA TGGSTDGRVG VINLAPGAAQ PGSWGLVHEL AHVLQNYTFL
     GRSGVGFTHA SAGTFWESSA EFMAMQALPG QGAGDLTRFI RTENLPYSSS RHHYGAWMLP
     QAIVDQRGLA FFNRIWNEAR STEHPLETYK RIAGLTQDQL GAEIARYAMR NVTWDYSNAA
     QVKPYIDRLY PFVVPQSFVQ VDAVDATQKH FAVPDGIAPG AYGYTKIKLV PSSSGALVRI
     HLKGHVDPNA GSGWSYGFVG VTNGVARYSP VTQGTDTEAS FQTRAGEQVY LVVSGTPTAV
     PKHGFLDGYP KNYRYPFEFR IDGALPSGHE PGFTRGTAPG GGRWHSNGGG WVDSRATVAS
     TAYVGPNAAV YGRSTVSGTA RIEGLAWVND GGTVSGSAVV RDSALIQGGV SIGGTAVVGG
     DAEPSGTCTS GAYLMFNPDR RCDGGAGETD VNRAHGRFTS AELAITGTTT PTPTPTVTPT
     PTPTVTPTPT PKPTVTPTPT VTPTPTPTPT ATRTPTPTPT PTTPPAGRSC TAAYTVTSTW
     PGGFVATVRV TAGSQAVDGW TVSIDLPSGA AVHHWSSEVL GTAPLTLGPA AWNSRLAAGG
     SVEIGFQGTG SPQATSVSCA AH
//
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