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Database: UniProt
Entry: A0A0M8XST1_9ACTN
LinkDB: A0A0M8XST1_9ACTN
Original site: A0A0M8XST1_9ACTN 
ID   A0A0M8XST1_9ACTN        Unreviewed;       353 AA.
AC   A0A0M8XST1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=CBM2 domain-containing protein {ECO:0000259|PROSITE:PS51173};
GN   ORFNames=ADK66_05365 {ECO:0000313|EMBL:KOX12342.1};
OS   Micromonospora sp. NRRL B-16802.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX12342.1, ECO:0000313|Proteomes:UP000037709};
RN   [1] {ECO:0000313|EMBL:KOX12342.1, ECO:0000313|Proteomes:UP000037709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX12342.1,
RC   ECO:0000313|Proteomes:UP000037709};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AHA1 family.
CC       {ECO:0000256|ARBA:ARBA00006817}.
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:KOX12342.1}.
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DR   EMBL; LGEB01000024; KOX12342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8XST1; -.
DR   STRING; 1415541.ADK66_05365; -.
DR   PATRIC; fig|1415541.3.peg.1133; -.
DR   Proteomes; UP000037709; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.530.20; -; 1.
DR   InterPro; IPR013538; ASHA1-like_C.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   Pfam; PF08327; AHSA1; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51173; CBM2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        162..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          246..353
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          185..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  37476 MW;  7E16C7BCD176EB3B CRC64;
     MSHPPDRVWL ALTDRELIGR WFAEADMVEG VPDRLLLHTA GLPGFDANVE VEVIERQVPE
     LLELRCDEAG RLTELTCVVT PTTQGCRLSV REVPTHGSWS AEQHGPREQQ LRQALTVRLP
     AILDWLAFQQ VDLRRGEAGM TAELPLIGGV GAARARRRRR TVVTALVGVV LVAGLVAWMT
     LPGGSKQAAA PVSSSPTATS EPTAATATST APPKATSSAR PSRTAASPTT SPSRTPTAKP
     SRTPTAAPPP PPLTARYDTD SSRLFGYTGK VVVNNPGRAP ADQWSVVVTL AEGSSVDEVE
     GAEWRQDDRA ITFSGPAVPA GGSRTIRFDV RDGRPKAREP VGCTVDGNPC AGL
//
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