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Database: UniProt
Entry: A0A0C2JG91_9ACTN
LinkDB: A0A0C2JG91_9ACTN
Original site: A0A0C2JG91_9ACTN 
ID   A0A0C2JG91_9ACTN        Unreviewed;       222 AA.
AC   A0A0C2JG91;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=CBM2 domain-containing protein {ECO:0000259|PROSITE:PS51173};
GN   ORFNames=LP52_16505 {ECO:0000313|EMBL:KIH97925.1};
OS   Streptomonospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH97925.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT   unusual lasso Peptide from an understudied halophilic actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
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:KIH97925.1}.
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DR   EMBL; JROO01000031; KIH97925.1; -; Genomic_DNA.
DR   RefSeq; WP_040274723.1; NZ_JROO01000031.1.
DR   AlphaFoldDB; A0A0C2JG91; -.
DR   STRING; 183763.LP52_16505; -.
DR   OrthoDB; 3425593at2; -.
DR   Proteomes; UP000031675; 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   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   Pfam; PF00553; CBM_2; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51173; CBM2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031675};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          106..214
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   222 AA;  23202 MW;  46E656FDFAAE598D CRC64;
     MRAGRDDPLE RPQRGLHRSE PVDKSRLAAV GYFLGSTVPK RVQPPRVLNV LLISGVTLAL
     TLFGYSTTQI YLRFSEPPTA QEAGPTAPDT SERLAPSSGP ATEESGKASA EMVSVVSYEA
     VASSGSGFTG EVTVTNTGSA LLKDWELALE FADARVTSVA DAEWRATENG VVASEPARAD
     GLEPGDSVTL SFTAEGRTQN PVACSLNGSP CDWGAADSAA QD
//
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