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Database: UniProt
Entry: A0A1M3EIN2_9CELL
LinkDB: A0A1M3EIN2_9CELL
Original site: A0A1M3EIN2_9CELL 
ID   A0A1M3EIN2_9CELL        Unreviewed;       329 AA.
AC   A0A1M3EIN2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN   ORFNames=BGO38_08480 {ECO:0000313|EMBL:OJV58350.1};
OS   Cellulomonas sp. 73-145.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV58350.1, ECO:0000313|Proteomes:UP000184491};
RN   [1] {ECO:0000313|EMBL:OJV58350.1, ECO:0000313|Proteomes:UP000184491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-145 {ECO:0000313|EMBL:OJV58350.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV58350.1}.
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DR   EMBL; MKTI01000009; OJV58350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3EIN2; -.
DR   STRING; 1895739.BGO38_08480; -.
DR   Proteomes; UP000184491; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10917; CE4_NodB_like_6s_7s; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
FT   DOMAIN          134..322
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..116
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  33174 MW;  F77BD7DE7543C518 CRC64;
     MGVGTVVLSS GVVGAGPGRR RGSALPLVGL LLTVLLAAGC TTSTTPPQAP TSTPVPTASS
     TPTPSTGPGT PTATASPPAT SPTPVPPPPS PSPAPPVPPP QPPAPPTVPP PAPPTGVPAA
     WRGVDVSRVA TDRAVVALTF DAGSSNAGVA SVLATLARYD VPATFFVTGQ FARRYPADVR
     AISAAGHPVG NHSDSHPDFT QTTTAEIQRQ LAAAEASISA ATGHAAKPLF RFPYGARTAE
     DIHVVNDAGY VPFRWTVDTL GWKGTSGGQS VESVRARVLG AAQPGEIVLM HVGANPDDGS
     TLDAAALGSV IEGLRERGYS FITLRSLLP
//
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