ID   A0A1E5MMY2_9MICO        Unreviewed;       537 AA.
AC   A0A1E5MMY2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Ribonuclease BN {ECO:0000313|EMBL:OEI69943.1};
GN   ORFNames=Cus16_0561 {ECO:0000313|EMBL:OEI69943.1};
OS   Curtobacterium sp. ER1/6.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1891920 {ECO:0000313|EMBL:OEI69943.1, ECO:0000313|Proteomes:UP000095245};
RN   [1] {ECO:0000313|EMBL:OEI69943.1, ECO:0000313|Proteomes:UP000095245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER1/6 {ECO:0000313|EMBL:OEI69943.1,
RC   ECO:0000313|Proteomes:UP000095245};
RA   Garrido L.M., Alves J.M., Oliveira L.S., Gruber A., Padilla G.,
RA   Araujo W.L.;
RT   "Draft genome sequence of Curtobacterium sp. strain ER1/6, an endophytic
RT   strain isolated from Citrus sinensis with potential to be used as a
RT   biocontrol agent.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:OEI69943.1}.
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DR   EMBL; MJAK01000001; OEI69943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5MMY2; -.
DR   STRING; 1891920.Cus16_0561; -.
DR   PATRIC; fig|1891920.3.peg.582; -.
DR   Proteomes; UP000095245; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000095245}.
FT   DOMAIN          94..312
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          400..515
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   537 AA;  57448 MW;  A7E55CD1BD22DE34 CRC64;
     MGTRGSSTMR LDAQRRYQDD EVVDVVVVGT GAGGAPLLAR LAREGLTAVA FEAGRNTEPG
     DHTPDEVEAP ADINWMDERI SGGATPTAFG PNNSGTGVGG STLHWGAFTP RPSVHDLRLR
     TESGQGEDWP IDHAELTGYI ERVEHEVGVA GPEHYPWDPS RRYRMGPPPR NASSDMMMRG
     TAALGITATD APVGLTTEDR HQEHHGLRQA CVSCGSCHQG CRNGAKVSMD TTYLPAAVAF
     GAEIRPESFV HGIELDADGK VCAVLYTRDG RERRQRCRSL VLAAGGVETP RLLLHTGLAN
     SSGQVGRNFT AHGATQVWAT FDESMRSYRG YPSSIITEDF VRPADADFAG GYLIQSLGVQ
     PLTFATSLVR GGSLRGAELV RAMRDYPRMA GVGINAECLP YDDNRLVLSD ELDEHGVPRA
     RVTFSPGSNE EAIRAHAVRT MTAIVEAAGG TDVRVLERTA HTIGTARMGV DAGSSVVDPA
     GRSWDVPNLW VCDNSVFPSA VIANPALTIM ALSLRTADRF LRDDPAADRA RSVAVAA
//