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Database: UniProt
Entry: A0A101KPH7_RHILI
LinkDB: A0A101KPH7_RHILI
Original site: A0A101KPH7_RHILI 
ID   A0A101KPH7_RHILI        Unreviewed;       461 AA.
AC   A0A101KPH7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=MFS transporter {ECO:0000313|EMBL:KUM24374.1};
GN   ORFNames=AU467_30595 {ECO:0000313|EMBL:KUM24374.1};
OS   Rhizobium loti (Mesorhizobium loti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=381 {ECO:0000313|EMBL:KUM24374.1, ECO:0000313|Proteomes:UP000053176};
RN   [1] {ECO:0000313|EMBL:KUM24374.1, ECO:0000313|Proteomes:UP000053176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM24374.1,
RC   ECO:0000313|Proteomes:UP000053176};
RA   Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA   Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT   "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT   efficient symbiont and plant-growth promoting strain isolated from Zn-
RT   mining soil using Leucaena leucocephala as a trap plant.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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:KUM24374.1}.
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DR   EMBL; LPWA01000138; KUM24374.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101KPH7; -.
DR   Proteomes; UP000053176; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          165..460
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          292..319
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        388
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         272..278
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         319
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         335
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   461 AA;  48839 MW;  AFA0419BD8620C84 CRC64;
     MVVSGAKRRP QNPGRRDGNA GEAIAGLAAR KAAARLLAAV IDAHTPLDGL TDNEHGHPQY
     KALDARDRAL VRAILVTALR HCMTIAGLLA KRLERPLPAN ATALSHILHV AAAQILFLDI
     PDSAAVDLAV THAKSDPRTL RFSGLVNGVL RSLARAKEAE LAPALAATNE APQWFSERLI
     AAYGAEKARA ILAAHRHEAP VDFTAKSDPA LWAGRLGGIV LPTGTVRVEK LQAGVTDLTG
     FAEGAWWVQD AAAALPARLF GDIKGLRVAD LCAAPGGKTA QLILAGANVT AVDTSKNRLA
     RLEQNLDRLG LSAELVQTDL LDYQPVELFD AVLLDAPCSS TGTVRRHPDV PWTKTMADVE
     KLAALQRRLL AHAVSLVKPG GRIVFSNCSL DPIEGEDLYR AFLAETSGVD ADPIQPGEFA
     GLDPFLTPEG TLRTTPADMM LGPPGISGLD GFFAARMRRV G
//
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