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Database: UniProt
Entry: A0A165Q3V3_9SPHN
LinkDB: A0A165Q3V3_9SPHN
Original site: A0A165Q3V3_9SPHN 
ID   A0A165Q3V3_9SPHN        Unreviewed;       412 AA.
AC   A0A165Q3V3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:KZY54750.1};
GN   ORFNames=A3736_13435 {ECO:0000313|EMBL:KZY54750.1};
OS   Erythrobacter sp. HI0063.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY54750.1, ECO:0000313|Proteomes:UP000077326};
RN   [1] {ECO:0000313|EMBL:KZY54750.1, ECO:0000313|Proteomes:UP000077326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0063 {ECO:0000313|EMBL:KZY54750.1,
RC   ECO:0000313|Proteomes:UP000077326};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-2016) 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:KZY54750.1}.
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DR   EMBL; LWFF01000333; KZY54750.1; -; Genomic_DNA.
DR   RefSeq; WP_067684355.1; NZ_LWFF01000333.1.
DR   AlphaFoldDB; A0A165Q3V3; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000077326; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000077326};
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          130..411
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        349
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         233..239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         254
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   412 AA;  44533 MW;  E8EA01344D360CC9 CRC64;
     MAQPPGIHAR RAALRLLDAV LRRGETLDVA FGAATSDIRK FEDKALARAI ASETLRWAID
     FDALIDSATR QNLPDDAKAR QVLRLMLAQW LRLGTPLHAV IATGLPLLSG GPRRLAHGVF
     STLTKREAKL PKAPTLPDAV AARWGERAQA IAAGLAEPPP LDLTLRDSAQ TEHFKTQLAA
     DSLMPGHLRL PRGAAVETLP GFEDGAWWVQ DLAASLPARL LGAGEGRTAL DLCAAPGGKT
     LQLAAQGWKV TALDISKQRL DLLKANLKRT GLSAGTIRAD ALKWEPKHHY DAILIDAPCT
     ATGTARRHPD VLHRIGPRQI EELTELQTAL LERTQGWLKP GGTLVYTVCS LEREEGEDQA
     ARAALDPVPI TQDELPDGVQ PTGEGWLRTD PGMLSDQGGM DGFFIARWRA PD
//
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