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Database: UniProt
Entry: A0A077HQM8_9CORY
LinkDB: A0A077HQM8_9CORY
Original site: A0A077HQM8_9CORY 
ID   A0A077HQM8_9CORY        Unreviewed;       497 AA.
AC   A0A077HQM8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=MFS transporter {ECO:0000313|EMBL:AIL96992.1};
GN   ORFNames=CUREI_06500 {ECO:0000313|EMBL:AIL96992.1};
OS   Corynebacterium ureicelerivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL96992.1, ECO:0000313|Proteomes:UP000028939};
RN   [1] {ECO:0000313|EMBL:AIL96992.1, ECO:0000313|Proteomes:UP000028939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL96992.1,
RC   ECO:0000313|Proteomes:UP000028939};
RA   Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.;
RT   "Complete genome sequence of Corynebacterium ureicelerivorans DSM 45051, a
RT   lipophilic and urea-splitting isolate from a blood culture of a septicaemia
RT   patient.";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009215; AIL96992.1; -; Genomic_DNA.
DR   RefSeq; WP_038611740.1; NZ_CP009215.1.
DR   AlphaFoldDB; A0A077HQM8; -.
DR   STRING; 401472.CUREI_06500; -.
DR   KEGG; cuv:CUREI_06500; -.
DR   HOGENOM; CLU_005316_0_3_11; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000028939; Chromosome.
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:UP000028939};
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          212..493
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        432
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         314..320
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         363
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         379
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   497 AA;  52928 MW;  D22A10330DA3CF76 CRC64;
     MSGGFRSRSA GRRDDKPEGN KGQKQGRAQA RHQTRGQGGG RQRYTVKGRP ASIGDPAREA
     AFEVVLRVAR DGAFANLTLP GILRERAIAG RDAAFATELA YGTLRSLGVL DAVIAKNSSR
     ELNRIAPEVL AALRLGTYQL LNTRVGDHAA VDTSVRLVEA AGHDKAKGFA NGVLRSVGRT
     PAEEWLRTLA PKSEMGALAF THAHPEWIAR AFAEALGDKR GELEAALEAD SARPVVHLVA
     RPGEISAEEL ALSTGGEQGK YSPYAVYLPE GDPGQLDPVR DGLAAVQDEG SQVIARAVTE
     VPVGDDHGRW LDLCAGPGGK VALMGAIAAI DGATVDAVEV SPHRAELIAK TVRGLPVTVH
     TADGRDTGLE PGYDRVLVDA PCSGLGALRR RPEARWTKAE SDIAELNQLQ EELLESAVEL
     AKPGGVIVYS TCSPDVRETR RIVEKQLAKG CVEELDAREW AAGMEDVGDG PSVQMWPHRH
     GTDAMFYAVL RKTGTLG
//
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