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Database: UniProt
Entry: M7N5E5_9MICC
LinkDB: M7N5E5_9MICC
Original site: M7N5E5_9MICC 
ID   M7N5E5_9MICC            Unreviewed;       517 AA.
AC   M7N5E5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Sun protein {ECO:0000313|EMBL:EMQ96989.1};
GN   ORFNames=ADIAG_03507 {ECO:0000313|EMBL:EMQ96989.1};
OS   Paeniglutamicibacter gangotriensis Lz1y.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paeniglutamicibacter.
OX   NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ96989.1, ECO:0000313|Proteomes:UP000012015};
RN   [1] {ECO:0000313|EMBL:EMQ96989.1, ECO:0000313|Proteomes:UP000012015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lz1y {ECO:0000313|EMBL:EMQ96989.1,
RC   ECO:0000313|Proteomes:UP000012015};
RX   PubMed=23766407;
RA   Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT   from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT   Station Dakshin Gangotri.";
RL   Genome Announc. 1:e00347-e00313(2013).
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:EMQ96989.1}.
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DR   EMBL; AOCK01000012; EMQ96989.1; -; Genomic_DNA.
DR   RefSeq; WP_007272664.1; NZ_AOCK01000012.1.
DR   AlphaFoldDB; M7N5E5; -.
DR   STRING; 1276920.ADIAG_03507; -.
DR   PATRIC; fig|1276920.7.peg.3509; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   Proteomes; UP000012015; 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   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:UP000012015};
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          215..516
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        445
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         321..327
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         346
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         373
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         392
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   517 AA;  55223 MW;  82ABCC6CEFA74320 CRC64;
     MSEFGQGRSD RPRRSEPNRG GGQERRDDAG RTRNRGGAGP RQFSSSAPSA RNRRADQARL
     TAFEVLRAVA ENDAYANLVL PARIREHHLD RRDAGFATEL TYGALRGQGL YDAILARCVD
     RPLDQLDPAV LDALRLGAHQ LLAMRVPNHA ALDEMVSLAR MVIGAGASGL INAVLRKVSL
     KDLETWSEEL VAGITDENAA AALVHSHPEW IVRALRQALV AHGRDASEIT ELLIADNVAP
     VVNLVALPGI GSLDEALDQG AEPGTLVADS AYYQGGDIAR LASVREGSTR VQDAGSQLVA
     RALAQVPLPD GGEDTYWLDL CAGPGGKAAL LAALADQHGA KLTANEPTQH RAELVSKALM
     AVDPETWMIS VRDGREYGES EYSGGYDRVM VDAPCSGLGA LRRRPESRWR KTPRDVAELT
     ILQGELLDAA LSAVRVGGVV AYMTCSPHPA ETVAVVDDLL ARNKNVRLMD TGAALEAAAL
     PGLASAARPL GEGSTIQLWP HIHSTDAMFM ALFTRTA
//
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