GenomeNet

Database: UniProt
Entry: R9GUT3_9SPHI
LinkDB: R9GUT3_9SPHI
Original site: R9GUT3_9SPHI 
ID   R9GUT3_9SPHI            Unreviewed;       474 AA.
AC   R9GUT3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:EOR95453.1};
GN   ORFNames=ADIARSV_1369 {ECO:0000313|EMBL:EOR95453.1};
OS   Arcticibacter svalbardensis MN12-7.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR95453.1, ECO:0000313|Proteomes:UP000014174};
RN   [1] {ECO:0000313|EMBL:EOR95453.1, ECO:0000313|Proteomes:UP000014174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN12-7 {ECO:0000313|EMBL:EOR95453.1,
RC   ECO:0000313|Proteomes:UP000014174};
RX   PubMed=23846277;
RA   Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA   Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT   Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT   Sample.";
RL   Genome Announc. 1:E00484-13(2013).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
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:EOR95453.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AQPN01000050; EOR95453.1; -; Genomic_DNA.
DR   RefSeq; WP_016194610.1; NZ_AQPN01000050.1.
DR   AlphaFoldDB; R9GUT3; -.
DR   STRING; 1150600.ADIARSV_1369; -.
DR   PATRIC; fig|1150600.3.peg.1346; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000014174; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000014174};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   DOMAIN          5..63
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        425
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         398
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   474 AA;  54036 MW;  A800FC548F780241 CRC64;
     MKKIPADKKQ VQNVLITDIA EEGKGLGKSE ELVIFVEKAI PGDVVDIEIY RKKKNFAEAK
     IIQIVTPSEY RTDSFCQHFG VCGGCKWQHM TYEAQLKFKQ KSVNDALERI AKIDTSSTET
     ILPSFETRYY RNKLEFTFSH KRWLTDVDVQ DEHQDMNALG FHVPLRFDKI LNIETCYLQG
     TPSNEIRNSV RAFAVENGIS FYDIRNNEGA LRNLIIRTST TGEVMVIVVF AYVEETQIQL
     MMEHIKGQFG DLTSLLYIVN QKKNDTIFDQ EIHVFSGRDY ILEDMEGLSF KIGPKSFYQT
     NSLQAYELYS LTREFAGFKG DELVYDLYTG AGTIANFIAR SVKHVIGIEY VPTAIEDAKE
     NSLLNGISNT TFFAGDMKDV LTPHFANEHG KPDVIITDPP RAGMHADVVQ RLLEMEAPKI
     VYVSCNAATQ ARDIFLLKEK YDTVRIRPVD MFPHTQHVEN VVLLTLRPVV HTEN
//
DBGET integrated database retrieval system