(data stored in ACNUC7421 zone)

SWISSPROT: A4ATP2_MARSH

ID   A4ATP2_MARSH            Unreviewed;       348 AA.
AC   A4ATP2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {ECO:0000256|HAMAP-Rule:MF_01849};
DE            EC=2.1.1.192 {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=tRNA m2A37 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
GN   Name=rlmN {ECO:0000256|HAMAP-Rule:MF_01849};
GN   OrderedLocusNames=FB2170_17046 {ECO:0000313|EMBL:EAR00812.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00812.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00812.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
CC       23S rRNA and position 2 of adenine 37 in tRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00721833}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-
CC         [ferredoxin] + 2 S-adenosyl-L-methionine = 2-
CC         methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-
CC         methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42916, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152, Rhea:RHEA-
CC         COMP:10282, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74497;
CC         EC=2.1.1.192; Evidence={ECO:0000256|HAMAP-Rule:MF_01849,
CC         ECO:0000256|SAAS:SAAS01114928};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] +
CC         2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-
CC         deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43332, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10162,
CC         Rhea:RHEA-COMP:10485, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74497;
CC         EC=2.1.1.192; Evidence={ECO:0000256|HAMAP-Rule:MF_01849,
CC         ECO:0000256|SAAS:SAAS01114934};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01849};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01849};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
CC       ECO:0000256|SAAS:SAAS00297762}.
CC   -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism
CC       involving intermediate methylation of a conserved cysteine
CC       residue. {ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
CC       {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00571858}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01849}.
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DR   EMBL; CP002157; EAR00812.1; -; Genomic_DNA.
DR   RefSeq; WP_013304615.1; NC_014472.1.
DR   STRING; 313603.FB2170_17046; -.
DR   EnsemblBacteria; EAR00812; EAR00812; FB2170_17046.
DR   KEGG; fbc:FB2170_17046; -.
DR   eggNOG; ENOG4105C55; Bacteria.
DR   eggNOG; COG0820; LUCA.
DR   HOGENOM; HOG000217991; -.
DR   KO; K06941; -.
DR   OMA; CGQLANK; -.
DR   OrthoDB; 1111428at2; -.
DR   BioCyc; MSP313603:G1GNS-186-MONOMER; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01849; RNA_methyltr_RlmN; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040072; Methyltransferase_A.
DR   InterPro; IPR027492; RNA_MTrfase_RlmN.
DR   InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30544; PTHR30544; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF006004; CHP00048; 1.
DR   SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATP2.
DR   SWISS-2DPAGE; A4ATP2.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297782};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297764};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00721829};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00297790};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297787};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297793};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297761};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00536180};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297766};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297763};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00721837}.
FT   DOMAIN      111    277       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   REGION      167    168       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   REGION      222    224       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   ACT_SITE     96     96       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01849}.
FT   ACT_SITE    341    341       S-methylcysteine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       116    116       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       120    120       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       123    123       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     199    199       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     298    298       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
SQ   SEQUENCE   348 AA;  39584 MW;  A935A9682C1808D2 CRC64;
     MKEVIKKKDI RALTLDQLRE FFVANGDKAF RGNQVYEWLW KKSAYSFEVM TNISKETRTL
     LTSNFVINHI KVDQMQRSKD GTIKNAVRLH DDLVVESVLI PTKTRTTACV SSQVGCSLDC
     KFCATARLKR MRNLNPDEIF DQVVAIDNES RLYFNRPLSN IVFMGMGEPL MNYNNVLKAI
     DKITSPDGLG MSPKRITVST SGVPKMIRKM ADEQVKFKLA VSLHSAIDEI RTSIMPFNAT
     LTLADLREAL QYWYSKTKSR ITYEYVVWKG INDTLNDAEA LVDFCRFAPS KVNLIEYNPI
     DDGDFQQANN KAIDMYVDTL ERRGITVTVR RSRGKDIDAA CGQLANKS
//

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