ID D9W1B7_9ACTN Unreviewed; 361 AA.
AC D9W1B7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=SSNG_03221 {ECO:0000313|EMBL:EFL15969.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL15969.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL15969.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL15969.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000256|ARBA:ARBA00001279};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; GG657750; EFL15969.1; -; Genomic_DNA.
DR AlphaFoldDB; D9W1B7; -.
DR STRING; 253839.SSNG_03221; -.
DR eggNOG; COG0338; Bacteria.
DR HOGENOM; CLU_063430_4_0_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF2; MODIFICATION METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 361 AA; 40631 MW; 936B2E410E2D4827 CRC64;
MEPISHALSQ GRYQSPLRYP GAKSSLAPVI SRVITSAKQS REVPEVNLLV EPFAGGASAS
LRSIGEGIVD RILLADADPL VTAFWQAAAA DTEQLIDRMH EEWKRYVRDG GASAVSRWDY
WRAWSPRPAM TSQDRRLSMA TQCLFLNRTT FSGILHGKAG PIGGRAQTSN YPIGCRWNPD
ALAERLRYVG HLYDIGRLVD VWCKDWRQTL DDVPEHYPQL LPSRVVAYLD PPYIEKSSLL
YRTSFDPRGG YGGGSSVETS ADPLHLSLAS YLRTRAQFRW LLSYDNHPML MQSKWLYAQS
RMTPSEVDRE TLGVRQWRIT KRLVATRYSA AGRSGKRSAE ELLITTLPPA TVPLDEQLRL
P
//
