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Database: UniProt
Entry: D7AYX8_NOCDD
LinkDB: D7AYX8_NOCDD
Original site: D7AYX8_NOCDD 
ID   D7AYX8_NOCDD            Unreviewed;      1363 AA.
AC   D7AYX8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=Ndas_2727 {ECO:0000313|EMBL:ADH68140.1};
OS   Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS   7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS   (Actinomadura dassonvillei).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH68140.1, ECO:0000313|Proteomes:UP000002219};
RN   [1] {ECO:0000313|EMBL:ADH68140.1, ECO:0000313|Proteomes:UP000002219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC   NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC   {ECO:0000313|Proteomes:UP000002219};
RX   PubMed=21304737; DOI=10.4056/sigs.1363462;
RA   Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA   Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT   509).";
RL   Stand. Genomic Sci. 3:325-336(2010).
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};
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DR   EMBL; CP002040; ADH68140.1; -; Genomic_DNA.
DR   RefSeq; WP_013153747.1; NC_014210.1.
DR   STRING; 446468.Ndas_2727; -.
DR   REBASE; 26264; NdaDORF2727P.
DR   KEGG; nda:Ndas_2727; -.
DR   eggNOG; COG1002; Bacteria.
DR   HOGENOM; CLU_004385_0_0_11; -.
DR   OrthoDB; 4280289at2; -.
DR   Proteomes; UP000002219; Chromosome 1.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0043412; P:macromolecule modification; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR046816; MmeI_Mtase.
DR   InterPro; IPR046820; MmeI_TRD.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF20473; MmeI_Mtase; 1.
DR   Pfam; PF20466; MmeI_TRD; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          886..984
FT                   /note="MmeI-like DNA-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20473"
FT   DOMAIN          1032..1228
FT                   /note="MmeI-like target recognition"
FT                   /evidence="ECO:0000259|Pfam:PF20466"
FT   REGION          1342..1363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1342..1357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1363 AA;  151811 MW;  9CC15EF2C99B0456 CRC64;
     MSNPRSRGKH SPADAVRQQH LDWLGLVEVS GPFLTLPVLR EVWSAGLDSL EPEQMRELRR
     TSALWRDQTG PGGGDREAGR DAWVRYVLGD LLDWRETLRT DGLEPLAMEV AEHDTAVAPS
     FVLTHPDAEP EGEVKADDVR LLGLTCPVDQ SPVQRVKDDS WSATPADRLA QLCRHHGVEL
     GLATNGRWWV LVWAPRGGVT TTALFDASLW TDAAERDVLR AFYSLLNRRR FFTVPDEQQL
     VPLLNRSLGS QEDVTEALGV QVRQAVELLV AAIGRADTRA RERGERDLSA VSAHDVYRGA
     VSVMMRTVFL LFAEERGLLP SDNDLYAGSY SAGGLYEELE ALAREGTEDD LERTTAAWHR
     LLALFHAVYH GVDHPKLRMH ALDGSLFNPE TFPWLPLDID DRTVLHMLKA VQYVKVGRGK
     SAELRKLSFR ALDVEQIGYV YEGLLAFDGF RAEDLVVGLV GKEGLEAEVQ LRDLEALAAR
     HTDVEELAEE LAAEYKDSGI GSARKLAKAL APLSKEERTE AVKQLRGVVP GDEPLVERLL
     PFFRILRNDL RGLPMVVRGG ELYVTESALR KNTGTHYTPR ELAEKVVFNA LEPLVYAPGP
     LQTADTSKWK LKNSHEILAL KVADIAMGSA AFLVAAARYL GDRLIEAWAK EKDPHAEGYT
     PQENDVRSDD DKVVIEARRQ VIEHCLYGVD INPMAVEMAK LSLWLVSMDP KRPFTFLDDR
     LASGDSLLGI TSLEQLEYMH MDPKQGRKIH ERGLVDFTRG VRVLIGRAAE SRRKLSKMDG
     ATMDGVNRKR SVLGETELET GQARLLADLV VGAALSSVGK SEAIARDQAL KAADLARRLN
     TAEPEARITA KKWLDTDRPN GAFERKPLHW PLAFPEVFEN GGFDAVIGNP PFLGGPKIRP
     TLGGQYRELI TEVIAKGTRA TNTDLVAYFA LQAHRVVNKE GQAGIIATNT LTQGATRRVG
     LDQIIESGVL IRGAIKSESW PSRSAALEYC VAWTTKKSLE KDSIVLADGV ATATITATLD
     ASTSKKKPAH KLAKNAKVSF LGHHVNGKGF ILTPQEASYL LSTEDNNSEV VFPYLIGQDI
     ADSPTSSPSR WIINFHDWSE EKSKKYKDPF QKVDSLVKPE RLKRNRESHR KYWWRYADYR
     RGLESSISSL DRIIAFARVS KTTAPVMVPT GQVFSEQIVV LASDDTAMLA LLSSTSHYWW
     AITRASTLET RIRYTPSDVF ETFAMPELTQ ELRDLGDRLD TYRRDVMLSR NTGLTKTYNL
     VFDPACNDSD IVELRAIHRA IDEATIRAYG WEDRIEAVSG LDHGFHKVGR ETRYTIGPAA
     QREVLDSLLE LNHERYAEEV AQGLHDKKGK RKSAAQEGTL FDV
//
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