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Database: UniProt
Entry: D0LVD7_HALO1
LinkDB: D0LVD7_HALO1
Original site: D0LVD7_HALO1 
ID   D0LVD7_HALO1            Unreviewed;       860 AA.
AC   D0LVD7;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=Hoch_5009 {ECO:0000313|EMBL:ACY17498.1};
OS   Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC   Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX   NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17498.1, ECO:0000313|Proteomes:UP000001880};
RN   [1] {ECO:0000313|EMBL:ACY17498.1, ECO:0000313|Proteomes:UP000001880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC   {ECO:0000313|Proteomes:UP000001880};
RX   PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA   Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA   Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA   Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL   Stand. Genomic Sci. 2:96-106(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; CP001804; ACY17498.1; -; Genomic_DNA.
DR   RefSeq; WP_012830090.1; NC_013440.1.
DR   AlphaFoldDB; D0LVD7; -.
DR   STRING; 502025.Hoch_5009; -.
DR   REBASE; 22285; M.HocORF5009P.
DR   KEGG; hoh:Hoch_5009; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_013049_4_0_7; -.
DR   Proteomes; UP000001880; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 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   ECO:0000313|EMBL:ACY17498.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACY17498.1}.
FT   DOMAIN          27..165
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          178..487
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          598..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..626
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  94219 MW;  4D6940C757B1A519 CRC64;
     MTDTTRRHTD EHRDALEAQQ PLTLGQLERH LYAAADILRG KMDASEFKEY IFGMLFIKRC
     SDEFEARREE ILAEQQAAGA SAEAAALAAE QPERYARSFF VPPSARWAQV SALERDLGTG
     LNAALAALED TNPALHGVLR HIDFNRTVGK SRMPDKRLRA LVAHFGRHRL RNRDFEFSDM
     LGAAYEYLIG EFADSAGKKG GEFYTPRPVV RLIVRLSDPR PGMRVYDPCS GSGGMLILAR
     QYVQEHGGDA GSLGLYGQED NGGVWTISQM NMLLHGVSDA DIRNGDTLHE PLHIDPASGE
     LLRFDRIITN PPFAQNYSPD ELPLPERFRF GMCPHAGKKA DWMYAQHMLA ALAPGGMAVT
     VMPHGVLFRG GVEQAIRSRV LEADLVEAVI GLPPNLFYGT SIPACVLVLR APEAKPPERQ
     GRVLFVDASD EFHAARAQNH LQPEHVEKIA TAFERFAEVP GYASVVSVDE ILAAGGNLNI
     RSYVSRAAAP TGYDVRGLIE GGVPRAEVEA ERARFAAVGL DLGSVLRLQG GGLSYWFADG
     ISQRRDLRAA VDGDLRVRSA HVDMLARTDA WWAAHRWVLE SLADARAGAV ADSDAGAVAD
     PDAGVERGRG GQRKGGARKR GRGDQAGACR GGEVAFLRVR RCFVDSFRDA LSPAGVLAPQ
     DLAGIAAGFW GSLELELKIL MTRGFAGLLY SWIKVLVRDD KPSARGQAEL GHIEVAAPSL
     DIVGRLLTEA GQADHELRAL EEGAAHSAEE LDGDAQAQLV GELTHLRKRR TRTRAQVLAC
     LRAAQGRMRE DECRELVIGL LQDQLIWKLE EALRGLRADL TAQLERWWDA YHVPLRALER
     ERDRAASELE TALRGLGYVG
//
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