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Database: UniProt
Entry: A0A257KG59_9BRAD
LinkDB: A0A257KG59_9BRAD
Original site: A0A257KG59_9BRAD 
ID   A0A257KG59_9BRAD        Unreviewed;      1701 AA.
AC   A0A257KG59;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=CFE29_28545 {ECO:0000313|EMBL:OYU86393.1};
OS   Bradyrhizobiaceae bacterium PARB1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=2015576 {ECO:0000313|EMBL:OYU86393.1, ECO:0000313|Proteomes:UP000216768};
RN   [1] {ECO:0000313|EMBL:OYU86393.1, ECO:0000313|Proteomes:UP000216768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PARB1 {ECO:0000313|EMBL:OYU86393.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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   -!- 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:OYU86393.1}.
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DR   EMBL; NKIY01000014; OYU86393.1; -; Genomic_DNA.
DR   Proteomes; UP000216768; Unassembled WGS sequence.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR41313; ADENINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR41313:SF1; DNA METHYLASE ADENINE-SPECIFIC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}.
FT   DOMAIN          863..1130
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
FT   REGION          32..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          985..1037
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1629..1656
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1701 AA;  187509 MW;  0DD372FF4F816D12 CRC64;
     MSNDDPFTLD LFGNTALSSG LGLGITAFPS SLEVGGDDDP SPSSPAPARA VTAAGRSPAP
     LKGENFYLGD HRGLATSWRE RARDNLAAIC LASEIEQAQR PATTKEQAAL IKFIGFGASD
     LANGVFRRPG ETDFRKGWEE IGADLEDAVA TGEYASLARC TQYAHFTPEF IVRAIWAGLQ
     RLGWRGGRVL EPGIGTGLFP ALIPEELRTA SHVTGIELDP VTARIVRLLQ PRARIIAGDF
     ARTELPAHFD LAIGNPPFSD RTVRSDRALR SMGLRLHDYF IVKALGLLKP GGLAAFVTSH
     GTMDKADHGA RAHIAGMADL VGAIRLPEGS FRADAGTDVV VDILFFRKRK DGESDGDLSW
     LDLDEVRPAA GDDSALRVNR WFARHPGMVL GTHALTSGPF GETYTCSPRK GENLDAALTT
     AVRLLPEAIY DGEPNAIEIE LENDVASDLE RRPDDRQVRE GSYFIGNRHG LMQLVDGAPV
     AIHVRKGRSA DGIPDKHVRI IRKLIPIRDA VREVLKAQEC DRPWKPAQVK LRIVWSNFVR
     AFGPINFTTV STIEDEETGE VRETHRRPNI QPFLDDPDCW LVASIEDYDL ESNTATPGPI
     FTERVIAPPA PPVITSAADA LAVVLNERGH VDPDHVAELL HRDVEDVIAE LGSAIFRDPG
     DGSWQTSDAY LSGAVRSKLV MAQAAAALDP AYQRNVTALQ AVQPADLRPS DITARLGAPW
     IPAADIVTFV NETMGAEIRI HHMPELASWT VEARQLGYLA AGTSEWGTDR RHAGQLLSDA
     LNSSVPQIFD IVKDGDSERR VLNVVDTEAA KEKLQKIKTA FQNWIWSDPD RTDRLARIYN
     DRFNNIAPRA FDGSHLQLPG ASGAFSLYGH QKRGIWRIIT AGSTYLAHAV GAGKTMTFAA
     AIMEQRRLGL IAKAMLVVPG HCLAQAAREF LALYPNARIL VADETNFTLA KRHRFLSRAA
     TATWDAIIIT HSAFRFIAVP SAFEQQMIQD ELELYEELLT KVESDDRVSR KRLERLKEGL
     KERLESLSTR KDDLLTMSEI GVDQIIVDEA QEFRKLSFAT NMSTLKGVDP NGSQRAWDLY
     VKSRFIETKN PARALILASG TPITNTLGEM FTVQRLLGHA ALRERGLHEF DAWASTFGDA
     STELELQPSG KYKPVTRFAQ FVNVPELIAM FRSFADVVMP AYLREYVKVP EISGGKRQIV
     AAPPTAAFKA YQRLLDARIT AIEQRDGPPQ PGDDILLSVI TDGRHAAIDL RLVDPGNDNE
     VDNKLNLLVA NTFRIWQDTA ANAYVRSDGK PFELTGAAQM IFSDLGTISV EKSRGFSAYR
     WIREELIRMG VPASEIAFMQ DYKKSEAKQR LFSDVRSGKV RVLIGSSDTM GTGVNAQLRL
     KALHHLDVPW LPSQIEQREG RIVRQGNQHD VVDIFAYATL GSLDATMWQN NERKARFIAA
     ALSGDTSIRR LEDMGEGQAN QFAMAKAIAS GDQRLMQKAG LEAEIARLDR LRAAHVDDQH
     AIRRQIRDAE REIELSTRRI GEIGQDIERL VPTAGDAFTM TVMGKAHDER KLAGRALMKE
     ILTLVQLQHE GEVVIVSIGG FDLEFSGERF GKDGFHFTTT LMRTGADYEI GLPVTVTPIG
     AVARVEHALA GFDDEQQNYR RRLAEARKRL SSYQSRIGEE FAFAAEFKMK REQLAEIDAD
     LARDTDAAAD GNAQPADRVA A
//
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