ID A0A1U7NTW7_9DEIO Unreviewed; 1706 AA.
AC A0A1U7NTW7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BOO71_0012016 {ECO:0000313|EMBL:OLV16369.1};
OS Deinococcus marmoris.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=249408 {ECO:0000313|EMBL:OLV16369.1, ECO:0000313|Proteomes:UP000186607};
RN [1] {ECO:0000313|EMBL:OLV16369.1, ECO:0000313|Proteomes:UP000186607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOPRI26562 {ECO:0000313|EMBL:OLV16369.1,
RC ECO:0000313|Proteomes:UP000186607};
RA Kim J.H., Oh H.-M.;
RT "Genome Analysis of Deinococcus marmoris KOPRI26562.";
RL Submitted (JAN-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:OLV16369.1}.
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DR EMBL; MSTI01000144; OLV16369.1; -; Genomic_DNA.
DR STRING; 249408.BOO71_0012016; -.
DR Proteomes; UP000186607; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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 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 InterPro; IPR000330; SNF2_N.
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 Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:OLV16369.1};
KW Transferase {ECO:0000313|EMBL:OLV16369.1}.
FT DOMAIN 817..1088
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1226..1384
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1706 AA; 183874 MW; 75AD593E40FCC120 CRC64;
MTAMTQTSKA KSTVPSLFAA LEEPGQQEPS AVPALPEEQT ELAAFTMLST PSRAPDTSGL
PLGTEALVKA SDAERVRANG LAREVAMSEG TMTPQATAAL RAWSGEGNLG GSTSAFYTPG
ALAGFMWNVL EGLKAGSRAL EFACGGGVFF EHAPQGTLLS GVEIDETTAR VARTLYPHAH
VHHAPFETYH TQSGDAPFDV VIGNPPFGVR GASAYRDRPE IEAAHWYFVL AGLERLQGGG
LMAVIVPESM LRNPSEQMLR ERLLDSAHLL CASAIPESAF RATGAGVSTA LLILRRHDAG
VGEAMKKLSE DERATLREAR MTDDGLLRHF VTGTALFYKR NETWQTTYGF PRLGESKEET
LRAGRFGDPV YGGPLHLDAD KLETVTAFCR DRQHGVLTRT GLLSAVYTLL GSDASARAAQ
GVPQAHPIQN GQVSSCGRYR FARGGWQYAD ALNTPSTLSA LNVARAVVAA RAAVNRGGAQ
ARRDEALQAH TAHLAQHGAY DIPALKKAAR TLNVLGVLTG EGDVGALLAE LPAQPLTFQG
QGMEAVAQEL EAYGMLSAAN LSQHAGVTQN AAYAHLRAAY AYTGRLWEAR STYLRGNAHS
RALHAEELSA SASGQEREAL ISQACELRAL APWTDLSDMT LEARDPLIPE SILSEWVNAA
LGSYTTLKRN AWDKDGERVG LLHAAREGGA VTLRIRNTLS GADNLEDRRQ IEPGRVRALE
AYLNFATPVG TVVNQNLKSP EQIAAERAAH VQAAGRWEKE LAAQFRSFVL GGPYAAEIER
LLNEGRYGLI PAQPDHRPLL LAGYSGPLAH PFQAAHVRTA ARMDGAILNF DVGLGKTLTG
LMLAALLLQS GRARTVAIVV PLSRLADWVM NARTALEKLN VVVIGGAVAC NENGSFTLDE
NGEPVVRSES AGARSAKLAR LLTHPPDVVI LTLDAFEAVP MLEETRLRMI HSDPTLMAGA
DQGTTFDERS RKMSGHRKLS AVEKTVGRHL ARVRVSTHTD LPWEVLGIGA IITDEVHALK
NSYSAPTVYG ESNPKFLGSG GESNRAIDAV HKYRFVRAFG GATVGLSATW FTNSPIEIFN
QLALHTDALA AYGLSTVAAF TARFCVIESR LITLPDGEVE FKPCVVGFRN LPELRAIMAQ
HVIRETEDTC LMHTGVGMPL PPLETVEHLF DLPAEVMERY EEERGSLAEV ESEGKMHLFS
IFARMMKLTL HPPLLGVGAP SVRFAECVSA CLKAREAGGR NVVFLSMGGK GGEAYSALRD
MLIAGGYPAG EIETITASSH PAAGQRLGVE RRLQRGELSC VIGSAVIEQG ANFQGATDLH
HLDYPHHSKA FDQRIGRARR QGTRVLKIRN HLYFGRDSFD MLRYQNMLGK KGWAEQVYDP
SVLSCENSDA GFDGEELAVM LSRDPQAMRA QILKKKEERH QQTRAATLLD DAAMIREYLD
TIRLLRSRHA AAQGREKGPS VHDKAGITRL VTALRTLHAG VVRLRAAGHP LSAVTRLKAA
PVWAAGLPMH PGLEFTTGGV SYRVKLAESA SPSVAVEELP GHALKLLAIS EIEPEQVTPT
RDEDAYGDEA LTALPRKLRE QIEAEAQPVA EVVAQPAAVA QPAGQAAPVS SEPMPITPPP
ARPYGLSVAH AARPHQALFS VVDDHLEAGA LSGAAVFALE YRADQSVRVV TLIVPDPQRS
QRTRQLLLAR DTRLRVRVDA LLATAV
//
