ID D1AVX7_STRM9 Unreviewed; 1359 AA.
AC D1AVX7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=Smon_1454 {ECO:0000313|EMBL:ACZ01887.1};
OS Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS 9901).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Streptobacillus.
OX NCBI_TaxID=519441 {ECO:0000313|EMBL:ACZ01887.1, ECO:0000313|Proteomes:UP000002072};
RN [1] {ECO:0000313|EMBL:ACZ01887.1, ECO:0000313|Proteomes:UP000002072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901
RC {ECO:0000313|Proteomes:UP000002072};
RX PubMed=21304670; DOI=10.4056/sigs.48727;
RA Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA Del Rio T.G., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C.,
RA Ovchinikova G., Pati A., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Streptobacillus moniliformis type strain
RT (9901T).";
RL Stand. Genomic Sci. 1:300-307(2009).
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; CP001779; ACZ01887.1; -; Genomic_DNA.
DR RefSeq; WP_012859433.1; NC_013515.1.
DR STRING; 519441.Smon_1454; -.
DR REBASE; 22746; SmoLII.
DR GeneID; 29673103; -.
DR KEGG; smf:Smon_1454; -.
DR eggNOG; COG0286; Bacteria.
DR eggNOG; COG1061; Bacteria.
DR HOGENOM; CLU_005929_0_0_0; -.
DR OrthoDB; 9813673at2; -.
DR Proteomes; UP000002072; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; 1.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF04851; ResIII; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:ACZ01887.1};
KW Hydrolase {ECO:0000313|EMBL:ACZ01887.1};
KW Nuclease {ECO:0000313|EMBL:ACZ01887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002072}.
FT DOMAIN 157..350
FT /note="Helicase/UvrB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04851"
FT DOMAIN 1011..1110
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT REGION 716..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1359 AA; 158485 MW; B5C39DAA039E4AC2 CRC64;
MKETKIEAID ILDRIIVGRV EPHIYAFTTN TIPNYLKIGD TYRSVTQRLN EWKNFFPDLE
KQYECKAVID NEIYFRDYSV HQFLENDLEK IRLLRSDLDD DIYYSKEFFK DTYPLDIEKA
IEDIKDNYIQ NTDKYEYYSS NNKLLKTFHY QRGANWNLRP NQLEVVNNFK KAIQNGRKNL
LMYAVMRFGK SFTSLCCALE MDANLVLIVS AKADVKDEWK KTLESAGNFY QYVFLDVNDL
ISNEKIIKDK IIENKKVVLF LTLQDLQGEN IKDKHRQLFE EKIDLLIVDE THFGARAESF
GKILKDEGYD RSDDKNFKKL SDYSMDIEEA NKKIKKINAT IRLHLSGTPY RILMGSEFEK
EDIISFVQFS DIVKEQEKWD KNNLNNDDVN EWDNPYYGFP QMIRFAFNPN KSSRQKMEAL
RKKGVSFVFS KLFEPISIKK DSKNNAHKKF QNESEIIDLL KVIDGSQDDE NLLGFLDYGK
MCKHMVMVLP YCASCDAMEE LIIKNKDFFK NLNEYKILNI SGVDSNKIYK TPNDIKNKIK
EFELENKKTL TLTVNRMLTG STVEQWDTMI YFKDTSSPQE YDQSIFRLQN QYIKTLSSEK
GIIKENLKPQ TLLVDFDPNR LFRMQEQKSL IYNVNIEENG NSKLKDRITE ELRISPIIVM
NNNKISQVEA TNILETVSLY NNQRSVSDEV SDIPVDLSIL EDDYVRKAIE EQGEFNSKQG
LTINPNQGDG NDIDIDDYSD STYEKENRKD KENQSYREEK TDEEIKRLER QIKTYYQRLL
FFSFLTKDNV SSLDDILNVL QKEENTRLAK KLYLNKDVLV KLSSLMDPFK RSKLDYKIQN
ISRLASDESV NPLDRALTSL KKFNRMSESE VITPTNICED MVNLFPEDGL REIVNNKNKL
LDIASKSGEY TVAIYKRLVD DLGFSHNEVS DIIYSIPTSS IAYEFTRRFY EILNLNVDNI
ATKFNSYDLI KITSENNEVD YKKVSNLLKQ NKKFSYIELT DEIKAGEETV NFGAIVGNPP
YQVSDNNSGT GSAKPIYNKF SMISFYLKPK FATLIVPSVW FSGGKGLDEF REYMLGLKGL
KQITNFITPQ DIFSNVNLRG GINYFLYQDK YDSDNNGIRI INIKDKKIIN NQLREKRIKN
LEIFISDNIA FNIVYRMVNN GGVQLNENSE NMLIKYISVR NPFGFNTKFI TTDLFKNNEK
EITNPVKIYA SKGKIGYVEK DLIKKNFNWI NKWKVITPFA NNIGKDLQDD NLNTIISEPN
SIVTETYLVI GGDLNLDKSS SMNIEKYLKT KFTRFLISIA KANQNGTKIT YRFVPIQDFS
DKSDIDWSKS IKEIDEQLFD KYELTSTERE HIRSSIKEM
//
