ID F9ZLE1_ACICS Unreviewed; 1253 AA.
AC F9ZLE1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=Atc_1161 {ECO:0000313|EMBL:AEK57810.1};
OS Acidithiobacillus caldus (strain SM-1).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK57810.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK57810.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK57810.1,
RC ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(2011).
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 type-I restriction system S methylase
CC family. {ECO:0000256|ARBA:ARBA00010923}.
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DR EMBL; CP002573; AEK57810.1; -; Genomic_DNA.
DR RefSeq; WP_014002682.1; NC_015850.1.
DR AlphaFoldDB; F9ZLE1; -.
DR STRING; 990288.Atc_1161; -.
DR REBASE; 38158; AcaSM1ORF1161P.
DR GeneID; 69614416; -.
DR KEGG; acu:Atc_1161; -.
DR HOGENOM; CLU_003347_0_0_6; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000006135; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd17524; RMtype1_S_EcoUTORF5051P-TRD2-CR2_like; 1.
DR CDD; cd17291; RMtype1_S_MgeORF438P-TRD-CR_like; 1.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 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; IPR029464; HSDR_N.
DR InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30408:SF12; TYPE I RESTRICTION ENZYME MJAVIII SPECIFICITY SUBUNIT; 1.
DR PANTHER; PTHR30408; TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN; 1.
DR Pfam; PF13588; HSDR_N_2; 1.
DR Pfam; PF01420; Methylase_S; 2.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000006135};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 70..146
FT /note="Type I restriction enzyme R protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13588"
FT DOMAIN 401..654
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 892..1021
FT /note="Type I restriction modification DNA specificity"
FT /evidence="ECO:0000259|Pfam:PF01420"
FT DOMAIN 1110..1232
FT /note="Type I restriction modification DNA specificity"
FT /evidence="ECO:0000259|Pfam:PF01420"
FT COILED 1217..1244
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1253 AA; 141823 MW; ACE12A3B975970A4 CRC64;
MLTQDNLADL LNALGFEKKG AIHRKLFGSA MLEVNFTKKE IHYPEEAGLI INERQTCNFD
ANENFVVLEC VHRLLEKGYK PEHIELEPKW KLGRGASGGR ADILVKDNEA RPLLIIECKT
AGTEFKRAWN KTLQDGDQLF SYAQQISETR FLCLYTSDLD AGTVNYTSHI IAHRDNDKYL
ADNPLFKSFK SATDVKDRYA VWRDTYKLDY TTKGIFEENI QPYHIGKDKY SVADLHTISA
SDQQKKYHEF ATILRQHNVS GRENAFDKLV NLFLCKLVDE IENPSDLKFY WKGVAYDTHF
DLMDRLQQLY QAGMGKFLGE DITYIHQGDV INALRFIKQN PDATQRAVWN LFIQQKFFTN
NDFSFIDVHN ERLFYQNAEV LLKTLQMWQD IRLTDPHGHN QFLGDMFEGF LDQGIKQSEG
QFFTPMPICR FILMSLPLAS LVQRRATPPK AIDYACGAGH FLTELALQLK PLVETHQPEA
DLATYHKALY GIEKEYRLSK VAKVSAFMYG QQGINICYGD GLIKRHEAFP EIQDGSFDLL
VANPPYSVRG FLETLPEEER KAYTLTETIN DLETSNSIET FFIERAKQLL RADGVAAIIL
PSSILSNGGA TYIRAREILL QYFDIVAIAE FGSGTFGKTG TNTVTLFLRR KQIQPDTAEH
YRERVDEWFK GCDASKRKQV IYKDEHLIAR YAAHIHVPLD DYKTLLKGDL EGPWINHLEK
IYLDKFNNST EISSLYRTRW FNALTPEEQD AELDKRFLAF VQSIERDKLY HFVMACDQPN
PVLIIRSPTE TKAIKQFLGY DWSSAKGDEG IKLIKDANGR HLTPLYDETN RDNTGKLNFS
IAANFNGTLT DIPAGLEGVA RMAPLVDMLD FSRAVFEKQI NLAIRGSTKF VSKWPISPLG
SIAEIRKGTS ITQKKAVPGI YKVIAGGMTH AYTHNTFNRP ANTITISASG ASAGYVAFWR
EPIFASDCTT VRGANDEHTE YLYHVLKSRQ GEIQAASSGA AQPHVYPKDL ETLPIPQPDQ
TTLRNIVSEC RSVDDAVNSS RDTLENTLAR IDAEVAEIYR SSAEHSEIDK LAIKIQYGLN
EAMNEGGVGY KIFRMNEIIR GRMVDNGSMK CADISAAEFA KYRLNKGDLL FNRTNSIEHV
GKTGLFDLDG DYCFASYLVR VVPDTGKVLP KFLEKMMNSS AFQTEAKGKA SRSINQANIN
ATVMRNIKVP VPSLAEQKEF VAKIEALEKQ IAEAQAVIDT AAARKRAILQ KYL
//
