ID A4P099_HAEIF Unreviewed; 658 AA.
AC A4P099;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=CGSHiR3021_00797 {ECO:0000313|EMBL:EDK13164.1};
OS Haemophilus influenzae 22.4-21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=375063 {ECO:0000313|EMBL:EDK13164.1, ECO:0000313|Proteomes:UP000005596};
RN [1] {ECO:0000313|EMBL:EDK13164.1, ECO:0000313|Proteomes:UP000005596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22.4-21 {ECO:0000313|EMBL:EDK13164.1,
RC ECO:0000313|Proteomes:UP000005596};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; AAZJ01000013; EDK13164.1; -; Genomic_DNA.
DR AlphaFoldDB; A4P099; -.
DR BioCyc; HINF375063:G119K-1901-MONOMER; -.
DR Proteomes; UP000005596; 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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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:EDK13164.1};
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:EDK13164.1}.
FT DOMAIN 42..365
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 658 AA; 74803 MW; BCA4F53CFA238D64 CRC64;
MSHKNVLLSV LEKFVSPYIN LTPKEQQDPE GNKLPVLTNL GMGYVFEELI RKFNEENNEE
AGEHFTPREV IELMTHLVFD PLKSQIPAII TIYDPACGSG GMLTESQNFI EQKYPLSESQ
GERSIFLFGK ETNDETYAIC KSDMMIKGDN PENIKVGSTL ATDSFQGNHF DFMLSNPPYG
KSWSKDQAYI KDGNEVIDSR FKVTLPDYWG NVETLDATPR SSDGQLLFLM EMVNKMKSPK
NNKIGSRVAS VHNGSSLFTG DAGSGESNIR RHIIENDLLE AIVQLPNNLF YNTGITTYIW
LLSNNKSEAR KGKVQLIDAS LLFRKLRKNL GDKNCEFAPE HIAEITQNYL DFTAKAREID
SQNEEVGLAS QIFDNQDFGY YKVTIERPDR RSAQFTAENI EPLRFDKALF EPMQYLYRQY
GGQVYNAGFL AQTEQEITAW CEAQGIALNN KNKAKLLDVK TWEKAAALFQ TASKLLKHFG
EQQFHDFNQF KQAVECRLKA EKIPLSATEK KAVFNAVSWY NENAAKVIAK TLKLKPNELD
ALCQRYQCQA DGLADFGYYA TGKAGEYIQY ETSSDLRDSE SIPLKQNIHD YFKAEVQPHI
SEAWLNMESV KIGYEISFNK YFYRHKPLRS LAEVAQDILA LEKQADGLIS EILGEIYE
//
