MTHD_HAEIN
ID MTHD_HAEIN Reviewed; 518 AA.
AC P44414;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Type II methyltransferase M.HindII {ECO:0000303|PubMed:12654995};
DE Short=M.HindII {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase HindII;
DE AltName: Full=Modification methylase HindII;
GN Name=hindIIM; OrderedLocusNames=HI_0513;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NOMENCLATURE, AND SUBTYPE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: A gamma subtype methylase, recognizes the double-stranded
CC sequence 5'-GTYRAC-3', methylates A-5 on both strands, and protects the
CC DNA from cleavage by the HindII endonuclease.
CC {ECO:0000303|PubMed:12654995}.
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22171.1; -; Genomic_DNA.
DR PIR; F64073; F64073.
DR RefSeq; NP_438671.1; NC_000907.1.
DR RefSeq; WP_010868995.1; NC_000907.1.
DR AlphaFoldDB; P44414; -.
DR SMR; P44414; -.
DR STRING; 71421.HI_0513; -.
DR REBASE; 3427; M.HindII.
DR EnsemblBacteria; AAC22171; AAC22171; HI_0513.
DR KEGG; hin:HI_0513; -.
DR PATRIC; fig|71421.8.peg.532; -.
DR eggNOG; COG0827; Bacteria.
DR HOGENOM; CLU_508657_0_0_6; -.
DR PhylomeDB; P44414; -.
DR BioCyc; HINF71421:G1GJ1-526-MON; -.
DR PRO; PR:P44414; -.
DR Proteomes; UP000000579; 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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; RM_methylase_Eco57I-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..518
FT /note="Type II methyltransferase M.HindII"
FT /id="PRO_0000087974"
SQ SEQUENCE 518 AA; 60410 MW; 2E0CAA5B9DBF2EF6 CRC64;
MDESKKISLG QFFTPTHIVK YMIGLMTKNK NASILEPSSG NGVFLDSLIQ LGYTNLTSYE
IDGDIISHPF VINSSFITSY DKPQYDSIIG NPPYVRWKNL SELQKKELKD NSIWKMYCNS
LCDYFYIFII KSILQLKVGG ELIFICPDYF FSTKNAEGLR KFLINNGSFE KIILFNESKV
FHGVSSSVVI FKYIKGKNID NINIINIDSK SPIKSEDIES LGESYYIPRF SSSDVWVTSP
NHIKVALDKF ESYCKTIKKV QPKSLFDDLE FSRIGSVCDI GNGMVSGLDK AFQMNDINYS
ELELLNSICV AKAKHLDAFC FSGYTRYKFI LDDINEDKLI TYFPNFFYEF NNYKDYLLKR
YSYNKYLPYW KWAFLRNFSL FSKNEKKIFV PCKERISKKS NFRFSLVDEF IYPTQDVTAL
YKKENVKESI EYITAYLNSK AVFLWMKYKG VVKGNVVEFS EKPLANIPFR RIDWQLKSEK
KIHDDITNLV RKYLSNKEFS ILHEINLNLE KLGIKVEI
