T3MH_HAEIN
ID T3MH_HAEIN Reviewed; 747 AA.
AC P71366; P44106;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable type III restriction-modification enzyme HindVI Mod subunit {ECO:0000303|PubMed:12654995};
DE Short=M.HindVI;
DE EC=2.1.1.72;
DE AltName: Full=Probable HindVI methyltransferase;
DE AltName: Full=Probable type III methyltransferase M.HindVI {ECO:0000303|PubMed:12654995};
GN Name=mod {ECO:0000303|PubMed:12654995}; OrderedLocusNames=HI_1058/HI_1056;
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 beta subtype methylase that binds the system-specific DNA
CC recognition site 5'-CGAAT-3' and methylates A-4 (of only 1 strand). DNA
CC restriction requires both the Res and Mod subunits.
CC {ECO:0000250|UniProtKB:P08763, 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 -!- SUBUNIT: Homodimer, also forms a functional restriction-competent
CC complex with Res. {ECO:0000250|UniProtKB:P12364}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC22721.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC22722.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC22722.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L42023; AAC22721.1; ALT_FRAME; Genomic_DNA.
DR PIR; C64180; C64180.
DR PIR; G64019; G64019.
DR RefSeq; NP_439215.1; NC_000907.1.
DR AlphaFoldDB; P71366; -.
DR STRING; 71421.HI_1056; -.
DR REBASE; 177015; M.Mph27ORF4193P.
DR PRIDE; P71366; -.
DR EnsemblBacteria; AAC22721; AAC22721; HI_1056.
DR EnsemblBacteria; AAC22722; AAC22722; HI_1058.
DR KEGG; hin:HI_1056; -.
DR KEGG; hin:HI_1058; -.
DR PATRIC; fig|71421.8.peg.1101; -.
DR eggNOG; COG2189; Bacteria.
DR HOGENOM; CLU_097494_1_0_6; -.
DR OMA; GGISKKC; -.
DR PhylomeDB; P71366; -.
DR BioCyc; HINF71421:G1GJ1-1094-MON; -.
DR BioCyc; HINF71421:G1GJ1-1095-MON; -.
DR PRO; PR:P71366; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
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; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR022221; TypeIII_RM_meth.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF12564; TypeIII_RM_meth; 1.
DR PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
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..747
FT /note="Probable type III restriction-modification enzyme
FT HindVI Mod subunit"
FT /id="PRO_0000088033"
FT REGION 267..270
FT /note="Binding of S-adenosyl methionine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 747 AA; 85590 MW; 996A1924DF53957D CRC64;
MKTDIQTELT QALLSHEKVW ANEEKTILAK NILLDLVEKT DPTIIGLLLG NDDLKRHFFV
EVNGVLVFKL QDFRFFLDKH SINNSYTKYA NRIGLTDGNR FLKDSSDIVL DFPFKDCVLN
GGQSTEEGEE IYFKRNNSQS VSQSVSQSVS QSVSQSVSQS VSQSVSQSVS QSVSQSVSQL
YTKLTRKRQE IFFNQTLAFD EIDRLFDAKA FSKFSRYTAD GKQAVGEIKR HSDGTPAENL
IIKGNNLIAL HSLAKQFKGK VKLIYIDPPY NTGNDGFKYN DKFNHSTWLT FMKNRLEIAK
TLLADDGVIF VQCDDIEQAY LKILMDDIFD RDNFLNIVTV KTKIGGVSGS SEGKSLKDST
EFINVFSKNR ERLFLNPVYQ KTEVNEFIKN YEDSGKSWKY TQVLIDLGEK ILLEEKDGFK
YYHYPNAQMT SIVKFSQDQN LSKEIIYTEY SHKVYRTTNA QSSIRSKIIE DLYSIKNGIV
SIEYIPQKGK NAGNLIEVFY NASNKDMFMF LSDMLIKEKN KYFYLQKVNT LWDDIQYNNL
NKEGGYIDFK NGKKPEALLR RIIDMTTKEG DIVLDYHLGS GTTAAVAHKM NRQYIGIEQM
DYIETLAVER LKKVIDGEQG GISKAVNWQG GGEFVYAELA PFNETAKQQI LACEDSDDIK
TLFEDLCERY FLKYNVSVKE FSQIIEEPEF QSLPLDEQKQ MVLEMLDLNQ MYVSLSEMDD
EQFAGCLNDD DKALSRAFYQ AEKKDGE
