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   27-MAR-2024, entry version 131.
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};
GN   OrderedLocusNames=HI_1058/HI_1056;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; 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   RefSeq; NP_439216.1; NC_000907.1.
DR   AlphaFoldDB; P71366; -.
DR   STRING; 71421.HI_1056; -.
DR   REBASE; 177015; M.Mph27ORF4193P.
DR   REBASE; 203794; M.Ppe892ORF72P.
DR   REBASE; 204714; M.Bso1395ORF3709P.
DR   REBASE; 3701; M.HindVI.
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   OrthoDB; 5677619at2; -.
DR   PhylomeDB; P71366; -.
DR   BioCyc; HINF71421:G1GJ1-1094-MONOMER; -.
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; Vaccinia Virus protein VP39; 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   PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
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; S-adenosyl-L-methionine-dependent methyltransferases; 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
//