ID MTH5_HAEIN Reviewed; 304 AA. AC P45000; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Type II methyltransferase M.HindV {ECO:0000303|PubMed:12654995}; DE Short=M.HindV {ECO:0000303|PubMed:12654995}; DE EC=2.1.1.37; DE AltName: Full=Cytosine-specific methyltransferase HindV; DE AltName: Full=Modification methylase HindV; GN Name=hindVM; OrderedLocusNames=HI_1041; 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. 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 methylase, recognizes the double-stranded sequence 5'- CC GRCGYC-3', methylates C-? on both strands, and protects the DNA from CC cleavage by the HindV endonuclease. {ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5- CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018}; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE- CC ProRule:PRU01016}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC22700.1; -; Genomic_DNA. DR PIR; C64109; C64109. DR RefSeq; NP_439200.1; NC_000907.1. DR AlphaFoldDB; P45000; -. DR SMR; P45000; -. DR STRING; 71421.HI_1041; -. DR REBASE; 3574; M.HindV. DR EnsemblBacteria; AAC22700; AAC22700; HI_1041. DR KEGG; hin:HI_1041; -. DR PATRIC; fig|71421.8.peg.1085; -. DR eggNOG; COG0270; Bacteria. DR HOGENOM; CLU_006958_2_1_6; -. DR OrthoDB; 9813719at2; -. DR PhylomeDB; P45000; -. DR BioCyc; HINF71421:G1GJ1-1080-MONOMER; -. DR PRO; PR:P45000; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR CDD; cd00315; Cyt_C5_DNA_methylase; 1. DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 2. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00675; dcm; 1. DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1. DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1. DR Pfam; PF00145; DNA_methylase; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS00095; C5_MTASE_2; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 3: Inferred from homology; KW DNA-binding; Methyltransferase; Reference proteome; Restriction system; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..304 FT /note="Type II methyltransferase M.HindV" FT /id="PRO_0000087881" FT DOMAIN 1..299 FT /note="SAM-dependent MTase C5-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT ACT_SITE 75 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016, FT ECO:0000255|PROSITE-ProRule:PRU10018" SQ SEQUENCE 304 AA; 34366 MW; 03DA1EAB27C84BBD CRC64; MKCVDLFSGC GGLSLGFELA GFEICAAFEN WEKAIEIYKN NFSHPIYNID LRNEKEAVEK IKKYSPDLIM GGPPCQDFSS AGKRDISLGR ADLTYSFANI VCNIRPKWFV MENVEQIKKS HILQDIINQF IDFGYGLTSA ILDASYCGVP QSRTRFSLIG KLNSEHNFLI PTLSRKLSDK PMTVRDYLGN SLNLEFYYRH PRNYNRRGIF SIDEPSPTIR GVNRPIPKGY NINSCDPKGV ELAKVRPLTT IERSYIQTFP KSFLFSGTKT DLEQMIGNAV PVNLAKFVAS AIINFEKEPI RSMG //