MTB1_HERAU
ID MTB1_HERAU Reviewed; 437 AA.
AC P25262;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Type II methyltransferase M.HgiBI {ECO:0000303|PubMed:12654995};
DE Short=M.HgiBI {ECO:0000303|PubMed:7607523};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase HgiBI;
DE AltName: Full=Modification methylase HgiBI;
GN Name=hgiBIM {ECO:0000303|PubMed:7607523};
OS Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=65;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HPG5;
RX PubMed=2062638; DOI=10.1093/nar/19.12.3207;
RA Duesterhoeft A., Erdmann D., Kroeger M.;
RT "Isolation and genetic structure of the AvaII isoschizomeric restriction-
RT modification system HgiBI from Herpetosiphon giganteus Hpg5: M.HgiBI
RT reveals high homology to M.BanI.";
RL Nucleic Acids Res. 19:3207-3211(1991).
RN [2]
RP DISCUSSION OF SEQUENCE, AND FUNCTION.
RX PubMed=7607523; DOI=10.1016/0378-1119(94)00779-r;
RA Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S.,
RA Meyer-Rogge S., Moestl D.;
RT "Organization and gene expression within restriction-modification systems
RT of Herpetosiphon giganteus.";
RL Gene 157:43-47(1995).
RN [3]
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 that recognizes the double-stranded sequence 5'-
CC GGWCC-3', methylates C-? on both strands, and protects the DNA from
CC cleavage by the HgiBI endonuclease (PubMed:12654995). This system is
CC less active than isoschizomeric RM.HgiEI (PubMed:7607523).
CC {ECO:0000269|PubMed:7607523, 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}.
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DR EMBL; X55137; CAA38927.1; -; Genomic_DNA.
DR PIR; S22307; S22307.
DR AlphaFoldDB; P25262; -.
DR SMR; P25262; -.
DR REBASE; 203803; M.Keu1446ORF816P.
DR REBASE; 233067; M.SpaF3KORF1926P.
DR REBASE; 256744; M.Ssp9304ORF2562P.
DR REBASE; 3414; M.HgiBI.
DR PRO; PR:P25262; -.
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 Gene3D; 3.40.50.150; -; 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 Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 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; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..437
FT /note="Type II methyltransferase M.HgiBI"
FT /id="PRO_0000087885"
FT DOMAIN 4..431
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 437 AA; 49627 MW; 70A658159D8D23AD CRC64;
MQQFRFIDLF AGIGGFRLGL EAVGGVCVAS AEIDQQAIKV YRQNWPTDGV DHNLGDITAI
QQLPAHDVLV GGVPCQPWSI AGKNQAFDDP RGQLWADVIR LVQINQPKAF IFENVKGLVD
PRNRLCLEII LDSFKDLGYS VFYKLLNSFD FGVAQNRDRV FIVGIQQKLD LNGFSFPEYT
ESEQRLYHIL DNLEVPETKL ESIPIQRNLF GERIDVGYNK LTPRGAFNDF FILNDIRNGP
TSIHSWEIYP TTEREKQICM IIMRNRRNSR YGDCDGNPMS YQDIAELVAG LAEKELQTLV
EKRILRQYPD GKYEFFNRRL SGGIDGTYRI FLPNARFFGT LTARGMHDEI AEISVSGANA
EEYKHNFIQQ VLIPKRYRKI TVSEAARLQG FPGSFQFHSN QSANFRLIGN SVAPPVIVAL
GKALQCVKLF EQELCEV
