ID F0IGQ4_9FLAO Unreviewed; 1151 AA.
AC F0IGQ4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=HMPREF9071_1751 {ECO:0000313|EMBL:EGD33589.1};
OS Capnocytophaga sp. oral taxon 338 str. F0234.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=888059 {ECO:0000313|EMBL:EGD33589.1, ECO:0000313|Proteomes:UP000003023};
RN [1] {ECO:0000313|EMBL:EGD33589.1, ECO:0000313|Proteomes:UP000003023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0234 {ECO:0000313|EMBL:EGD33589.1,
RC ECO:0000313|Proteomes:UP000003023};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001279};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD33589.1}.
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DR EMBL; AEXX01000043; EGD33589.1; -; Genomic_DNA.
DR RefSeq; WP_009746193.1; NZ_GL872413.1.
DR AlphaFoldDB; F0IGQ4; -.
DR STRING; 888059.HMPREF9071_1751; -.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_002539_1_1_10; -.
DR Proteomes; UP000003023; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:EGD33589.1};
KW Hydrolase {ECO:0000313|EMBL:EGD33589.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:EGD33589.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003023};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 716..836
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 936..1107
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 1151 AA; 133792 MW; EE8B09498CB455CD CRC64;
MENIIHTFKS GNLFEATTFF FKHLNISTQT FEEQAFLPQD FLKNLYKPEK HKVINEIYLV
GMVTDEVFSG KSLAEIDNEL SYDYQGLLII AVDLEDKTAT RTELSTLTRL FNRRFNAMPV
AVLFRYGNHI ALANAERTEY KQAFREGEKI GKVSILKDID TLNPHRGHLD ILETLKIPAK
IKTFKDLYKH WQEVFNVSTL NKKFYNELFA WYQWTISEEV GVTYPNDTQT DQDDRVQLEE
QIIRLITRVL FVWFIKQKQL VPNKLFEEDS LNQLLKDFKP TSLSEGSYYN AILQNLFFAT
LNKKVTERAF AKAKNTRDVK TLYRYEEMFN CSEEEVIKLF APIPFLNGGL FECLDKDKGN
DGVRYHLDGF SRNDRRSQAN GHYTHRAFIP NAVFFDKEKG LFPLLNRYHF TIEENSPNDV
QVALDPELLG NVFENLLGAF NPETKESARK QSGSFYTPKE VVHYMVDESL KAYLKNHLPQ
LTYENLEELF EENGQLTTLW STPLRTEVAQ YLRKVKILDP ACGSGAFPMG ILSRMVQLLE
KLNTNEETSL YDLKLHLIEN CIYGVDIQNI ASQISKLRFF ISLIVEQKES NTDAENNYGV
HTLPNLETKF ITANTLISIR EKKASYGSLF DIAISEIREA LIEIRKAHFY AKNPYQKKQL
REKDEALREV LAQKLEEFGQ ASSDNAKEFV HWNPYDQNAS ASFFDPEWMF GISDGFDIVI
GNPPYFSLTT DSPEKDKRTG TPIKHNTLYE KQGYETFART GDIYCLFYEK AHQLLKQGGI
CNFITSNKWM RTGYGQATRK FFLEHTNPLI LVDFAGIKVF ETATVDVNIL LYVKEKPTFN
TWACTIKDNE LKKLSLYVRQ HGGKTTFSSD ESWVILSEIE QRIKAKIEAI GTPLKEWNIS
INYGIKTGFN DAFIINGEKR AELIAQDPKS AEIIRPILRG RDIKRYGYEF ADLYLLFIPW
HFPLHQRTPE IKGASKEAEK AFENQYPAIY NHLLQYKEEL SNRNKAETGI RYEWYALQRW
GANYWEDFYK QKIVYPETTQ GAYFALDTNK VMLDKTCFMI ISDKPKFLIA LLSSRLYEFS
YKSIFSSIEL GVSGYQYNKH ALIRLPIIEP SQEIEQEIIT LLDQKEYSKI DTLVYKLYNL
SEEEIIFIES I
//
